Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Collagen alpha-1(II) chain (Alpha-1 type II collagen) [Cleaved into: Collagen alpha-1(II) chain; Chondrocalcin]

 CO2A1_HUMAN             Reviewed;        1487 AA.
P02458; A6NGA0; Q12985; Q14009; Q14044; Q14045; Q14046; Q14047;
Q14056; Q14058; Q16672; Q1JQ82; Q2V4X7; Q6LBY1; Q6LBY2; Q6LBY3;
Q96IT5; Q99227; Q9UE38; Q9UE39; Q9UE40; Q9UE41; Q9UE42; Q9UE43;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
22-NOV-2017, entry version 215.
RecName: Full=Collagen alpha-1(II) chain {ECO:0000305};
AltName: Full=Alpha-1 type II collagen {ECO:0000305};
Contains:
RecName: Full=Collagen alpha-1(II) chain {ECO:0000305};
Contains:
RecName: Full=Chondrocalcin {ECO:0000303|PubMed:3800925};
Flags: Precursor;
Name=COL2A1 {ECO:0000312|HGNC:HGNC:2200};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS SER-9 AND
LEU-158.
PubMed=2587267; DOI=10.1093/nar/17.22.9473;
Su M.W., Lee B., Ramirez F., Machado M.A., Horton W.A.;
"Nucleotide sequence of the full length cDNA encoding for human type
II procollagen.";
Nucleic Acids Res. 17:9473-9473(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2), AND VARIANT SER-9.
TISSUE=Blood;
PubMed=8948452; DOI=10.1042/bj3080923;
Ala-Kokko L., Kvist A.-P., Metsaranta M., Kivirikko K.I.,
de Crombrugghe B., Prockop D.J., Vuorio E.;
"Conservation of the sizes of 53 introns and over 100 intronic
sequences for the binding of common transcription factors in the human
and mouse genes for type II procollagen (COL2A1).";
Biochem. J. 308:923-929(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 1109-1487 (ISOFORMS 1/2).
TISSUE=Embryonic stem cell, and Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-1229 (ISOFORM 1), AND VARIANT SER-9.
PubMed=2803268; DOI=10.1042/bj2620521;
Baldwin C.T., Reginato A.M., Smith C., Jimenez S.A., Prockop D.J.;
"Structure of cDNA clones coding for human type II procollagen. The
alpha 1(II) chain is more similar to the alpha 1(I) chain than two
other alpha chains of fibrillar collagens.";
Biochem. J. 262:521-528(1989).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-236 (ISOFORM 1), AND VARIANT
SER-9.
PubMed=2714801; DOI=10.1016/0888-7543(89)90353-4;
Su M.W., Benson-Chanda V., Vissing H., Ramirez F.;
"Organization of the exons coding for pro alpha 1(II) collagen N-
propeptide confirms a distinct evolutionary history of this domain of
the fibrillar collagen genes.";
Genomics 4:438-441(1989).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-103 (ISOFORM 2), AND VARIANT
SER-9.
PubMed=2081599; DOI=10.1016/0888-7543(90)90224-I;
Ryan M.C., Sieraski M., Sandell L.J.;
"The human type II procollagen gene: identification of an additional
protein-coding domain and location of potential regulatory sequences
in the promoter and first intron.";
Genomics 8:41-48(1990).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28 (ISOFORMS 1/2).
PubMed=3021582; DOI=10.1016/0378-1119(86)90037-5;
Nunez A.M., Kohno K., Martin G.R., Yamada Y.;
"Promoter region of the human pro-alpha 1(II)-collagen gene.";
Gene 44:11-16(1986).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28 (ISOFORMS 1/2).
PubMed=1637314; DOI=10.1042/bj2850287;
Vikkula M., Metsaranta M., Syvaenen A.-C., Ala-Kokko L., Vuorio E.,
Peltonen L.;
"Structural analysis of the regulatory elements of the type-II
procollagen gene. Conservation of promoter and first intron sequences
between human and mouse.";
Biochem. J. 285:287-294(1992).
[11]
NUCLEOTIDE SEQUENCE OF 27-103 (ISOFORM 2), AND TISSUE SPECIFICITY.
PubMed=2355003;
Ryan M.C., Sandell L.J.;
"Differential expression of a cysteine-rich domain in the amino-
terminal propeptide of type II (cartilage) procollagen by alternative
splicing of mRNA.";
J. Biol. Chem. 265:10334-10339(1990).
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 99-341 (ISOFORMS 1/2).
TISSUE=Fetal sternum;
PubMed=1999183; DOI=10.1111/j.1432-1033.1991.tb15742.x;
Huang M.C., Seyer J.M., Thompson J.P., Spinella D.G., Cheah K.S.,
Kang A.H.;
"Genomic organization of the human procollagen alpha 1(II) collagen
gene.";
Eur. J. Biochem. 195:593-600(1991).
[13]
PROTEIN SEQUENCE OF 188-195 AND 1224-1236.
PubMed=8660302; DOI=10.1042/bj3140327;
Diab M., Wu J.J., Eyre D.R.;
"Collagen type IX from human cartilage: a structural profile of
intermolecular cross-linking sites.";
Biochem. J. 314:327-332(1996).
[14]
PROTEIN SEQUENCE OF 243-261; 575-590 AND 756-779.
PubMed=8529631; DOI=10.1111/j.1432-1033.1995.125_c.x;
Franc S., Marzin E., Boutillon M.-M., Lafont R.,
Lechene de la Porte P., Herbage D.;
"Immunohistochemical and biochemical analyses of 20,000-25,000-year-
old fossil cartilage.";
Eur. J. Biochem. 234:125-131(1995).
[15]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 440-509 (ISOFORMS 1/2).
PubMed=7847372;
Tiller G.E., Weis M.A., Polumbo P.A., Gruber H.E., Rimoin D.L.,
Cohn D.H., Eyre D.R.;
"An RNA-splicing mutation (G+5IVS20) in the type II collagen gene
(COL2A1) in a family with spondyloepiphyseal dysplasia congenita.";
Am. J. Hum. Genet. 56:388-395(1995).
[16]
NUCLEOTIDE SEQUENCE [MRNA] OF 501-1214 (ISOFORMS 1/2).
Ramirez F.;
Submitted (DEC-1988) to the EMBL/GenBank/DDBJ databases.
[17]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 541-578; 784-803; 1056-1109 AND
1200-1487 (ISOFORMS 1/2).
PubMed=2987845; DOI=10.1093/nar/13.7.2207;
Sangiorgi F.O., Benson-Chanda V., de Wet W.J., Sobel M.E.,
Tsipouras P., Ramirez F.;
"Isolation and partial characterization of the entire human pro alpha
1(II) collagen gene.";
Nucleic Acids Res. 13:2207-2225(1985).
[18]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 630-785 (ISOFORMS 1/2).
PubMed=2753125; DOI=10.1016/0014-5793(89)80713-6;
Vikkula M., Peltonen L.;
"Structural analyses of the polymorphic area in type II collagen
gene.";
FEBS Lett. 250:171-174(1989).
[19]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1032-1487 (ISOFORMS 1/2).
PubMed=3857598; DOI=10.1073/pnas.82.9.2555;
Cheah K.S.E., Stoker N.G., Griffin J.R., Grosveld F.G., Solomon E.;
"Identification and characterization of the human type II collagen
gene (COL2A1).";
Proc. Natl. Acad. Sci. U.S.A. 82:2555-2559(1985).
[20]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1038-1055 (ISOFORMS 1/2), AND
VARIANT HYPOCHONDROGENESIS GLU-1053.
PubMed=1429602;
Bogaert R., Tiller G.E., Wies M.A., Gruber H.E., Rimoin D.L.,
Cohn D.H., Eyre D.R.;
"An amino acid substitution (Gly853-->Glu) in the collagen alpha 1(II)
chain produces hypochondrogenesis.";
J. Biol. Chem. 267:22522-22526(1992).
[21]
NUCLEOTIDE SEQUENCE [MRNA] OF 1082-1288 (ISOFORMS 1/2).
PubMed=1905723;
Chan D., Cole W.G.;
"Low basal transcription of genes for tissue-specific collagens by
fibroblasts and lymphoblastoid cells. Application to the
characterization of a glycine 997 to serine substitution in alpha
1(II) collagen chains of a patient with spondyloepiphyseal
dysplasia.";
J. Biol. Chem. 266:12487-12494(1991).
[22]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1146-1199 (ISOFORMS 1/2), AND
VARIANT SEDC 1164-GLY--TYR-1399 DEL.
PubMed=2543071; DOI=10.1126/science.2543071;
Lee B., Vissing H., Ramirez F., Rogers D., Rimoin D.L.;
"Identification of the molecular defect in a family with
spondyloepiphyseal dysplasia.";
Science 244:978-980(1989).
[23]
NUCLEOTIDE SEQUENCE OF 1164-1199 (ISOFORMS 1/2), AND VARIANT SEDC
GLY-PRO-SER-GLY-LYS-ASP-GLY-ALA-ASN-GLY-ILE-PRO-GLY-PRO-ILE-1184 INS.
PubMed=2339128; DOI=10.1073/pnas.87.10.3889;
Tiller G.E., Rimoin D.L., Murray L.W., Cohn D.H.;
"Tandem duplication within a type II collagen gene (COL2A1) exon in an
individual with spondyloepiphyseal dysplasia.";
Proc. Natl. Acad. Sci. U.S.A. 87:3889-3893(1990).
[24]
NUCLEOTIDE SEQUENCE [MRNA] OF 1175-1487 (ISOFORMS 1/2).
PubMed=2825137; DOI=10.1093/nar/15.22.9499;
Elima K., Vuorio T., Vuorio E.;
"Determination of the single polyadenylation site of the human pro
alpha 1(II) collagen gene.";
Nucleic Acids Res. 15:9499-9504(1987).
[25]
NUCLEOTIDE SEQUENCE [MRNA] OF 1189-1467 (ISOFORMS 1/2).
PubMed=3840017; DOI=10.1042/bj2290183;
Elima K., Maekelae J.K., Vuorio T., Kauppinen S., Knowles J.,
Vuorio E.;
"Construction and identification of a cDNA clone for human type II
procollagen mRNA.";
Biochem. J. 229:183-188(1985).
[26]
PROTEIN SEQUENCE OF 1242-1265; 1295-1305 AND 1395-1408.
PubMed=3800925;
Van der Rest M., Rosenberg L.C., Olsen B.R., Poole A.R.;
"Chondrocalcin is identical with the C-propeptide of type II
procollagen.";
Biochem. J. 237:923-925(1986).
[27]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1245-1295 (ISOFORMS 1/2/3).
PubMed=6320112; DOI=10.1093/nar/12.2.1025;
Strom C.M., Upholt W.B.;
"Isolation and characterization of genomic clones corresponding to the
human type II procollagen gene.";
Nucleic Acids Res. 12:1025-1038(1984).
[28]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1296-1358 (ISOFORMS 1/2/3).
PubMed=3002437; DOI=10.1021/bi00344a004;
Nunez A.M., Francomano C., Young M.F., Martin G.R., Yamada Y.;
"Isolation and partial characterization of genomic clones coding for a
human pro-alpha 1 (II) collagen chain and demonstration of restriction
fragment length polymorphism at the 3' end of the gene.";
Biochemistry 24:6343-6348(1985).
[29]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1238-1247.
PubMed=9354468; DOI=10.1016/S1074-7613(00)80369-6;
Dessen A., Lawrence C.M., Cupo S., Zaller D.M., Wiley D.C.;
"X-ray crystal structure of HLA-DR4 (DRA*0101, DRB1*0401) complexed
with a peptide from human collagen II.";
Immunity 7:473-481(1997).
[30]
STRUCTURE BY NMR OF 25-162 (ISOFORM 2), AND DISULFIDE BONDS.
PubMed=15466413; DOI=10.1074/jbc.M409225200;
O'Leary J.M., Hamilton J.M., Deane C.M., Valeyev N.V., Sandell L.J.,
Downing A.K.;
"Solution structure and dynamics of a prototypical chordin-like
cysteine-rich repeat (von Willebrand Factor type C module) from
collagen IIA.";
J. Biol. Chem. 279:53857-53866(2004).
[31]
INVOLVEMENT IN SEDSTN, AND VARIANT SEDSTN ARG-207.
PubMed=26183434; DOI=10.1002/humu.22839;
Jurgens J., Sobreira N., Modaff P., Reiser C.A., Seo S.H., Seong M.W.,
Park S.S., Kim O.H., Cho T.J., Pauli R.M.;
"Novel COL2A1 variant (c.619G>A, p.Gly207Arg) manifesting as a
phenotype similar to progressive pseudorheumatoid dysplasia and
spondyloepiphyseal dysplasia, Stanescu type.";
Hum. Mutat. 36:1004-1008(2015).
[32]
REVIEW ON VARIANTS.
PubMed=2010058;
Kuivaniemi H., Tromp G., Prockop D.J.;
"Mutations in collagen genes: causes of rare and some common diseases
in humans.";
FASEB J. 5:2052-2060(1991).
[33]
REVIEW ON VARIANTS.
PubMed=9101290;
DOI=10.1002/(SICI)1098-1004(1997)9:4<300::AID-HUMU2>3.0.CO;2-9;
Kuivaniemi H., Tromp G., Prockop D.J.;
"Mutations in fibrillar collagens (types I, II, III, and XI), fibril-
associated collagen (type IX), and network-forming collagen (type X)
cause a spectrum of diseases of bone, cartilage, and blood vessels.";
Hum. Mutat. 9:300-315(1997).
[34]
VARIANT ACG2 SER-1143.
PubMed=2572591;
Vissing H., D'Alessio M., Lee B., Ramirez F., Godfrey M.,
Hollister D.W.;
"Glycine to serine substitution in the triple helical domain of pro-
alpha 1 (II) collagen results in a lethal perinatal form of short-
limbed dwarfism.";
J. Biol. Chem. 264:18265-18267(1989).
[35]
VARIANT OSCDP CYS-719.
PubMed=1975693; DOI=10.1073/pnas.87.17.6565;
Ala-Kokko L., Baldwin C.T., Moskowitz R.W., Prockop D.J.;
"Single base mutation in the type II procollagen gene (COL2A1) as a
cause of primary osteoarthritis associated with a mild
chondrodysplasia.";
Proc. Natl. Acad. Sci. U.S.A. 87:6565-6568(1990).
[36]
VARIANT OSCDP CYS-719.
PubMed=1985108; DOI=10.1172/JCI114994;
Eyre D.R., Weis M.A., Moskowitz R.W.;
"Cartilage expression of a type II collagen mutation in an inherited
form of osteoarthritis associated with a mild chondrodysplasia.";
J. Clin. Invest. 87:357-361(1991).
[37]
VARIANT HYPOCHONDROGENESIS SER-774.
PubMed=1374906; DOI=10.1073/pnas.89.10.4583;
Horton W.A., Machado M.A., Ellard J., Campbell D., Bartley J.,
Ramirez F., Vitale E., Lee B.;
"Characterization of a type II collagen gene (COL2A1) mutation
identified in cultured chondrocytes from human hypochondrogenesis.";
Proc. Natl. Acad. Sci. U.S.A. 89:4583-4587(1992).
[38]
VARIANT STL1O ASP-267.
PubMed=8317498;
Koerkkoe J., Ritvaniemi P., Haataja L., Kaeaeriaeinen H.,
Kivirikko K.I., Prockop D.J., Ala-Kokko L.;
"Mutation in type II procollagen (COL2A1) that substitutes aspartate
for glycine alpha 1-67 and that causes cataracts and retinal
detachment: evidence for molecular heterogeneity in the Wagner
syndrome and the Stickler syndrome (arthro-ophthalmopathy).";
Am. J. Hum. Genet. 53:55-61(1993).
[39]
VARIANTS SEMDSTWK VAL-897 AND CYS-909.
Tiller G.E., Weis M.A., Lachman R.S., Cohn D.H., Rimoin D.L.,
Eyre D.R.;
"A dominant mutation in the type II collagen gene (COL2A1) produces
spondyloepimetaphyseal dysplasia (SEMD), Strudwick type.";
Am. J. Hum. Genet. 53:A209-A209(1993).
[40]
VARIANT OSCDP CYS-719.
PubMed=8507190; DOI=10.1006/bbrc.1993.1539;
Holderbaum D., Malemud C.J., Moskowitz R.W., Haqqi T.M.;
"Human cartilage from late stage familial osteoarthritis transcribes
type II collagen mRNA encoding a cysteine in position 519.";
Biochem. Biophys. Res. Commun. 192:1169-1174(1993).
[41]
VARIANT SPONDYLOMETAPHYSEAL DYSPLASIA ARG-354.
PubMed=8486375; DOI=10.1006/geno.1993.1179;
Vikkula M., Ritvaniemi P., Vuorio A.F., Kaitila I., Ala-Kokko L.,
Peltonen L.;
"A mutation in the amino-terminal end of the triple helix of type II
collagen causing severe osteochondrodysplasia.";
Genomics 16:282-285(1993).
[42]
VARIANT CZECHD CYS-275.
PubMed=8244341; DOI=10.1007/BF00216458;
Williams C.J., Considine E.L., Knowlton R.G., Reginato A., Neumann G.,
Harrison D., Buxton P., Jimenez S.A., Prockop D.J.;
"Spondyloepiphyseal dysplasia and precocious osteoarthritis in a
family with an Arg75-->Cys mutation in the procollagen type II gene
(COL2A1).";
Hum. Genet. 92:499-505(1993).
[43]
VARIANT SEDC CYS-989.
PubMed=8325895;
Chan D., Taylor T.K.F., Cole W.G.;
"Characterization of an arginine 789 to cysteine substitution in alpha
1 (II) collagen chains of a patient with spondyloepiphyseal
dysplasia.";
J. Biol. Chem. 268:15238-15245(1993).
[44]
VARIANT SEDC SER-1197.
PubMed=8423604; DOI=10.1136/jmg.30.1.27;
Cole W.G., Hall R.K., Rogers J.G.;
"The clinical features of spondyloepiphyseal dysplasia congenita
resulting from the substitution of glycine 997 by serine in the alpha
1(II) chain of type II collagen.";
J. Med. Genet. 30:27-35(1993).
[45]
VARIANT STL1 302-ALA--LYS-308 DEL.
PubMed=7977371;
Bogaert R., Wilkin D.J., Wilcox W.R., Lachman R.S., Rimoin D.L.,
Cohn D.H., Eyre D.R.;
"Expression, in cartilage, of a 7-amino-acid deletion in type II
collagen from two unrelated individuals with Kniest dysplasia.";
Am. J. Hum. Genet. 55:1128-1136(1994).
[46]
VARIANT KD ASP-303.
PubMed=7874117; DOI=10.1093/hmg/3.11.1999;
Wilkin D.J., Bogaert R., Lachman R.S., Rimoin D.L., Eyres D.R.,
Cohn D.H.;
"A single amino acid substitution (G103D) in the type II collagen
triple helix produces Kniest dysplasia.";
Hum. Mol. Genet. 3:1999-2003(1994).
[47]
VARIANT SEDC SER-447.
PubMed=8019561; DOI=10.1002/humu.1380030314;
Ritvaniemi P., Sokolov B.P., Williams C.J., Considine W., Yurgenev L.,
Meerson E.M., Ala-Kokko L., Prockop D.J.;
"A single base mutation in the type II procollagen gene (COL2A1) that
converts glycine alpha 1-247 to serine in a family with late-onset
spondyloepiphyseal dysplasia.";
Hum. Mutat. 3:261-267(1994).
[48]
VARIANT ACG2 ARG-891.
PubMed=7757081; DOI=10.1093/hmg/4.2.285;
Mortier G.R., Wilkin D.J., Wilcox W.R., Rimoin D.L., Lachman R.S.,
Eyre D.R., Cohn D.H.;
"A radiographic, morphologic, biochemical and molecular analysis of a
case of achondrogenesis type II resulting from substitution for a
glycine residue (Gly691-->Arg) in the type II collagen trimer.";
Hum. Mol. Genet. 4:285-288(1995).
[49]
VARIANT CZECHD CYS-275, VARIANT SEDC SER-1176, VARIANT OSCDP CYS-719,
VARIANT HYPOCHONDROGENESIS ARG-891, AND VARIANT ACG2 ARG-1188.
PubMed=7757086; DOI=10.1093/hmg/4.2.309;
Williams C.J., Rock M., Considine E.L., McCarron S., Gow P., Ladda R.,
McLain D., Michels V.M., Murphy W., Prockop D.J., Ganguly A.;
"Three new point mutations in type II procollagen (COL2A1) and
identification of a fourth family with the COL2A1 Arg519-->Cys base
substitution using conformation sensitive gel electrophoresis.";
Hum. Mol. Genet. 4:309-312(1995).
[50]
VARIANT ACG2 SER-969.
PubMed=7829510; DOI=10.1074/jbc.270.44.26292;
Chan D., Cole W.G., Chow C.W., Mundlos S., Bateman J.F.;
"A COL2A1 mutation in achondrogenesis type II results in the
replacement of type II collagen by type I and III collagens in
cartilage.";
J. Biol. Chem. 270:1747-1753(1995).
[51]
VARIANTS SEMDSTWK VAL-492; CYS-504 AND CYS-909.
PubMed=7550321; DOI=10.1038/ng0995-87;
Tiller G.E., Polumbo P.A., Weis M.A., Bogaert R., Lachman R.S.,
Cohn D.H., Rimoin D.L., Eyre D.R.;
"Dominant mutations in the type II collagen gene, COL2A1, produce
spondyloepimetaphyseal dysplasia, Strudwick type.";
Nat. Genet. 11:87-89(1995).
[52]
VARIANT HYPOCHONDROGENESIS CYS-1113.
PubMed=8723098;
DOI=10.1002/(SICI)1096-8628(19960503)63:1<129::AID-AJMG23>3.0.CO;2-P;
Mundlos S., Chan D., McGill J., Bateman J.F.;
"An alpha 1(II) Gly913 to Cys substitution prevents the matrix
incorporation of type II collagen which is replaced with type I and
III collagens in cartilage from a patient with hypochondrogenesis.";
Am. J. Med. Genet. 63:129-136(1996).
[53]
VARIANT KD 1207-PRO--GLY-1212 DEL.
PubMed=8863156; DOI=10.1136/jmg.33.8.649;
Winterpacht A., Superti-Furga A., Schwarze U., Stoess H.,
Steinmann B., Spranger J., Zabel B.;
"The deletion of six amino acids at the C-terminus of the alpha 1 (II)
chain causes overmodification of type II and type XI collagen: further
evidence for the association between small deletions in COL2A1 and
Kniest dysplasia.";
J. Med. Genet. 33:649-654(1996).
[54]
VARIANT EDMMD CYS-904.
PubMed=9800905;
DOI=10.1002/(SICI)1096-8628(19981102)80:1<6::AID-AJMG2>3.0.CO;2-0;
Ballo R., Beighton P.H., Ramesar R.S.;
"Stickler-like syndrome due to a dominant negative mutation in the
COL2A1 gene.";
Am. J. Med. Genet. 80:6-11(1998).
[55]
VARIANT SPONDYLOEPIPHYSEAL DYSPLASIA CYS-719.
PubMed=9711874;
DOI=10.1002/(SICI)1098-1004(1998)12:3<172::AID-HUMU4>3.0.CO;2-J;
Bleasel J.F., Holderbaum D., Brancolini V., Moskowitz R.W.,
Considine E.L., Prockop D.J., Devoto M., Williams C.J.;
"Five families with arginine 519-cysteine mutation in COL2A1: evidence
for three distinct founders.";
Hum. Mutat. 12:172-176(1998).
[56]
VARIANT STL1 CYS-565, AND VARIANT DRRD PHE-667.
PubMed=11007540; DOI=10.1086/321189;
Richards A.J., Baguley D.M., Yates J.R.W., Lane C., Nicol M.,
Harper P.S., Scott J.D., Snead M.P.;
"Variation in the vitreous phenotype of Stickler syndrome can be
caused by different amino acid substitutions in the X position of the
type II collagen Gly-X-Y triple helix.";
Am. J. Hum. Genet. 67:1083-1094(2000).
[57]
VARIANT SEDC ARG-1173.
PubMed=10678662;
DOI=10.1002/(SICI)1096-8628(20000131)90:3<239::AID-AJMG10>3.3.CO;2-F;
Sobetzko D., Eich G., Kalff-Suske M., Grzeschik K.-H.,
Superti-Furga A.;
"Boy with syndactylies, macrocephaly, and severe skeletal dysplasia:
not a new syndrome, but two dominant mutations (GLI3 E543X and COL2A1
G973R) in the same individual.";
Am. J. Med. Genet. 90:239-242(2000).
[58]
VARIANTS ACG2 VAL-453; ASP-453; ASP-771; ARG-780; ARG-795; GLU-894;
ASP-948; SER-981; VAL-1065 AND ARG-1119, VARIANT HYPOCHONDROGENESIS
1017-GLY--VAL-1022 DEL, AND VARIANT ILE-1331.
PubMed=10797431;
DOI=10.1002/(SICI)1096-8628(20000515)92:2<95::AID-AJMG3>3.0.CO;2-9;
Koerkkoe J., Cohn D.H., Ala-Kokko L., Krakow D., Prockop D.J.;
"Widely distributed mutations in the COL2A1 gene produce
achondrogenesis type II/hypochondrogenesis.";
Am. J. Med. Genet. 92:95-100(2000).
[59]
VARIANTS ACG2 SER-513; VAL-717; ALA-771; CYS-1110 AND SER-1143, AND
VARIANT PLSD-T ASN-1390.
PubMed=10745044; DOI=10.1136/jmg.37.4.263;
Mortier G.R., Weis M., Nuytinck L., King L.M., Wilkin D.J.,
De Paepe A., Lachman R.S., Rimoin D.L., Eyre D.R., Cohn D.H.;
"Report of five novel and one recurrent COL2A1 mutations with analysis
of genotype-phenotype correlation in patients with a lethal type II
collagen disorder.";
J. Med. Genet. 37:263-271(2000).
[60]
VARIANT SEDC MET-1439.
PubMed=11746045; DOI=10.1002/ajmg.10062;
Unger S., Koerkkoe J., Krakow D., Lachman R.S., Rimoin D.L.,
Cohn D.H.;
"Double heterozygosity for pseudoachondroplasia and spondyloepiphyseal
dysplasia congenita.";
Am. J. Med. Genet. 104:140-146(2001).
[61]
VARIANT VITREORETINOPATHY ASP-1305.
PubMed=12205109; DOI=10.1136/jmg.39.9.661;
Richards A.J., Morgan J., Bearcroft P.W.P., Pickering E., Owen M.J.,
Holmans P., Williams N., Tysoe C., Pope F.M., Snead M.P., Hughes H.;
"Vitreoretinopathy with phalangeal epiphyseal dysplasia, a type II
collagenopathy resulting from a novel mutation in the C-propeptide
region of the molecule.";
J. Med. Genet. 39:661-665(2002).
[62]
VARIANT ACG2 ASP-516.
PubMed=15054848; DOI=10.1002/ajmg.a.20597;
Faivre L., Le Merrer M., Douvier S., Laurent N., Thauvin-Robinet C.,
Rousseau T., Vereecke I., Sagot P., Delezoide A.-L., Coucke P.,
Mortier G.;
"Recurrence of achondrogenesis type II within the same family:
evidence for germline mosaicism.";
Am. J. Med. Genet. A 126:308-312(2004).
[63]
INVOLVEMENT IN SPONDYLOPERIPHERAL DYSPLASIA.
PubMed=15316962; DOI=10.1002/ajmg.a.30222;
Zankl A., Zabel B., Hilbert K., Wildhardt G., Cuenot S., Xavier B.,
Ha-Vinh R., Bonafe L., Spranger J., Superti-Furga A.;
"Spondyloperipheral dysplasia is caused by truncating mutations in the
C-propeptide of COL2A1.";
Am. J. Med. Genet. A 129:144-148(2004).
[64]
VARIANT PLSD-T CYS-1391.
PubMed=14729840; DOI=10.1136/jmg.2003.013722;
Nishimura G., Nakashima E., Mabuchi A., Shimamoto K., Shimamoto T.,
Shimao Y., Nagai T., Yamaguchi T., Kosaki R., Ohashi H., Makita Y.,
Ikegawa S.;
"Identification of COL2A1 mutations in platyspondylic skeletal
dysplasia, Torrance type.";
J. Med. Genet. 41:75-79(2004).
[65]
VARIANTS PLSD-T PRO-1448; HIS-1469; VAL-1484 DEL AND GLY-1485, AND
DISCUSSION OF VARIANT ASN-1390.
PubMed=15643621; DOI=10.1002/ajmg.a.30531;
Zankl A., Neumann L., Ignatius J., Nikkels P., Schrander-Stumpel C.,
Mortier G., Omran H., Wright M., Hilbert K., Bonafe L., Spranger J.,
Zabel B., Superti-Furga A.;
"Dominant negative mutations in the C-propeptide of COL2A1 cause
platyspondylic lethal skeletal dysplasia, torrance type, and define a
novel subfamily within the type 2 collagenopathies.";
Am. J. Med. Genet. A 133:61-67(2005).
[66]
VARIANT SEMDSTWK GLY-992.
PubMed=16088915; DOI=10.1002/ajmg.a.30881;
Sulko J., Czarny-Ratajczak M., Wozniak A., Latos-Bielenska A.,
Kozlowski K.;
"Novel amino acid substitution in the Y-position of collagen type II
causes spondyloepimetaphyseal dysplasia congenita.";
Am. J. Med. Genet. A 137:292-297(2005).
[67]
VARIANTS DRRD ARG-318 AND PHE-667.
PubMed=15671297; DOI=10.1167/iovs.04-1017;
Richards A.J., Meredith S., Poulson A., Bearcroft P., Crossland G.,
Baguley D.M., Scott J.D., Snead M.P.;
"A novel mutation of COL2A1 resulting in dominantly inherited
rhegmatogenous retinal detachment.";
Invest. Ophthalmol. Vis. Sci. 46:663-668(2005).
[68]
VARIANTS ANFH1 SER-717 AND SER-1170.
PubMed=15930420; DOI=10.1056/NEJMoa042480;
Liu Y.-F., Chen W.-M., Lin Y.-F., Yang R.-C., Lin M.-W., Li L.-H.,
Chang Y.-H., Jou Y.-S., Lin P.-Y., Su J.-S., Huang S.-F., Hsiao K.-J.,
Fann C.S.J., Hwang H.-W., Chen Y.-T., Tsai S.-F.;
"Type II collagen gene variants and inherited osteonecrosis of the
femoral head.";
N. Engl. J. Med. 352:2294-2301(2005).
[69]
INVOLVEMENT IN STL1O.
PubMed=16752401; DOI=10.1002/humu.20347;
Richards A.J., Laidlaw M., Whittaker J., Treacy B., Rai H.,
Bearcroft P., Baguley D.M., Poulson A., Ang A., Scott J.D.,
Snead M.P.;
"High efficiency of mutation detection in type 1 stickler syndrome
using a two-stage approach: vitreoretinal assessment coupled with exon
sequencing for screening COL2A1.";
Hum. Mutat. 27:696-704(2006).
[70]
VARIANT ACG2 VAL-547.
PubMed=17994563; DOI=10.1002/ajmg.a.32047;
Forzano F., Lituania M., Viassolo A., Superti-Furga V., Wildhardt G.,
Zabel B., Faravelli F.;
"A familial case of achondrogenesis type II caused by a dominant
COL2A1 mutation and 'patchy' expression in the mosaic father.";
Am. J. Med. Genet. A 143:2815-2820(2007).
[71]
VARIANT LCPD SER-1170.
PubMed=17394019; DOI=10.1007/s00439-007-0354-y;
Miyamoto Y., Matsuda T., Kitoh H., Haga N., Ohashi H., Nishimura G.,
Ikegawa S.;
"A recurrent mutation in type II collagen gene causes Legg-Calve-
Perthes disease in a Japanese family.";
Hum. Genet. 121:625-629(2007).
[72]
VARIANT CZECHD CYS-275.
PubMed=18553548; DOI=10.1002/ajmg.a.32389;
Tzschach A., Tinschert S., Kaminsky E., Lusga E., Mundlos S.,
Graul-Neumann L.M.;
"Czech dysplasia: report of a large family and further delineation of
the phenotype.";
Am. J. Med. Genet. A 146:1859-1864(2008).
[73]
VARIANTS SER-9; ASP-142; ILE-638; THR-1051; ILE-1331 AND SER-1405.
PubMed=18272325; DOI=10.1016/j.ygeno.2007.12.008;
Chan T.F., Poon A., Basu A., Addleman N.R., Chen J., Phong A.,
Byers P.H., Klein T.E., Kwok P.Y.;
"Natural variation in four human collagen genes across an ethnically
diverse population.";
Genomics 91:307-314(2008).
[74]
VARIANT STL1O TYR-57.
PubMed=17721977; DOI=10.1002/humu.20603;
McAlinden A., Majava M., Bishop P.N., Perveen R., Black G.C.M.,
Pierpont M.E., Ala-Kokko L., Maennikkoe M.;
"Missense and nonsense mutations in the alternatively-spliced exon 2
of COL2A1 cause the ocular variant of Stickler syndrome.";
Hum. Mutat. 29:83-90(2008).
[75]
VARIANT CZECHD CYS-275.
PubMed=19764028; DOI=10.1002/ajmg.a.33010;
Matsui Y., Michigami T., Tachikawa K., Yamazaki M., Kawabata H.,
Nishimura G.;
"Czech dysplasia occurring in a Japanese family.";
Am. J. Med. Genet. A 149:2285-2289(2009).
[76]
VARIANTS STL1 ASP-240; ARG-270; ASP-282; ALA-453; ARG-501; CYS-904 AND
ALA-1158.
PubMed=20513134; DOI=10.1002/humu.21257;
Richards A.J., McNinch A., Martin H., Oakhill K., Rai H., Waller S.,
Treacy B., Whittaker J., Meredith S., Poulson A., Snead M.P.;
"Stickler syndrome and the vitreous phenotype: mutations in COL2A1 and
COL11A1.";
Hum. Mutat. 31:E1461-E1471(2010).
[77]
VARIANT ANFH1 MET-1383.
PubMed=21671384; DOI=10.1002/ajmg.a.34056;
Kannu P., O'Rielly D.D., Hyland J.C., Kokko L.A.;
"Avascular necrosis of the femoral head due to a novel C propeptide
mutation in COL2A1.";
Am. J. Med. Genet. A 155A:1759-1762(2011).
[78]
VARIANTS VAL-1176 AND ARG-1179.
PubMed=21922596; DOI=10.1002/humu.21611;
Jackson G.C., Mittaz-Crettol L., Taylor J.A., Mortier G.R.,
Spranger J., Zabel B., Le Merrer M., Cormier-Daire V., Hall C.M.,
Offiah A., Wright M.J., Savarirayan R., Nishimura G., Ramsden S.C.,
Elles R., Bonafe L., Superti-Furga A., Unger S., Zankl A.,
Briggs M.D.;
"Pseudoachondroplasia and multiple epiphyseal dysplasia: A 7-year
comprehensive analysis of the known disease genes identify novel and
recurrent mutations and provides an accurate assessment of their
relative contribution.";
Hum. Mutat. 33:144-157(2012).
-!- FUNCTION: Type II collagen is specific for cartilaginous tissues.
It is essential for the normal embryonic development of the
skeleton, for linear growth and for the ability of cartilage to
resist compressive forces.
-!- SUBUNIT: Homotrimers of alpha 1(II) chains.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=2;
IsoId=P02458-2; Sequence=Displayed;
Name=1;
IsoId=P02458-1; Sequence=VSP_022366;
Name=3;
IsoId=P02458-3; Sequence=VSP_022365;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Isoform 2 is highly expressed in juvenile
chondrocyte and low in fetal chondrocyte.
{ECO:0000269|PubMed:2355003}.
-!- DOMAIN: The C-terminal propeptide, also known as COLFI domain,
have crucial roles in tissue growth and repair by controlling both
the intracellular assembly of procollagen molecules and the
extracellular assembly of collagen fibrils. It binds a calcium ion
which is essential for its function (By similarity).
{ECO:0000250}.
-!- PTM: The N-telopeptide is covalently linked to the helical COL2
region of alpha 1(IX), alpha 2(IX) and alpha 3(IX) chain. The C-
telopeptide is covalently linked to an another site in the helical
region of alpha 3(IX) COL2.
-!- PTM: Contains mostly 4-hydroxyproline. Prolines at the third
position of the tripeptide repeating unit (G-X-P) are 4-
hydroxylated in some or all of the chains.
{ECO:0000250|UniProtKB:P05539}.
-!- PTM: Contains 3-hydroxyproline at a few sites. This modification
occurs on the first proline residue in the sequence motif Gly-Pro-
Hyp, where Hyp is 4-hydroxyproline.
{ECO:0000250|UniProtKB:P05539}.
-!- PTM: Lysine residues at the third position of the tripeptide
repeating unit (G-X-Y) are 5-hydroxylated in some or all of the
chains. {ECO:0000250|UniProtKB:P05539}.
-!- PTM: O-glycosylated on hydroxylated lysine residues. The O-linked
glycan consists of a Glc-Gal disaccharide.
{ECO:0000250|UniProtKB:P05539}.
-!- DISEASE: Spondyloepiphyseal dysplasia congenital type (SEDC)
[MIM:183900]: Disorder characterized by disproportionate short
stature and pleiotropic involvement of the skeletal and ocular
systems. {ECO:0000269|PubMed:10678662,
ECO:0000269|PubMed:11746045, ECO:0000269|PubMed:2339128,
ECO:0000269|PubMed:2543071, ECO:0000269|PubMed:7757086,
ECO:0000269|PubMed:8019561, ECO:0000269|PubMed:8325895,
ECO:0000269|PubMed:8423604}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Spondyloepiphyseal dysplasia, Stanescu type (SEDSTN)
[MIM:616583]: An autosomal dominant spondyloepiphyseal dysplasia
characterized by glycoproteins accumulation in chondrocytes.
Clinical features include progressive joint contractures,
premature degenerative joint disease particularly in the knee, hip
and finger joints, and osseous distention of the metaphyseal ends
of the phalanges causing swolling of interphalangeal joints of the
hands. Radiological features include generalized platyspondyly,
hypoplastic pelvis, epiphyseal flattening with metaphyseal
splaying of the long bones, and enlarged phalangeal epimetaphyses
of the hands. {ECO:0000269|PubMed:26183434}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- DISEASE: Spondyloepimetaphyseal dysplasia, Strudwick type
(SEMDSTWK) [MIM:184250]: A bone disease characterized by
disproportionate short stature from birth, with a very short trunk
and shortened limbs, and skeletal abnormalities including
lordosis, scoliosis, flattened vertebrae, pectus carinatum, coxa
vara, clubfoot, and abnormal epiphyses or metaphyses. A
distinctive radiographic feature is irregular sclerotic changes,
described as dappled in the metaphyses of the long bones.
{ECO:0000269|PubMed:16088915, ECO:0000269|PubMed:7550321,
ECO:0000269|Ref.39}. Note=The disease is caused by mutations
affecting the gene represented in this entry.
-!- DISEASE: Achondrogenesis 2 (ACG2) [MIM:200610]: A disease
characterized by the absence of ossification in the vertebral
column, sacrum and pubic bones. {ECO:0000269|PubMed:10745044,
ECO:0000269|PubMed:10797431, ECO:0000269|PubMed:15054848,
ECO:0000269|PubMed:17994563, ECO:0000269|PubMed:2572591,
ECO:0000269|PubMed:7757081, ECO:0000269|PubMed:7757086,
ECO:0000269|PubMed:7829510}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Legg-Calve-Perthes disease (LCPD) [MIM:150600]:
Characterized by loss of circulation to the femoral head,
resulting in avascular necrosis in a growing child. Clinical
pictures of the disease vary, depending on the phase of disease
progression through ischemia, revascularization, fracture and
collapse, and repair and remodeling of the bone.
{ECO:0000269|PubMed:17394019}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Kniest dysplasia (KD) [MIM:156550]: Moderately severe
chondrodysplasia phenotype that results from mutations in the
COL2A1 gene. Characteristics of the disorder include a short trunk
and extremities, mid-face hypoplasia, cleft palate, myopia,
retinal detachment, and hearing loss. {ECO:0000269|PubMed:7874117,
ECO:0000269|PubMed:8863156}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Avascular necrosis of femoral head, primary, 1 (ANFH1)
[MIM:608805]: A disease characterized by mechanical failure of the
subchondral bone, and degeneration of the hip joint. It usually
leads to destruction of the hip joint in the third to fifth decade
of life. The clinical manifestations, such as pain on exertion, a
limping gait, and a discrepancy in leg length, cause considerable
disability. ANFH1 inheritance is autosomal dominant.
{ECO:0000269|PubMed:15930420, ECO:0000269|PubMed:21671384}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Osteoarthritis with mild chondrodysplasia (OSCDP)
[MIM:604864]: Osteoarthritis is a common disease that produces
joint pain and stiffness together with radiologic evidence of
progressive degeneration of joint cartilage.
{ECO:0000269|PubMed:1975693, ECO:0000269|PubMed:1985108,
ECO:0000269|PubMed:7757086, ECO:0000269|PubMed:8507190}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Platyspondylic lethal skeletal dysplasia Torrance type
(PLSD-T) [MIM:151210]: Platyspondylic lethal skeletal dysplasias
(PLSDs) are a heterogeneous group of chondrodysplasias
characterized by severe platyspondyly and limb shortening. PLSD-T
is characterized by varying platyspondyly, short ribs with
anterior cupping, hypoplasia of the lower ilia with broad ischial
and pubic bones, and shortening of the tubular bones with splayed
and cupped metaphyses. Histology of the growth plate typically
shows focal hypercellularity with slightly enlarged chondrocytes
in the resting cartilage and relatively well-preserved columnar
formation and ossification at the chondro-osseous junction. PLSD-T
is generally a perinatally lethal disease, but a few long-term
survivors have been reported. {ECO:0000269|PubMed:10745044,
ECO:0000269|PubMed:14729840, ECO:0000269|PubMed:15643621}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Multiple epiphyseal dysplasia with myopia and conductive
deafness (EDMMD) [MIM:132450]: A generalized skeletal dysplasia
associated with significant morbidity. Joint pain, joint
deformity, waddling gait, and short stature are the main clinical
signs and symptoms. EDMMD is an autosomal dominant disorder
characterized by epiphyseal dysplasia associated with progressive
myopia, retinal thinning, crenated cataracts, conductive deafness.
{ECO:0000269|PubMed:9800905}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Spondyloperipheral dysplasia (SPD) [MIM:271700]: SPD
patients manifest short stature, midface hypoplasia, sensorineural
hearing loss, spondyloepiphyseal dysplasia, platyspondyly and
brachydactyly. {ECO:0000269|PubMed:15316962}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- DISEASE: Stickler syndrome 1 (STL1) [MIM:108300]: An autosomal
dominant form of Stickler syndrome, an inherited disorder that
associates ocular signs with more or less complete forms of Pierre
Robin sequence, bone disorders and sensorineural deafness. Ocular
disorders may include juvenile cataract, myopia, strabismus,
vitreoretinal or chorioretinal degeneration, retinal detachment,
and chronic uveitis. Pierre Robin sequence includes an opening in
the roof of the mouth (a cleft palate), a large tongue
(macroglossia), and a small lower jaw (micrognathia). Bones are
affected by slight platyspondylisis and large, often defective
epiphyses. Juvenile joint laxity is followed by early signs of
arthrosis. The degree of hearing loss varies among affected
individuals and may become more severe over time. Syndrome
expressivity is variable. {ECO:0000269|PubMed:11007540,
ECO:0000269|PubMed:20513134, ECO:0000269|PubMed:7977371}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Stickler syndrome 1 non-syndromic ocular (STL1O)
[MIM:609508]: An autosomal dominant form of Stickler syndrome
characterized by the ocular signs typically seen in Stickler
syndrome type 1 such as cataract, myopia, retinal detachment.
Systemic features of premature osteoarthritis, cleft palate,
hearing impairment, and craniofacial abnormalities are either
absent or very mild. {ECO:0000269|PubMed:16752401,
ECO:0000269|PubMed:17721977, ECO:0000269|PubMed:8317498}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Rhegmatogenous retinal detachment autosomal dominant
(DRRD) [MIM:609508]: A eye disease that most frequently results
from a break or tear in the retina that allows fluid from the
vitreous humor to enter the potential space beneath the retina. It
is often associated with pathologic myopia and in most cases leads
to visual impairment or blindness if untreated.
{ECO:0000269|PubMed:11007540, ECO:0000269|PubMed:15671297}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Czech dysplasia (CZECHD) [MIM:609162]: A skeletal
dysplasia characterized by early-onset, progressive
pseudorheumatoid arthritis, platyspondyly, and short third and
fourth toes. {ECO:0000269|PubMed:18553548,
ECO:0000269|PubMed:19764028, ECO:0000269|PubMed:7757086,
ECO:0000269|PubMed:8244341}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the fibrillar collagen family.
{ECO:0000255|PROSITE-ProRule:PRU00793}.
-!- SEQUENCE CAUTION:
Sequence=AAH07252.1; Type=Frameshift; Positions=1198; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X16468; CAA34488.1; -; mRNA.
EMBL; L10347; AAC41772.1; -; Genomic_DNA.
EMBL; BT007205; AAP35869.1; -; mRNA.
EMBL; AC004801; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC007252; AAH07252.1; ALT_FRAME; mRNA.
EMBL; BC116449; AAI16450.1; -; mRNA.
EMBL; X16711; CAA34683.1; -; mRNA.
EMBL; M25730; AAA58428.2; -; Genomic_DNA.
EMBL; M32168; AAA58428.2; JOINED; Genomic_DNA.
EMBL; M25655; AAA58428.2; JOINED; Genomic_DNA.
EMBL; M25656; AAA58428.2; JOINED; Genomic_DNA.
EMBL; M64345; AAA58428.2; JOINED; Genomic_DNA.
EMBL; M60299; AAA73873.1; -; Genomic_DNA.
EMBL; M25698; AAA52051.1; -; Genomic_DNA.
EMBL; X58709; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; X57010; CAA40330.1; -; Genomic_DNA.
EMBL; U15195; AAB60370.1; -; Genomic_DNA.
EMBL; X13783; CAA32030.1; -; mRNA.
EMBL; M25728; AAD15287.1; -; Genomic_DNA.
EMBL; X02371; CAA26223.1; -; Genomic_DNA.
EMBL; X02372; CAA26223.1; JOINED; Genomic_DNA.
EMBL; X02373; CAA26223.1; JOINED; Genomic_DNA.
EMBL; X02374; CAA26223.1; JOINED; Genomic_DNA.
EMBL; X02375; CAA26224.1; -; Genomic_DNA.
EMBL; X02376; CAA26225.1; -; Genomic_DNA.
EMBL; X02377; CAA26226.1; -; Genomic_DNA.
EMBL; X02378; CAA26227.1; -; Genomic_DNA.
EMBL; X16158; CAA34278.1; -; Genomic_DNA.
EMBL; X16158; CAA34279.1; -; Genomic_DNA.
EMBL; X16158; CAA34280.1; -; Genomic_DNA.
EMBL; X16158; CAA34281.1; -; Genomic_DNA.
EMBL; X16158; CAA34282.1; -; Genomic_DNA.
EMBL; X16158; CAA34283.1; -; Genomic_DNA.
EMBL; X16158; CAA34284.1; -; Genomic_DNA.
EMBL; J00116; AAA51997.1; -; Genomic_DNA.
EMBL; L00977; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; M63281; AAA52038.1; -; mRNA.
EMBL; M27468; AAA52039.1; -; Genomic_DNA.
EMBL; X06268; CAA29604.1; -; mRNA.
EMBL; X00339; CAA25092.1; -; Genomic_DNA.
EMBL; M12048; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS41778.1; -. [P02458-2]
CCDS; CCDS8759.1; -. [P02458-1]
PIR; A38513; CGHU6C.
RefSeq; NP_001835.3; NM_001844.4. [P02458-2]
RefSeq; NP_149162.2; NM_033150.2. [P02458-1]
UniGene; Hs.408182; -.
PDB; 1U5M; NMR; -; A=29-97.
PDB; 2FSE; X-ray; 3.10 A; E/F=461-474.
PDB; 2SEB; X-ray; 2.50 A; E=1238-1247.
PDB; 5NIR; X-ray; 1.74 A; A/B=29-98.
PDBsum; 1U5M; -.
PDBsum; 2FSE; -.
PDBsum; 2SEB; -.
PDBsum; 5NIR; -.
DisProt; DP00274; -.
ProteinModelPortal; P02458; -.
SMR; P02458; -.
BioGrid; 107677; 27.
IntAct; P02458; 4.
MINT; MINT-6796075; -.
STRING; 9606.ENSP00000369889; -.
ChEMBL; CHEMBL2364188; -.
DrugBank; DB00048; Collagenase clostridium histolyticum.
iPTMnet; P02458; -.
PhosphoSitePlus; P02458; -.
BioMuta; COL2A1; -.
DMDM; 124056489; -.
EPD; P02458; -.
PaxDb; P02458; -.
PeptideAtlas; P02458; -.
PRIDE; P02458; -.
DNASU; 1280; -.
Ensembl; ENST00000337299; ENSP00000338213; ENSG00000139219. [P02458-1]
Ensembl; ENST00000380518; ENSP00000369889; ENSG00000139219. [P02458-2]
GeneID; 1280; -.
KEGG; hsa:1280; -.
UCSC; uc001rqu.4; human. [P02458-2]
CTD; 1280; -.
DisGeNET; 1280; -.
EuPathDB; HostDB:ENSG00000139219.17; -.
GeneCards; COL2A1; -.
GeneReviews; COL2A1; -.
HGNC; HGNC:2200; COL2A1.
HPA; CAB002214; -.
HPA; HPA055753; -.
MalaCards; COL2A1; -.
MIM; 108300; phenotype.
MIM; 120140; gene+phenotype.
MIM; 132450; phenotype.
MIM; 150600; phenotype.
MIM; 151210; phenotype.
MIM; 156550; phenotype.
MIM; 183900; phenotype.
MIM; 184250; phenotype.
MIM; 200610; phenotype.
MIM; 271700; phenotype.
MIM; 604864; phenotype.
MIM; 608805; phenotype.
MIM; 609162; phenotype.
MIM; 609508; phenotype.
MIM; 616583; phenotype.
neXtProt; NX_P02458; -.
OpenTargets; ENSG00000139219; -.
Orphanet; 93296; Achondrogenesis type 2.
Orphanet; 209867; Autosomal dominant rhegmatogenous retinal detachment.
Orphanet; 137678; Czech dysplasia, metatarsal type.
Orphanet; 85198; Dysspondyloenchondromatosis.
Orphanet; 86820; Familial avascular necrosis of femoral head.
Orphanet; 93297; Hypochondrogenesis.
Orphanet; 485; Kniest dysplasia.
Orphanet; 2380; Legg-Calve-Perthes disease.
Orphanet; 93279; Mild spondyloepiphyseal dysplasia due to COL2A1 mutation with early-onset osteoarthritis.
Orphanet; 166011; Multiple epiphyseal dysplasia, Beighton type.
Orphanet; 85166; Platyspondylic dysplasia, Torrance type.
Orphanet; 93346; Spondyloepimetaphyseal dysplasia congenita, Strudwick type.
Orphanet; 94068; Spondyloepiphyseal dysplasia congenita.
Orphanet; 93315; Spondylometaphyseal dysplasia, 'corner fracture' type.
Orphanet; 93316; Spondylometaphyseal dysplasia, Schmidt type.
Orphanet; 1856; Spondyloperipheral dysplasia - short ulna.
Orphanet; 90653; Stickler syndrome type 1.
Orphanet; 3450; Weissenbacher- Zweymuller syndrome.
PharmGKB; PA26715; -.
eggNOG; KOG3544; Eukaryota.
eggNOG; ENOG410XNMM; LUCA.
GeneTree; ENSGT00900000140789; -.
HOVERGEN; HBG004933; -.
InParanoid; P02458; -.
KO; K19719; -.
OMA; PLQYMRA; -.
OrthoDB; EOG091G03LV; -.
PhylomeDB; P02458; -.
TreeFam; TF344135; -.
Reactome; R-HSA-1442490; Collagen degradation.
Reactome; R-HSA-1474244; Extracellular matrix organization.
Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes.
Reactome; R-HSA-186797; Signaling by PDGF.
Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
Reactome; R-HSA-2022090; Assembly of collagen fibrils and other multimeric structures.
Reactome; R-HSA-216083; Integrin cell surface interactions.
Reactome; R-HSA-3000171; Non-integrin membrane-ECM interactions.
Reactome; R-HSA-3000178; ECM proteoglycans.
Reactome; R-HSA-419037; NCAM1 interactions.
Reactome; R-HSA-8874081; MET activates PTK2 signaling.
Reactome; R-HSA-8948216; Collagen chain trimerization.
SIGNOR; P02458; -.
ChiTaRS; COL2A1; human.
EvolutionaryTrace; P02458; -.
GeneWiki; Collagen,_type_II,_alpha_1; -.
GenomeRNAi; 1280; -.
PMAP-CutDB; P02458; -.
PRO; PR:P02458; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000139219; -.
Genevisible; P02458; HS.
GO; GO:0005604; C:basement membrane; IEA:Ensembl.
GO; GO:0005585; C:collagen type II trimer; IDA:BHF-UCL.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0031012; C:extracellular matrix; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; IDA:BHF-UCL.
GO; GO:0005615; C:extracellular space; IEA:Ensembl.
GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IC:BHF-UCL.
GO; GO:0042802; F:identical protein binding; NAS:BHF-UCL.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0042289; F:MHC class II protein binding; IPI:CAFA.
GO; GO:0048407; F:platelet-derived growth factor binding; IDA:MGI.
GO; GO:0001502; P:cartilage condensation; IEA:Ensembl.
GO; GO:0051216; P:cartilage development; TAS:BHF-UCL.
GO; GO:0060351; P:cartilage development involved in endochondral bone morphogenesis; IEA:Ensembl.
GO; GO:0071773; P:cellular response to BMP stimulus; IEA:Ensembl.
GO; GO:0007417; P:central nervous system development; IEA:Ensembl.
GO; GO:0002062; P:chondrocyte differentiation; IEA:Ensembl.
GO; GO:0030574; P:collagen catabolic process; TAS:Reactome.
GO; GO:0030199; P:collagen fibril organization; IMP:BHF-UCL.
GO; GO:0060272; P:embryonic skeletal joint morphogenesis; IMP:BHF-UCL.
GO; GO:0001958; P:endochondral ossification; IEA:Ensembl.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0003007; P:heart morphogenesis; IEA:Ensembl.
GO; GO:0042472; P:inner ear morphogenesis; IEA:Ensembl.
GO; GO:0060174; P:limb bud formation; IEA:Ensembl.
GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
GO; GO:0030903; P:notochord development; IEA:Ensembl.
GO; GO:0071599; P:otic vesicle development; IEA:Ensembl.
GO; GO:0060021; P:palate development; IEA:Ensembl.
GO; GO:0006029; P:proteoglycan metabolic process; IEA:Ensembl.
GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl.
GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
GO; GO:0007605; P:sensory perception of sound; IMP:BHF-UCL.
GO; GO:0001501; P:skeletal system development; IMP:BHF-UCL.
GO; GO:0001894; P:tissue homeostasis; IEA:Ensembl.
GO; GO:0007601; P:visual perception; IMP:UniProtKB.
Gene3D; 2.160.20.50; -; 10.
Gene3D; 3.90.215.10; -; 1.
InterPro; IPR008160; Collagen.
InterPro; IPR000885; Fib_collagen_C.
InterPro; IPR014716; Fibrinogen_a/b/g_C_1.
InterPro; IPR016133; Insect_cyst_antifreeze_prot.
InterPro; IPR001007; VWF_dom.
Pfam; PF01410; COLFI; 1.
Pfam; PF01391; Collagen; 6.
Pfam; PF00093; VWC; 1.
ProDom; PD002078; Fib_collagen_C; 1.
SMART; SM00038; COLFI; 1.
SMART; SM00214; VWC; 1.
PROSITE; PS51461; NC1_FIB; 1.
PROSITE; PS01208; VWFC_1; 1.
PROSITE; PS50184; VWFC_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Calcium; Cataract; Collagen;
Complete proteome; Deafness; Direct protein sequencing;
Disease mutation; Disulfide bond; Dwarfism; Extracellular matrix;
Glycoprotein; Hydroxylation; Metal-binding; Polymorphism;
Reference proteome; Repeat; Secreted; Signal; Stickler syndrome.
SIGNAL 1 25 {ECO:0000255}.
PROPEP 26 181 N-terminal propeptide.
/FTId=PRO_0000005729.
CHAIN 182 1241 Collagen alpha-1(II) chain.
/FTId=PRO_0000005730.
CHAIN 1242 1487 Chondrocalcin.
/FTId=PRO_0000005731.
DOMAIN 32 90 VWFC. {ECO:0000255|PROSITE-
ProRule:PRU00220}.
DOMAIN 1253 1487 Fibrillar collagen NC1.
{ECO:0000255|PROSITE-ProRule:PRU00793}.
REGION 201 1214 Triple-helical region.
REGION 1215 1241 Nonhelical region (C-terminal).
METAL 1301 1301 Calcium. {ECO:0000250}.
METAL 1303 1303 Calcium. {ECO:0000250}.
METAL 1304 1304 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 1306 1306 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 1309 1309 Calcium. {ECO:0000250}.
SITE 181 182 Cleavage; by procollagen N-endopeptidase.
{ECO:0000250}.
SITE 1241 1242 Cleavage; by procollagen C-endopeptidase.
{ECO:0000250}.
MOD_RES 190 190 5-hydroxylysine. {ECO:0000250}.
MOD_RES 287 287 5-hydroxylysine. {ECO:0000250}.
MOD_RES 299 299 5-hydroxylysine. {ECO:0000250}.
MOD_RES 308 308 5-hydroxylysine. {ECO:0000250}.
MOD_RES 374 374 5-hydroxylysine. {ECO:0000250}.
MOD_RES 608 608 5-hydroxylysine. {ECO:0000250}.
MOD_RES 620 620 5-hydroxylysine. {ECO:0000250}.
MOD_RES 659 659 4-hydroxyproline.
{ECO:0000250|UniProtKB:P05539}.
MOD_RES 668 668 4-hydroxyproline.
{ECO:0000250|UniProtKB:P05539}.
MOD_RES 670 670 3-hydroxyproline.
{ECO:0000250|UniProtKB:P05539}.
MOD_RES 671 671 4-hydroxyproline.
{ECO:0000250|UniProtKB:P05539}.
MOD_RES 674 674 4-hydroxyproline.
{ECO:0000250|UniProtKB:P05539}.
MOD_RES 907 907 3-hydroxyproline.
{ECO:0000250|UniProtKB:P05539}.
MOD_RES 908 908 4-hydroxyproline.
{ECO:0000250|UniProtKB:P05539}.
MOD_RES 914 914 4-hydroxyproline.
{ECO:0000250|UniProtKB:P05539}.
MOD_RES 920 920 4-hydroxyproline.
{ECO:0000250|UniProtKB:P05539}.
MOD_RES 1130 1130 5-hydroxylysine. {ECO:0000250}.
MOD_RES 1144 1144 3-hydroxyproline. {ECO:0000250}.
MOD_RES 1181 1181 4-hydroxyproline.
{ECO:0000250|UniProtKB:P05539}.
MOD_RES 1186 1186 3-hydroxyproline.
{ECO:0000250|UniProtKB:P05539}.
MOD_RES 1187 1187 4-hydroxyproline.
{ECO:0000250|UniProtKB:P05539}.
MOD_RES 1201 1201 3-hydroxyproline.
{ECO:0000250|UniProtKB:P05539}.
MOD_RES 1202 1202 4-hydroxyproline.
{ECO:0000250|UniProtKB:P05539}.
MOD_RES 1205 1205 4-hydroxyproline.
{ECO:0000250|UniProtKB:P05539}.
MOD_RES 1207 1207 3-hydroxyproline.
{ECO:0000250|UniProtKB:P05539}.
MOD_RES 1208 1208 4-hydroxyproline.
{ECO:0000250|UniProtKB:P05539}.
MOD_RES 1211 1211 4-hydroxyproline.
{ECO:0000250|UniProtKB:P05539}.
MOD_RES 1213 1213 3-hydroxyproline.
{ECO:0000250|UniProtKB:P05539}.
MOD_RES 1214 1214 4-hydroxyproline.
{ECO:0000250|UniProtKB:P05539}.
CARBOHYD 190 190 O-linked (Gal...) hydroxylysine.
{ECO:0000250}.
CARBOHYD 287 287 O-linked (Gal...) hydroxylysine.
{ECO:0000250}.
CARBOHYD 299 299 O-linked (Gal...) hydroxylysine.
{ECO:0000250}.
CARBOHYD 308 308 O-linked (Gal...) hydroxylysine.
{ECO:0000250}.
CARBOHYD 374 374 O-linked (Gal...) hydroxylysine.
{ECO:0000250}.
CARBOHYD 608 608 O-linked (Gal...) hydroxylysine.
{ECO:0000250}.
CARBOHYD 620 620 O-linked (Gal...) hydroxylysine.
{ECO:0000250}.
CARBOHYD 1130 1130 O-linked (Gal...) hydroxylysine.
{ECO:0000250}.
CARBOHYD 1388 1388 N-linked (GlcNAc...) asparagine.
DISULFID 1283 1315 {ECO:0000255|PROSITE-ProRule:PRU00793}.
DISULFID 1289 1289 Interchain (with C-1306).
{ECO:0000255|PROSITE-ProRule:PRU00793}.
DISULFID 1306 1306 Interchain (with C-1289).
{ECO:0000255|PROSITE-ProRule:PRU00793}.
DISULFID 1323 1485 {ECO:0000255|PROSITE-ProRule:PRU00793}.
DISULFID 1393 1438 {ECO:0000255|PROSITE-ProRule:PRU00793}.
VAR_SEQ 1 1219 Missing (in isoform 3).
{ECO:0000303|Ref.3}.
/FTId=VSP_022365.
VAR_SEQ 29 98 QEAGSCVQDGQRYNDKDVWKPEPCRICVCDTGTVLCDDIIC
EDVKDCLSPEIPFGECCPICPTDLATASG -> R (in
isoform 1). {ECO:0000303|PubMed:2587267,
ECO:0000303|PubMed:2803268}.
/FTId=VSP_022366.
VARIANT 9 9 T -> S (in dbSNP:rs3803183).
{ECO:0000269|PubMed:18272325,
ECO:0000269|PubMed:2081599,
ECO:0000269|PubMed:2587267,
ECO:0000269|PubMed:2714801,
ECO:0000269|PubMed:2803268,
ECO:0000269|PubMed:8948452}.
/FTId=VAR_017638.
VARIANT 57 57 C -> Y (in STL1O; dbSNP:rs121912898).
{ECO:0000269|PubMed:17721977}.
/FTId=VAR_063891.
VARIANT 142 142 E -> D (in dbSNP:rs34392760).
{ECO:0000269|PubMed:18272325}.
/FTId=VAR_033782.
VARIANT 158 158 P -> L (in dbSNP:rs1050861).
{ECO:0000269|PubMed:2587267}.
/FTId=VAR_019836.
VARIANT 207 207 G -> R (in SEDSTN; dbSNP:rs869312907).
{ECO:0000269|PubMed:26183434}.
/FTId=VAR_075729.
VARIANT 240 240 G -> D (in STL1).
{ECO:0000269|PubMed:20513134}.
/FTId=VAR_063892.
VARIANT 267 267 G -> D (in STL1O; dbSNP:rs121912872).
{ECO:0000269|PubMed:8317498}.
/FTId=VAR_001738.
VARIANT 270 270 G -> R (in STL1).
{ECO:0000269|PubMed:20513134}.
/FTId=VAR_063893.
VARIANT 275 275 R -> C (in CZECHD; dbSNP:rs121912876).
{ECO:0000269|PubMed:18553548,
ECO:0000269|PubMed:19764028,
ECO:0000269|PubMed:7757086,
ECO:0000269|PubMed:8244341}.
/FTId=VAR_001739.
VARIANT 282 282 G -> D (in STL1).
{ECO:0000269|PubMed:20513134}.
/FTId=VAR_063894.
VARIANT 302 308 Missing (in STL1).
{ECO:0000269|PubMed:7977371}.
/FTId=VAR_001740.
VARIANT 303 303 G -> D (in KD; abnormal allele expressed
in the cartilage; dbSNP:rs121912877).
{ECO:0000269|PubMed:7874117}.
/FTId=VAR_001741.
VARIANT 318 318 G -> R (in DRRD; dbSNP:rs121912894).
{ECO:0000269|PubMed:15671297}.
/FTId=VAR_023925.
VARIANT 354 354 G -> R (in spondylometaphyseal dysplasia;
congenital type; dbSNP:rs121912871).
{ECO:0000269|PubMed:8486375}.
/FTId=VAR_001742.
VARIANT 375 375 G -> R (in SEDC).
/FTId=VAR_001743.
VARIANT 447 447 G -> S (in SEDC).
{ECO:0000269|PubMed:8019561}.
/FTId=VAR_001744.
VARIANT 453 453 G -> A (in STL1; dbSNP:rs794727339).
{ECO:0000269|PubMed:20513134}.
/FTId=VAR_063895.
VARIANT 453 453 G -> D (in ACG2).
{ECO:0000269|PubMed:10797431}.
/FTId=VAR_017639.
VARIANT 453 453 G -> V (in ACG2).
{ECO:0000269|PubMed:10797431}.
/FTId=VAR_017640.
VARIANT 492 492 G -> V (in SEMDSTWK; dbSNP:rs121912881).
{ECO:0000269|PubMed:7550321}.
/FTId=VAR_001745.
VARIANT 501 501 G -> R (in STL1).
{ECO:0000269|PubMed:20513134}.
/FTId=VAR_063896.
VARIANT 504 504 G -> C (in SEMDSTWK; dbSNP:rs121912880).
{ECO:0000269|PubMed:7550321}.
/FTId=VAR_001746.
VARIANT 510 510 G -> D (in ACG2).
/FTId=VAR_001747.
VARIANT 513 513 G -> S (in ACG2).
{ECO:0000269|PubMed:10745044}.
/FTId=VAR_024819.
VARIANT 516 516 G -> D (in ACG2; dbSNP:rs121912888).
{ECO:0000269|PubMed:15054848}.
/FTId=VAR_023926.
VARIANT 547 547 D -> V (in ACG2).
{ECO:0000269|PubMed:17994563}.
/FTId=VAR_063897.
VARIANT 565 565 R -> C (in STL1; dbSNP:rs121912884).
{ECO:0000269|PubMed:11007540}.
/FTId=VAR_023927.
VARIANT 638 638 T -> I (in dbSNP:rs41263847).
{ECO:0000269|PubMed:18272325}.
/FTId=VAR_033783.
VARIANT 667 667 L -> F (in DRRD; dbSNP:rs121912885).
{ECO:0000269|PubMed:11007540,
ECO:0000269|PubMed:15671297}.
/FTId=VAR_023928.
VARIANT 717 717 G -> S (in ANFH1; dbSNP:rs387906558).
{ECO:0000269|PubMed:15930420}.
/FTId=VAR_023929.
VARIANT 717 717 G -> V (in ACG2).
{ECO:0000269|PubMed:10745044}.
/FTId=VAR_024820.
VARIANT 719 719 R -> C (in OSCDP; also in mild
spondyloepiphyseal dysplasia and
precocious osteoarthritis;
dbSNP:rs121912865).
{ECO:0000269|PubMed:1975693,
ECO:0000269|PubMed:1985108,
ECO:0000269|PubMed:7757086,
ECO:0000269|PubMed:8507190,
ECO:0000269|PubMed:9711874}.
/FTId=VAR_001748.
VARIANT 771 771 G -> A (in ACG2).
{ECO:0000269|PubMed:10745044}.
/FTId=VAR_024821.
VARIANT 771 771 G -> D (in ACG2).
{ECO:0000269|PubMed:10797431}.
/FTId=VAR_017641.
VARIANT 774 774 G -> S (in SEDC and hypochondrogenesis;
lethal; dbSNP:rs121912867).
{ECO:0000269|PubMed:1374906}.
/FTId=VAR_001749.
VARIANT 780 780 G -> R (in ACG2).
{ECO:0000269|PubMed:10797431}.
/FTId=VAR_017642.
VARIANT 795 795 G -> R (in ACG2).
{ECO:0000269|PubMed:10797431}.
/FTId=VAR_017643.
VARIANT 804 804 G -> A (in hypochondrogenesis).
/FTId=VAR_001751.
VARIANT 855 855 G -> S (in SEDC).
/FTId=VAR_023930.
VARIANT 891 891 G -> R (in ACG2 and SEDC;
dbSNP:rs121912879).
{ECO:0000269|PubMed:7757081,
ECO:0000269|PubMed:7757086}.
/FTId=VAR_001752.
VARIANT 894 894 G -> E (in ACG2).
{ECO:0000269|PubMed:10797431}.
/FTId=VAR_017644.
VARIANT 897 897 G -> V (in SEMDSTWK).
{ECO:0000269|Ref.39}.
/FTId=VAR_023931.
VARIANT 904 904 R -> C (in EDMMD and STL1;
dbSNP:rs121912882).
{ECO:0000269|PubMed:20513134,
ECO:0000269|PubMed:9800905}.
/FTId=VAR_017645.
VARIANT 909 909 G -> C (in SEMDSTWK; dbSNP:rs121912875).
{ECO:0000269|PubMed:7550321,
ECO:0000269|Ref.39}.
/FTId=VAR_001753.
VARIANT 948 948 G -> D (in ACG2).
{ECO:0000269|PubMed:10797431}.
/FTId=VAR_017646.
VARIANT 969 969 G -> S (in ACG2; dbSNP:rs121912878).
{ECO:0000269|PubMed:7829510}.
/FTId=VAR_001754.
VARIANT 981 981 G -> S (in ACG2).
{ECO:0000269|PubMed:10797431}.
/FTId=VAR_017647.
VARIANT 989 989 R -> C (in SEDC; dbSNP:rs121912874).
{ECO:0000269|PubMed:8325895}.
/FTId=VAR_001755.
VARIANT 992 992 R -> G (in SEMDSTWK; dbSNP:rs121912895).
{ECO:0000269|PubMed:16088915}.
/FTId=VAR_023932.
VARIANT 1005 1005 G -> S (in hypochondrogenesis;
dbSNP:rs753342774).
/FTId=VAR_001756.
VARIANT 1017 1022 Missing (in hypochondrogenesis).
{ECO:0000269|PubMed:10797431}.
/FTId=VAR_017648.
VARIANT 1017 1017 G -> V (in ACG2).
/FTId=VAR_001757.
VARIANT 1051 1051 A -> T (in dbSNP:rs41272041).
{ECO:0000269|PubMed:18272325}.
/FTId=VAR_033784.
VARIANT 1053 1053 G -> E (in hypochondrogenesis; lethal;
dbSNP:rs121912868).
{ECO:0000269|PubMed:1429602}.
/FTId=VAR_001758.
VARIANT 1065 1065 G -> V (in ACG2).
{ECO:0000269|PubMed:10797431}.
/FTId=VAR_017649.
VARIANT 1110 1110 G -> C (in ACG2).
{ECO:0000269|PubMed:10745044}.
/FTId=VAR_001759.
VARIANT 1113 1113 G -> C (in hypochondrogenesis).
{ECO:0000269|PubMed:8723098}.
/FTId=VAR_001760.
VARIANT 1119 1119 G -> R (in ACG2).
{ECO:0000269|PubMed:10797431}.
/FTId=VAR_017650.
VARIANT 1143 1143 G -> S (in ACG2).
{ECO:0000269|PubMed:10745044,
ECO:0000269|PubMed:2572591}.
/FTId=VAR_001761.
VARIANT 1158 1158 G -> A (in STL1).
{ECO:0000269|PubMed:20513134}.
/FTId=VAR_063898.
VARIANT 1164 1199 Missing (in SEDC).
/FTId=VAR_001762.
VARIANT 1170 1170 G -> S (in ANFH1 and LCPD;
dbSNP:rs121912891).
{ECO:0000269|PubMed:15930420,
ECO:0000269|PubMed:17394019}.
/FTId=VAR_023933.
VARIANT 1173 1173 G -> R (in SEDC; dbSNP:rs121912883).
{ECO:0000269|PubMed:10678662}.
/FTId=VAR_017651.
VARIANT 1176 1176 G -> S (in SEDC).
{ECO:0000269|PubMed:7757086}.
/FTId=VAR_001763.
VARIANT 1176 1176 G -> V (mutation found in a patient with
features of multiple epiphyseal
dysplasia; features overlap with SEDC).
{ECO:0000269|PubMed:21922596}.
/FTId=VAR_066836.
VARIANT 1179 1179 G -> R (mutation found in a patient with
features of multiple epiphyseal
dysplasia; features overlap with SEDC).
{ECO:0000269|PubMed:21922596}.
/FTId=VAR_066837.
VARIANT 1184 1184 I -> IGPSGKDGANGIPGPI (in SEDC).
{ECO:0000269|PubMed:2339128}.
/FTId=VAR_019837.
VARIANT 1188 1188 G -> R (in ACG2).
{ECO:0000269|PubMed:7757086}.
/FTId=VAR_001764.
VARIANT 1197 1197 G -> S (in SEDC; dbSNP:rs121912870).
{ECO:0000269|PubMed:8423604}.
/FTId=VAR_001765.
VARIANT 1207 1212 Missing (in KD).
{ECO:0000269|PubMed:8863156}.
/FTId=VAR_001766.
VARIANT 1305 1305 G -> D (in vitreoretinopathy; with
phalangeal epiphyseal dysplasia;
dbSNP:rs121912887).
{ECO:0000269|PubMed:12205109}.
/FTId=VAR_023934.
VARIANT 1331 1331 V -> I (in dbSNP:rs12721427).
{ECO:0000269|PubMed:10797431,
ECO:0000269|PubMed:18272325}.
/FTId=VAR_017652.
VARIANT 1383 1383 T -> M (in ANFH1; dbSNP:rs138498898).
{ECO:0000269|PubMed:21671384}.
/FTId=VAR_075730.
VARIANT 1390 1390 T -> N (in PLSD-T; phenotype previously
considered as achondrogenesis-
hypochondrogenesis type 2).
{ECO:0000269|PubMed:10745044,
ECO:0000269|PubMed:15643621}.
/FTId=VAR_024822.
VARIANT 1391 1391 Y -> C (in PLSD-T; dbSNP:rs121912889).
{ECO:0000269|PubMed:14729840}.
/FTId=VAR_023935.
VARIANT 1405 1405 G -> S (in dbSNP:rs2070739).
{ECO:0000269|PubMed:18272325}.
/FTId=VAR_033785.
VARIANT 1439 1439 T -> M (in SEDC; dbSNP:rs121912886).
{ECO:0000269|PubMed:11746045}.
/FTId=VAR_017105.
VARIANT 1448 1448 T -> P (in PLSD-T).
{ECO:0000269|PubMed:15643621}.
/FTId=VAR_024823.
VARIANT 1469 1469 D -> H (in PLSD-T).
{ECO:0000269|PubMed:15643621}.
/FTId=VAR_024824.
VARIANT 1484 1484 Missing (in PLSD-T).
{ECO:0000269|PubMed:15643621}.
/FTId=VAR_024825.
VARIANT 1485 1485 C -> G (in PLSD-T).
{ECO:0000269|PubMed:15643621}.
/FTId=VAR_024826.
CONFLICT 441 441 G -> D (in Ref. 1; CAA34488).
{ECO:0000305}.
CONFLICT 457 457 E -> K (in Ref. 1; CAA34488).
{ECO:0000305}.
CONFLICT 481 481 A -> P (in Ref. 15; AAB60370).
{ECO:0000305}.
CONFLICT 641 641 A -> E (in Ref. 1; CAA34488 and 16;
CAA32030). {ECO:0000305}.
CONFLICT 677 677 G -> A (in Ref. 16; CAA32030).
{ECO:0000305}.
CONFLICT 784 784 G -> A (in Ref. 16; CAA32030).
{ECO:0000305}.
CONFLICT 832 835 PAGF -> TSGI (in Ref. 1; CAA34488).
{ECO:0000305}.
CONFLICT 1006 1006 K -> Q (in Ref. 1; CAA34488 and 16;
CAA32030). {ECO:0000305}.
CONFLICT 1037 1037 E -> Q (in Ref. 6; CAA34683).
{ECO:0000305}.
CONFLICT 1057 1057 D -> N (in Ref. 17; AAD15287/CAA26223 and
19; AAA51997). {ECO:0000305}.
CONFLICT 1069 1069 A -> T (in Ref. 6; CAA34683, 17;
AAD15287/CAA26223 and 19; AAA51997).
{ECO:0000305}.
CONFLICT 1243 1243 Q -> E (in Ref. 24; CAA29604).
{ECO:0000305}.
CONFLICT 1247 1247 G -> N (in Ref. 24; CAA29604).
{ECO:0000305}.
CONFLICT 1271 1271 S -> T (in Ref. 21; AAA52038).
{ECO:0000305}.
CONFLICT 1274 1274 G -> A (in Ref. 21; AAA52038).
{ECO:0000305}.
CONFLICT 1333 1333 K -> R (in Ref. 28; M12048).
{ECO:0000305}.
CONFLICT 1350 1350 G -> A (in Ref. 28; M12048).
{ECO:0000305}.
CONFLICT 1372 1372 N -> D (in Ref. 17; CAA26223).
{ECO:0000305}.
CONFLICT 1383 1383 T -> A (in Ref. 17; CAA26223).
{ECO:0000305}.
CONFLICT 1400 1400 L -> M (in Ref. 17; CAA26223).
{ECO:0000305}.
STRAND 34 36 {ECO:0000244|PDB:5NIR}.
STRAND 39 41 {ECO:0000244|PDB:5NIR}.
STRAND 46 50 {ECO:0000244|PDB:5NIR}.
STRAND 53 58 {ECO:0000244|PDB:5NIR}.
STRAND 61 70 {ECO:0000244|PDB:5NIR}.
TURN 93 95 {ECO:0000244|PDB:5NIR}.
SEQUENCE 1487 AA; 141785 MW; A8312503825BF0BB CRC64;
MIRLGAPQTL VLLTLLVAAV LRCQGQDVQE AGSCVQDGQR YNDKDVWKPE PCRICVCDTG
TVLCDDIICE DVKDCLSPEI PFGECCPICP TDLATASGQP GPKGQKGEPG DIKDIVGPKG
PPGPQGPAGE QGPRGDRGDK GEKGAPGPRG RDGEPGTPGN PGPPGPPGPP GPPGLGGNFA
AQMAGGFDEK AGGAQLGVMQ GPMGPMGPRG PPGPAGAPGP QGFQGNPGEP GEPGVSGPMG
PRGPPGPPGK PGDDGEAGKP GKAGERGPPG PQGARGFPGT PGLPGVKGHR GYPGLDGAKG
EAGAPGVKGE SGSPGENGSP GPMGPRGLPG ERGRTGPAGA AGARGNDGQP GPAGPPGPVG
PAGGPGFPGA PGAKGEAGPT GARGPEGAQG PRGEPGTPGS PGPAGASGNP GTDGIPGAKG
SAGAPGIAGA PGFPGPRGPP GPQGATGPLG PKGQTGEPGI AGFKGEQGPK GEPGPAGPQG
APGPAGEEGK RGARGEPGGV GPIGPPGERG APGNRGFPGQ DGLAGPKGAP GERGPSGLAG
PKGANGDPGR PGEPGLPGAR GLTGRPGDAG PQGKVGPSGA PGEDGRPGPP GPQGARGQPG
VMGFPGPKGA NGEPGKAGEK GLPGAPGLRG LPGKDGETGA AGPPGPAGPA GERGEQGAPG
PSGFQGLPGP PGPPGEGGKP GDQGVPGEAG APGLVGPRGE RGFPGERGSP GAQGLQGPRG
LPGTPGTDGP KGASGPAGPP GAQGPPGLQG MPGERGAAGI AGPKGDRGDV GEKGPEGAPG
KDGGRGLTGP IGPPGPAGAN GEKGEVGPPG PAGSAGARGA PGERGETGPP GPAGFAGPPG
ADGQPGAKGE QGEAGQKGDA GAPGPQGPSG APGPQGPTGV TGPKGARGAQ GPPGATGFPG
AAGRVGPPGS NGNPGPPGPP GPSGKDGPKG ARGDSGPPGR AGEPGLQGPA GPPGEKGEPG
DDGPSGAEGP PGPQGLAGQR GIVGLPGQRG ERGFPGLPGP SGEPGKQGAP GASGDRGPPG
PVGPPGLTGP AGEPGREGSP GADGPPGRDG AAGVKGDRGE TGAVGAPGAP GPPGSPGPAG
PTGKQGDRGE AGAQGPMGPS GPAGARGIQG PQGPRGDKGE AGEPGERGLK GHRGFTGLQG
LPGPPGPSGD QGASGPAGPS GPRGPPGPVG PSGKDGANGI PGPIGPPGPR GRSGETGPAG
PPGNPGPPGP PGPPGPGIDM SAFAGLGPRE KGPDPLQYMR ADQAAGGLRQ HDAEVDATLK
SLNNQIESIR SPEGSRKNPA RTCRDLKLCH PEWKSGDYWI DPNQGCTLDA MKVFCNMETG
ETCVYPNPAN VPKKNWWSSK SKEKKHIWFG ETINGGFHFS YGDDNLAPNT ANVQMTFLRL
LSTEGSQNIT YHCKNSIAYL DEAAGNLKKA LLIQGSNDVE IRAEGNSRFT YTALKDGCTK
HTGKWGKTVI EYRSQKTSRL PIIDIAPMDI GGPEQEFGVD IGPVCFL


Related products :

Catalog number Product name Quantity
EIAAB08410 COL29A1,COL6A5,Collagen alpha-1(XXIX) chain,Collagen alpha-5(VI) chain,Homo sapiens,Human,von Willebrand factor A domain-containing protein 4,VWA4
E0572h ELISA Alpha-1 type II collagen,COL2A1,Collagen alpha-1(II) chain,Homo sapiens,Human 96T
U0572h CLIA Alpha-1 type II collagen,COL2A1,Collagen alpha-1(II) chain,Homo sapiens,Human 96T
E0571Rb ELISA Alpha-1 type I collagen,COL1A1,Collagen alpha-1(I) chain,Oryctolagus cuniculus,Rabbit 96T
E0571h ELISA Alpha-1 type I collagen,COL1A1,Collagen alpha-1(I) chain,Homo sapiens,Human 96T
E0571m ELISA Alpha-1 type I collagen,Col1a1,Cola1,Collagen alpha-1(I) chain,Mouse,Mus musculus 96T
E0571h ELISA kit Alpha-1 type I collagen,COL1A1,Collagen alpha-1(I) chain,Homo sapiens,Human 96T
U0571h CLIA Alpha-1 type I collagen,COL1A1,Collagen alpha-1(I) chain,Homo sapiens,Human 96T
E0571Rb ELISA kit Alpha-1 type I collagen,COL1A1,Collagen alpha-1(I) chain,Oryctolagus cuniculus,Rabbit 96T
U0571m CLIA Alpha-1 type I collagen,Col1a1,Cola1,Collagen alpha-1(I) chain,Mouse,Mus musculus 96T
E0571m ELISA kit Alpha-1 type I collagen,Col1a1,Cola1,Collagen alpha-1(I) chain,Mouse,Mus musculus 96T
E0572h ELISA kit Alpha-1 type II collagen,COL2A1,Collagen alpha-1(II) chain,Homo sapiens,Human 96T
U0571Rb CLIA Alpha-1 type I collagen,COL1A1,Collagen alpha-1(I) chain,Oryctolagus cuniculus,Rabbit 96T
E0572m ELISA Alpha-1 type II collagen,Col2a1,Collagen alpha-1(II) chain,Mouse,Mus musculus 96T
EIAAB08377 Alpha-2 type I collagen,Col1a2,Cola2,Collagen alpha-2(I) chain,Mouse,Mus musculus
E0572b ELISA Alpha-1 type II collagen,Bos taurus,Bovine,COL2A1,Collagen alpha-1(II) chain 96T
E0571r ELISA Alpha-1 type I collagen,Col1a1,Collagen alpha-1(I) chain,Rat,Rattus norvegicus 96T
U0572m CLIA Alpha-1 type II collagen,Col2a1,Collagen alpha-1(II) chain,Mouse,Mus musculus 96T
U0572r CLIA Alpha-1 type II collagen,Col2a1,Collagen alpha-1(II) chain,Rat,Rattus norvegicus 96T
U0571b CLIA Alpha-1 type I collagen,Bos taurus,Bovine,COL1A1,Collagen alpha-1(I) chain 96T
'AM10160PU-N Collagen type V (collagen v alpha-1 chain) (alpha-1) IgG1 antibody Ab host: Mouse 0.1 mg
U0571r CLIA Alpha-1 type I collagen,Col1a1,Collagen alpha-1(I) chain,Rat,Rattus norvegicus 96T
U0572b CLIA Alpha-1 type II collagen,Bos taurus,Bovine,COL2A1,Collagen alpha-1(II) chain 96T
AM10160PU-N Collagen type V (collagen v alpha-1 chain) (alpha-1) Mouse IgG1 antibody Ab Purified 0.1 mg
E0572b ELISA kit Alpha-1 type II collagen,Bos taurus,Bovine,COL2A1,Collagen alpha-1(II) chain 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur