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Collagen alpha-1(III) chain

 CO3A1_HUMAN             Reviewed;        1466 AA.
P02461; D2JYH5; D3DPH4; P78429; Q15112; Q16403; Q53S91; Q541P8;
Q6LDB3; Q6LDJ2; Q6LDJ3; Q7KZ56; Q8N6U4; Q9UC88; Q9UC89; Q9UC90;
Q9UC91; R4N3C5; V9GZI1;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
27-SEP-2017, entry version 199.
RecName: Full=Collagen alpha-1(III) chain;
Flags: Precursor;
Name=COL3A1;
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 VARIANT GLN-1353.
TISSUE=Skin fibroblast;
PubMed=2764886; DOI=10.1042/bj2600509;
Ala-Kokko L., Kontusaari S., Baldwin C.T., Kuivaniemi H.,
Prockop D.J.;
"Structure of cDNA clones coding for the entire prepro alpha 1 (III)
chain of human type III procollagen. Differences in protein structure
from type I procollagen and conservation of codon preferences.";
Biochem. J. 260:509-516(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANT GLN-1353.
PubMed=11566270; DOI=10.1016/S0945-053X(01)00145-7;
Valkkila M., Melkoniemi M., Kvist L., Kuivaniemi H., Tromp G.,
Ala-Kokko L.;
"Genomic organization of the human COL3A1 and COL5A2 genes: COL5A2 has
evolved differently than the other minor fibrillar collagen genes.";
Matrix Biol. 20:357-366(2001).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ARG-726.
Fang H.;
Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLN-1353.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT
GLN-1353.
TISSUE=Liver;
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).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-176.
PubMed=2777083; DOI=10.1016/0378-1119(89)90228-X;
Benson-Chanda V., Su M.W., Weil D., Chu M.-L., Ramirez F.;
"Cloning and analysis of the 5' portion of the human type-III
procollagen gene (COL3A1).";
Gene 78:255-265(1989).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-170 (ISOFORMS 1/2).
TISSUE=Placenta;
PubMed=3405773; DOI=10.1093/nar/16.14.7201;
Toman D., Ricca G., de Crombrugghe B.;
"Nucleotide sequence of a cDNA coding for the amino-terminal region of
human prepro alpha 1(III) collagen.";
Nucleic Acids Res. 16:7201-7201(1988).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 149-1225 (ISOFORM 1).
PubMed=2780304; DOI=10.1093/nar/17.16.6742;
Janeczko R.A., Ramirez F.;
"Nucleotide and amino acid sequences of the entire human alpha 1 (III)
collagen.";
Nucleic Acids Res. 17:6742-6742(1989).
[11]
PROTEIN SEQUENCE OF 168-398, AND HYDROXYLATION.
PubMed=557335; DOI=10.1021/bi00625a020;
Seyer J.M., Kang A.H.;
"Covalent structure of collagen: amino acid sequence of cyanogen
bromide peptides from the amino-terminal segment of type III collagen
of human liver.";
Biochemistry 16:1158-1164(1977).
[12]
SEQUENCE REVISION.
Seyer J.M.;
Submitted (DEC-1977) to the PIR data bank.
[13]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 186-194 (ISOFORMS 1/2).
PubMed=8317500;
Milewicz D.M., Witz A.M., Smith A.C., Manchester D.K., Waldstein G.,
Byers P.H.;
"Parental somatic and germ-line mosaicism for a multiexon deletion
with unusual endpoints in a type III collagen (COL3A1) allele produces
Ehlers-Danlos syndrome type IV in the heterozygous offspring.";
Am. J. Hum. Genet. 53:62-70(1993).
[14]
NUCLEOTIDE SEQUENCE [MRNA] OF 302-423 (ISOFORMS 1/2).
PubMed=7487954; DOI=10.1042/bj3110939;
Chiodo A.A., Sillence D.O., Cole W.G., Bateman J.F.;
"Abnormal type III collagen produced by an exon-17-skipping mutation
of the COL3A1 gene in Ehlers-Danlos syndrome type IV is not
incorporated into the extracellular matrix.";
Biochem. J. 311:939-943(1995).
[15]
PROTEIN SEQUENCE OF 395-416; 579-595; 800-814 AND 1064-1079.
TISSUE=Colon carcinoma;
PubMed=7864881; DOI=10.1006/bbrc.1995.1264;
Minafra I.P., Andriolo M., Basirico L., Aquino A., Minafra S.,
Boutillon M.-M., van der Rest M.;
"Onco-fetal/laminin-binding collagen from colon carcinoma: detection
of new sequences.";
Biochem. Biophys. Res. Commun. 207:852-859(1995).
[16]
PROTEIN SEQUENCE OF 399-727.
PubMed=687591; DOI=10.1021/bi00609a034;
Seyer J.M., Kang A.H.;
"Covalent structure of collagen: amino acid sequence of five
consecutive CNBr peptides from type III collagen of human liver.";
Biochemistry 17:3404-3411(1978).
[17]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 537-605.
PubMed=1672129;
Lee B., Vitale E., Superti-Furga A., Steinmann B., Ramirez F.;
"G to T transversion at position +5 of a splice donor site causes
skipping of the preceding exon in the type III procollagen transcripts
of a patient with Ehlers-Danlos syndrome type IV.";
J. Biol. Chem. 266:5256-5259(1991).
[18]
PROTEIN SEQUENCE OF 728-964.
PubMed=6246925; DOI=10.1021/bi00549a008;
Seyer J.M., Mainardi C., Kang A.H.;
"Covalent structure of collagen: amino acid sequence of alpha 1 (III)-
CB5 from type III collagen of human liver.";
Biochemistry 19:1583-1589(1980).
[19]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 861-1015 (ISOFORM 1).
PubMed=2145268;
Cole W.G., Chiodo A.A., Lamande S.R., Janeczko R., Ramirez F.,
Dahl H.-H.M., Chan D., Bateman J.F.;
"A base substitution at a splice site in the COL3A1 gene causes exon
skipping and generates abnormal type III procollagen in a patient with
Ehlers-Danlos syndrome type IV.";
J. Biol. Chem. 265:17070-17077(1990).
[20]
NUCLEOTIDE SEQUENCE [MRNA] OF 950-1466 (ISOFORM 1), AND VARIANT
GLN-1353.
PubMed=3357782; DOI=10.1093/nar/16.5.2337;
Mankoo B.S., Dalgleish R.;
"Human pro alpha 1(III) collagen: cDNA sequence for the 3' end.";
Nucleic Acids Res. 16:2337-2337(1988).
[21]
SEQUENCE REVISION TO 1184.
PubMed=3211760; DOI=10.1093/nar/16.24.11833;
Molyneux K., Dalgleish R.;
"Human type III collagen 'variant' is a cDNA cloning artefact.";
Nucleic Acids Res. 16:11833-11833(1988).
[22]
PROTEIN SEQUENCE OF 965-1200, AND HYDROXYLATION.
PubMed=7016180; DOI=10.1021/bi00512a040;
Seyer J.M., Kang A.H.;
"Covalent structure of collagen: amino acid sequence of alpha 1(III)-
CB9 from type III collagen of human liver.";
Biochemistry 20:2621-2627(1981).
[23]
NUCLEOTIDE SEQUENCE [MRNA] OF 1065-1466 (ISOFORM 1).
PubMed=6096827; DOI=10.1093/nar/12.24.9383;
Loidl H.R., Brinker J.M., May M., Pihlajaniemi T., Morrow S.,
Rosenbloom J., Myers J.C.;
"Molecular cloning and carboxyl-propeptide analysis of human type III
procollagen.";
Nucleic Acids Res. 12:9383-9394(1984).
[24]
NUCLEOTIDE SEQUENCE [MRNA] OF 1161-1200 (ISOFORMS 1/2).
PubMed=3754462; DOI=10.1021/bi00354a033;
Miskulin M., Dalgleish R., Kluve-Beckerman B., Rennard S.I.,
Tolstoshev P., Brantly M., Crystal R.G.;
"Human type III collagen gene expression is coordinately modulated
with the type I collagen genes during fibroblast growth.";
Biochemistry 25:1408-1413(1986).
[25]
NUCLEOTIDE SEQUENCE [MRNA] OF 1165-1196 (ISOFORMS 1/2).
PubMed=3858826; DOI=10.1073/pnas.82.10.3385;
Emanuel B.S., Cannizzaro L.A., Seyer J.M., Myers J.C.;
"Human alpha 1(III) and alpha 2(V) procollagen genes are located on
the long arm of chromosome 2.";
Proc. Natl. Acad. Sci. U.S.A. 82:3385-3389(1985).
[26]
NUCLEOTIDE SEQUENCE [MRNA] OF 1122-1466 (ISOFORMS 1/2), AND VARIANT
GLN-1353.
PubMed=2579949;
Chu M.-L., Weil D., de Wet W.J., Bernard M.P., Sippola M., Ramirez F.;
"Isolation of cDNA and genomic clones encoding human pro-alpha 1 (III)
collagen. Partial characterization of the 3' end region of the gene.";
J. Biol. Chem. 260:4357-4363(1985).
[27]
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).
[28]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22905912; DOI=10.1021/pr300539b;
Rosenow A., Noben J.P., Jocken J., Kallendrusch S.,
Fischer-Posovszky P., Mariman E.C., Renes J.;
"Resveratrol-induced changes of the human adipocyte secretion
profile.";
J. Proteome Res. 11:4733-4743(2012).
[29]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[30]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1158-1199, AND INTERCHAIN
DISULFIDE BONDS.
PubMed=18805790; DOI=10.1074/jbc.M805394200;
Boudko S.P., Engel J., Okuyama K., Mizuno K., Bachinger H.P.,
Schumacher M.A.;
"Crystal structure of human type III collagen Gly991-Gly1032 cystine
knot-containing peptide shows both 7/2 and 10/3 triple helical
symmetries.";
J. Biol. Chem. 283:32580-32589(2008).
[31]
X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) OF 1222-1466, PROPEPTIDE,
DISULFIDE BONDS, AND CALCIUM-BINDING SITES.
PubMed=23001006; DOI=10.1038/nsmb.2389;
Bourhis J.M., Mariano N., Zhao Y., Harlos K., Exposito J.Y.,
Jones E.Y., Moali C., Aghajari N., Hulmes D.J.;
"Structural basis of fibrillar collagen trimerization and related
genetic disorders.";
Nat. Struct. Mol. Biol. 19:1031-1036(2012).
[32]
VARIANT EDS4 ARG-303, AND VARIANT THR-668.
PubMed=8514866; DOI=10.1172/JCI116490;
Tromp G., Wu Y., Prockop D.J., Madhatheri S.L., Kleinert C.,
Earley J.J., Zhuang J., Noerrgaard O., Darling R.C., Abbott W.M.,
Cole C.W., Jaakkola P., Ryynaenen M., Pearce W.H., Yao J.S.T.,
Majamaa K., Smullens S.N., Gatalica Z., Ferrell R.E., Jimenez S.A.,
Jackson C.E., Michels V.V., Kaye M., Kuivaniemi H.;
"Sequencing of cDNA from 50 unrelated patients reveals that mutations
in the triple-helical domain of type III procollagen are an infrequent
cause of aortic aneurysms.";
J. Clin. Invest. 91:2539-2545(1993).
[33]
VARIANT THR-698.
PubMed=2235526; DOI=10.1093/nar/18.20.6180;
Zafarullah K., Kleinert C., Tromp G., Kuivaniemi H., Kontusaari S.,
Wu Y., Ganguly A., Prockop D.J.;
"G to A polymorphism in exon 31 of the COL3A1 gene.";
Nucleic Acids Res. 18:6180-6180(1990).
[34]
VARIANT EDS4 ARG-786.
PubMed=2243125; DOI=10.1172/JCI114863;
Kontusaari S., Tromp G., Kuivaniemi H., Romanic A.M., Prockop D.J.;
"A mutation in the gene for type III procollagen (COL3A1) in a family
with aortic aneurysms.";
J. Clin. Invest. 86:1465-1473(1990).
[35]
VARIANT EDS4 830-PRO--PRO-838 DEL.
PubMed=1370809; DOI=10.1007/BF00197268;
Richards A.J., Lloyd J.C., Narcisi P., Ward P.N., Nicholls A.C.,
De Paepe A., Pope F.M.;
"A 27-bp deletion from one allele of the type III collagen gene
(COL3A1) in a large family with Ehlers-Danlos syndrome type IV.";
Hum. Genet. 88:325-330(1992).
[36]
VARIANT EDS4 ARG-828.
PubMed=8411057; DOI=10.1136/jmg.30.8.690;
Richards A.J., Narcisi P., Lloyd J.C., Ferguson C., Pope F.M.;
"The substitution of glycine 661 by arginine in type III collagen
produces mutant molecules with different thermal stabilities and
causes Ehlers-Danlos syndrome type IV.";
J. Med. Genet. 30:690-693(1993).
[37]
VARIANT EDS4 SER-957.
PubMed=2492273;
Tromp G., Kuivaniemi H., Shikata H., Prockop D.J.;
"A single base mutation that substitutes serine for glycine 790 of the
alpha 1 (III) chain of type III procollagen exposes an arginine and
causes Ehlers-Danlos syndrome IV.";
J. Biol. Chem. 264:1349-1352(1989).
[38]
VARIANT EDS4 VAL-960.
PubMed=7749417; DOI=10.1002/humu.1380050213;
Tromp G., de Paepe A., Nuytinck L., Madhatheri S.L., Kuivaniemi H.;
"Substitution of valine for glycine 793 in type III procollagen in
Ehlers-Danlos syndrome type IV.";
Hum. Mutat. 5:179-181(1995).
[39]
VARIANT EDS4 GLU-1014.
PubMed=1352273; DOI=10.1007/BF00194313;
Richards A.J., Ward P.N., Narcisi P., Nicholls A.C., Lloyd J.C.,
Pope F.M.;
"A single base mutation in the gene for type III collagen (COL3A1)
converts glycine 847 to glutamic acid in a family with Ehlers-Danlos
syndrome type IV. An unaffected family member is mosaic for the
mutation.";
Hum. Genet. 89:414-418(1992).
[40]
VARIANT EDS4 ASP-1050.
PubMed=2808425;
Tromp G., Kuivaniemi H., Stolle C.A., Pope F.M., Prockop D.J.;
"Single base mutation in the type III procollagen gene that converts
the codon for glycine 883 to aspartate in a mild variant of Ehlers-
Danlos syndrome IV.";
J. Biol. Chem. 264:19313-19317(1989).
[41]
INVOLVEMENT IN EDS4.
PubMed=2349939;
Kontusaari S., Tromp G., Kuivaniemi H., Ladda R.L., Prockop D.J.;
"Inheritance of an RNA splicing mutation (G+ 1 IVS20) in the type III
procollagen gene (COL3A1) in a family having aortic aneurysms and easy
bruisability: phenotypic overlap between familial arterial aneurysms
and Ehlers-Danlos syndrome type IV.";
Am. J. Hum. Genet. 47:112-120(1990).
[42]
VARIANT EDS4 VAL-1077.
PubMed=1895316; DOI=10.1136/jmg.28.7.458;
Richards A.J., Lloyd J.C., Ward P.N., de Paepe A., Narcisi P.,
Pope F.M.;
"Characterisation of a glycine to valine substitution at amino acid
position 910 of the triple helical region of type III collagen in a
patient with Ehlers-Danlos syndrome type IV.";
J. Med. Genet. 28:458-463(1991).
[43]
VARIANT EDS4 GLU-1173.
PubMed=1357232; DOI=10.1007/BF02435995;
Johnson P.H., Richards A.J., Pope F.M., Hopkinson D.A.;
"A COL3A1 glycine 1006 to glutamic acid substitution in a patient with
Ehlers-Danlos syndrome type IV detected by denaturing gradient gel
electrophoresis.";
J. Inherit. Metab. Dis. 15:426-430(1992).
[44]
VARIANT EDS4 ASP-1185.
PubMed=1496983;
Kontusaari S., Tromp G., Kuivaniemi H., Stolle C.A., Pope F.M.,
Prockop D.J.;
"Substitution of aspartate for glycine 1018 in the type III
procollagen (COL3A1) gene causes type IV Ehlers-Danlos syndrome: the
mutated allele is present in most blood leukocytes of the asymptomatic
and mosaic mother.";
Am. J. Hum. Genet. 51:497-507(1992).
[45]
VARIANT EDS4 GLU-1188.
PubMed=8098182; DOI=10.1002/ajmg.1320460308;
Narcisi P., Wu Y., Tromp G., Earley J.J., Richards A.J., Pope F.M.,
Kuivaniemi H.;
"Single base mutation that substitutes glutamic acid for glycine 1021
in the COL3A1 gene and causes Ehlers-Danlos syndrome type IV.";
Am. J. Med. Genet. 46:278-283(1993).
[46]
VARIANTS EDS4 VAL-1167; ASP-1170 AND GLU-1173.
Richards A.J., Narcisi P., Lloyd J.C., Johnson P.H., Hopkinson D.A.,
Pope F.M.;
"Substitution of glycines 1000, 1003 and 1006 in type III collagen all
cause the acrogeric form of EDS-IV, and destabilise the collagen
triple helix.";
Matrix 13:47-47(1993).
[47]
VARIANTS THR-602 AND LEU-635.
PubMed=8255472; DOI=10.1212/WNL.43.12.2652;
Kuivaniemi H., Prockop D.J., Wu Y., Madhatheri S.L., Kleinert C.,
Earley J.J., Jokinen A., Stolle C.A., Majamaa K., Mylllylae V.V.,
Noerrgaard O., Schievink W.I., Mokri B., Fukawa O., Ter Berg J.W.M.,
de Paepe A., Lozano A.M., Leblanc R., Ryynaenen M., Baxter B.T.,
Shikata H., Ferrell R.E., Tromp G.;
"Exclusion of mutations in the gene for type III collagen (COL3A1) as
a common cause of intracranial aneurysms or cervical artery
dissections: results from sequence analysis of the coding sequences of
type III collagen from 55 unrelated patients.";
Neurology 43:2652-2658(1993).
[48]
VARIANT EDS4 GLU-756.
PubMed=7912131; DOI=10.1093/hmg/3.3.511;
Madhatheri S.L., Tromp G., Gustavson K.H., Kuivaniemi H.;
"Substitution of glutamic acid for glycine 589 in the triple-helical
domain of type III procollagen (COL3A1) in a family with variable
phenotype of the Ehlers-Danlos syndrome type IV.";
Hum. Mol. Genet. 3:511-512(1994).
[49]
VARIANT EDS3 SER-804.
PubMed=7833919; DOI=10.1093/hmg/3.9.1617;
Narcisi P., Richards A.J., Ferguson S.D., Pope F.M.;
"A family with Ehlers-Danlos syndrome type III/articular hypermobility
syndrome has a glycine 637-to-serine substitution in type III
collagen.";
Hum. Mol. Genet. 3:1617-1620(1994).
[50]
VARIANT EDS4 VAL-1176.
PubMed=8019562; DOI=10.1002/humu.1380030315;
Nuytinck L., De Paepe A., Renard J.P., Adriaens F., Leroy J.;
"Single-strand conformation polymorphism (SSCP) analysis of the COL3A1
gene detects a mutation that results in the substitution of glycine
1009 to valine and causes severe Ehlers-Danlos syndrome type IV.";
Hum. Mutat. 3:268-274(1994).
[51]
VARIANTS EDS4 CYS-183; ARG-201; GLU-228; ARG-540; ARG-936; GLU-996;
VAL-1071; ALA-1104; GLU-1182; VAL-1185; GLU-1188 AND ARG-1188.
Goldstein J.A., Schwarze U., Witz A., Byers P.H.;
"Marked heterogeneity in COL3A1 mutations that produce the EDS type IV
phenotype.";
Matrix Biol. 14:392-393(1994).
[52]
VARIANTS EDS4 ASP-909 AND ASP-939.
PubMed=8680408; DOI=10.1002/humu.1380060408;
Johnson P.H., Richards A.J., Lloyd J.C., Pope F.M., Hopkinson D.A.;
"Efficient strategy for the detection of mutations in acrogeric
Ehlers-Danlos syndrome type IV.";
Hum. Mutat. 6:336-342(1995).
[53]
VARIANTS EDS4 GLU-567; CYS-762 AND ASP-1170.
PubMed=8884076;
Mackay K., Raghunath M., Superti-Furga A., Steinmann B., Dalgleish R.;
"Ehlers-Danlos syndrome type IV caused by Gly400Glu, Gly595Cys and
Gly1003Asp substitutions in collagen III: clinical features,
biochemical screening, and molecular confirmation.";
Clin. Genet. 49:286-295(1996).
[54]
VARIANT EDS4 GLU-1101.
PubMed=9147870;
McGrory J., Weksberg R., Thorner P., Cole W.G.;
"Abnormal extracellular matrix in Ehlers-Danlos syndrome type IV due
to the substitution of glycine 934 by glutamic acid in the triple
helical domain of type III collagen.";
Clin. Genet. 50:442-445(1996).
[55]
VARIANT EDS4 ASP-666.
PubMed=8664902;
DOI=10.1002/(SICI)1098-1004(1996)7:1<59::AID-HUMU8>3.3.CO;2-R;
McGrory J., Costa T., Cole W.G.;
"A novel G499D substitution in the alpha 1(III) chain of type III
collagen produces variable forms of Ehlers-Danlos syndrome type IV.";
Hum. Mutat. 7:59-60(1996).
[56]
VARIANT EDS4 SER-582.
PubMed=8990011;
DOI=10.1002/(SICI)1098-1004(1997)9:1<62::AID-HUMU11>3.3.CO;2-B;
Anderson D.W., Thakker-Varia S., Tromp G., Kuivaniemi H., Stolle C.A.;
"A glycine (415)-to-serine substitution results in impaired secretion
and decreased thermal stability of type III procollagen in a patient
with Ehlers-Danlos syndrome type IV.";
Hum. Mutat. 9:62-63(1997).
[57]
VARIANTS EDS4 CYS-183; ARG-201; GLU-228; ARG-540 AND ARG-936.
PubMed=9036918; DOI=10.1111/1523-1747.ep12286441;
Smith L.T., Schwarze U., Goldstein J., Byers P.H.;
"Mutations in the COL3A1 gene result in the Ehlers-Danlos syndrome
type IV and alterations in the size and distribution of the major
collagen fibrils of the dermis.";
J. Invest. Dermatol. 108:241-247(1997).
[58]
VARIANT EDS4 ARG-726.
PubMed=9452103;
Bateman J.F., Chiodo A.A., Weng Y.M., Chan D., Haan E.;
"A type III collagen Gly559 to Arg helix mutation in Ehler's-Danlos
syndrome type IV.";
Hum. Mutat. Suppl. 1:S257-S259(1998).
[59]
VARIANT EDS-IV ARG-1173.
PubMed=10819545; DOI=10.1046/j.1365-2133.2000.03266.x;
Jansen T., de Paepe A., Luytinck N., Plewig G.;
"COL3A1 mutation leading to acrogeria (Gottron Type).";
Br. J. Dermatol. 142:178-180(2000).
[60]
VARIANTS EDS4 ASP-204; ASP-210; ARG-264; ASP-327; ASP-1098 AND
GLU-1173.
PubMed=10923041;
DOI=10.1002/1098-1004(200008)16:2<176::AID-HUMU12>3.0.CO;2-E;
Giunta C., Steinmann B.;
"Characterization of 11 new mutations in COL3A1 of individuals with
Ehlers-Danlos syndrome type IV: preliminary comparison of RNase
cleavage, EMC and DHPLC assays.";
Hum. Mutat. 16:176-177(2000).
[61]
VARIANTS EDS4.
PubMed=10706896; DOI=10.1056/NEJM200003093421001;
Pepin M., Schwarze U., Superti-Furga A., Byers P.H.;
"Clinical and genetic features of Ehlers-Danlos syndrome type IV, the
vascular type.";
N. Engl. J. Med. 342:673-680(2000).
[62]
VARIANT EDS4 ASP-1044.
PubMed=11168790; DOI=10.1046/j.1365-2796.2001.00761.x;
Nishiyama Y., Nejima J., Watanabe A., Kotani E., Sakai N.,
Hatamochi A., Shinkai H., Kiuchi K., Tamura K., Shimada T., Takano T.,
Katayama Y.;
"Ehlers-Danlos syndrome type IV with a unique point mutation in COL3A1
and familial phenotype of myocardial infarction without organic
coronary stenosis.";
J. Intern. Med. 249:103-108(2001).
[63]
VARIANT EDS4 ARG-297.
PubMed=12694234; DOI=10.1034/j.1399-0004.2003.00047.x;
Kroes H.Y., Pals G., van Essen A.J.;
"Ehlers-Danlos syndrome type IV: unusual congenital anomalies in a
mother and son with a COL3A1 mutation and a normal collagen III
protein profile.";
Clin. Genet. 63:224-227(2003).
[64]
ERRATUM.
Kroes H.Y., Pals G., van Essen A.J.;
Clin. Genet. 64:375-375(2003).
[65]
VARIANT EDS4 VAL-1050.
PubMed=12786757; DOI=10.1034/j.1399-0004.2003.00075.x;
Palmeri S., Mari F., Meloni I., Malandrini A., Ariani F.,
Villanova M., Pompilio A., Schwarze U., Byers P.H., Renieri A.;
"Neurological presentation of Ehlers-Danlos syndrome type IV in a
family with parental mosaicism.";
Clin. Genet. 63:510-515(2003).
[66]
VARIANTS [LARGE SCALE ANALYSIS] SER-420 AND CYS-1434.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[67]
VARIANTS THR-679; THR-698; VAL-1205 AND GLN-1353.
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).
-!- FUNCTION: Collagen type III occurs in most soft connective tissues
along with type I collagen. Involved in regulation of cortical
development. Is the major ligand of ADGRG1 in the developing brain
and binding to ADGRG1 inhibits neuronal migration and activates
the RhoA pathway by coupling ADGRG1 to GNA13 and possibly GNA12.
-!- SUBUNIT: Trimers of identical alpha 1(III) chains. The chains are
linked to each other by interchain disulfide bonds. Trimers are
also cross-linked via hydroxylysines.
-!- INTERACTION:
O01949:AAEL010235 (xeno); NbExp=2; IntAct=EBI-2431491, EBI-7685554;
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P02461-1; Sequence=Displayed;
Name=2;
IsoId=P02461-2; Sequence=VSP_022502;
Note=No experimental confirmation available.;
-!- 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.
-!- PTM: Proline residues at the third position of the tripeptide
repeating unit (G-X-Y) are hydroxylated in some or all of the
chains. {ECO:0000269|PubMed:557335, ECO:0000269|PubMed:7016180}.
-!- PTM: O-linked glycan consists of a Glc-Gal disaccharide bound to
the oxygen atom of a post-translationally added hydroxyl group.
-!- DISEASE: Ehlers-Danlos syndrome 3 (EDS3) [MIM:130020]: A
connective tissue disorder characterized by hyperextensible skin,
atrophic cutaneous scars due to tissue fragility and joint
hyperlaxity. It is a form of Ehlers-Danlos syndrome characterized
by marked joint hyperextensibility without skeletal deformity.
{ECO:0000269|PubMed:7833919}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Ehlers-Danlos syndrome 4 (EDS4) [MIM:130050]: The most
severe form of Ehlers-Danlos syndrome, a connective tissue
disorder characterized by hyperextensible skin, atrophic cutaneous
scars due to tissue fragility and joint hyperlaxity. Characterized
by the joint and dermal manifestations as in other forms of the
syndrome, characteristic facial features (acrogeria) in most
patients, and by proneness to spontaneous rupture of bowel and
large arteries. The vascular complications may affect all
anatomical areas. {ECO:0000269|PubMed:10706896,
ECO:0000269|PubMed:10923041, ECO:0000269|PubMed:11168790,
ECO:0000269|PubMed:12694234, ECO:0000269|PubMed:12786757,
ECO:0000269|PubMed:1352273, ECO:0000269|PubMed:1357232,
ECO:0000269|PubMed:1370809, ECO:0000269|PubMed:1496983,
ECO:0000269|PubMed:1895316, ECO:0000269|PubMed:2243125,
ECO:0000269|PubMed:2349939, ECO:0000269|PubMed:2492273,
ECO:0000269|PubMed:2808425, ECO:0000269|PubMed:7749417,
ECO:0000269|PubMed:7912131, ECO:0000269|PubMed:8019562,
ECO:0000269|PubMed:8098182, ECO:0000269|PubMed:8411057,
ECO:0000269|PubMed:8514866, ECO:0000269|PubMed:8664902,
ECO:0000269|PubMed:8680408, ECO:0000269|PubMed:8884076,
ECO:0000269|PubMed:8990011, ECO:0000269|PubMed:9036918,
ECO:0000269|PubMed:9147870, ECO:0000269|PubMed:9452103,
ECO:0000269|Ref.46, ECO:0000269|Ref.51}. 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}.
-!- WEB RESOURCE: Name=COL3A1; Note=Collagen type III alpha-1 chain
mutations;
URL="http://www.le.ac.uk/genetics/collagen/col3a1.html";
-!- WEB RESOURCE: Name=Wikipedia; Note=Type-III collagen entry;
URL="https://en.wikipedia.org/wiki/Type-III_collagen";
-----------------------------------------------------------------------
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EMBL; X14420; CAA32583.1; -; mRNA.
EMBL; AY054301; AAL13167.1; -; Genomic_DNA.
EMBL; AY016295; AAL13167.1; JOINED; Genomic_DNA.
EMBL; KC567894; AGL34959.1; -; Genomic_DNA.
EMBL; GU143397; ACZ58371.1; -; Genomic_DNA.
EMBL; AC066694; AAY24164.1; -; Genomic_DNA.
EMBL; CH471058; EAX10910.1; -; Genomic_DNA.
EMBL; CH471058; EAX10911.1; -; Genomic_DNA.
EMBL; BC028178; AAH28178.1; -; mRNA.
EMBL; M26939; AAA52040.1; -; Genomic_DNA.
EMBL; X07240; CAA30229.1; -; mRNA.
EMBL; X15332; CAA33387.1; -; mRNA.
EMBL; S62925; AAD13937.1; -; Genomic_DNA.
EMBL; S79877; AAB35615.1; -; mRNA.
EMBL; M59312; AAA52041.1; -; Genomic_DNA.
EMBL; M59227; AAB59383.1; -; mRNA.
EMBL; M55603; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; X06700; CAA29886.1; -; mRNA.
EMBL; X01655; CAA25821.1; -; mRNA.
EMBL; X01742; CAA25879.1; -; mRNA.
EMBL; M13146; AAA52003.1; -; mRNA.
EMBL; M11134; AAA52004.1; -; mRNA.
EMBL; M10795; AAA52002.1; -; Genomic_DNA.
EMBL; M10615; AAA52002.1; JOINED; Genomic_DNA.
EMBL; M10793; AAA52002.1; JOINED; Genomic_DNA.
EMBL; M10794; AAA52002.1; JOINED; Genomic_DNA.
EMBL; M10800; AAA52002.1; JOINED; Genomic_DNA.
EMBL; M10801; AAA52002.1; JOINED; Genomic_DNA.
CCDS; CCDS2297.1; -. [P02461-1]
PIR; S05272; CGHU7L.
RefSeq; NP_000081.1; NM_000090.3.
UniGene; Hs.443625; -.
PDB; 2V53; X-ray; 3.20 A; B/C/D=564-584.
PDB; 3DMW; X-ray; 2.30 A; A/B/C=1158-1199.
PDB; 4AE2; X-ray; 1.68 A; A/B/C=1222-1466.
PDB; 4AEJ; X-ray; 2.21 A; A/B/C=1222-1466.
PDB; 4AK3; X-ray; 3.50 A; A=1222-1466.
PDB; 4GYX; X-ray; 1.49 A; A/B/C=1158-1200.
PDBsum; 2V53; -.
PDBsum; 3DMW; -.
PDBsum; 4AE2; -.
PDBsum; 4AEJ; -.
PDBsum; 4AK3; -.
PDBsum; 4GYX; -.
ProteinModelPortal; P02461; -.
SMR; P02461; -.
BioGrid; 107678; 11.
DIP; DIP-57177N; -.
IntAct; P02461; 21.
MINT; MINT-7299332; -.
STRING; 9606.ENSP00000304408; -.
ChEMBL; CHEMBL2364188; -.
DrugBank; DB00048; Collagenase clostridium histolyticum.
iPTMnet; P02461; -.
PhosphoSitePlus; P02461; -.
BioMuta; COL3A1; -.
DMDM; 124056490; -.
PaxDb; P02461; -.
PeptideAtlas; P02461; -.
PRIDE; P02461; -.
Ensembl; ENST00000304636; ENSP00000304408; ENSG00000168542. [P02461-1]
Ensembl; ENST00000317840; ENSP00000315243; ENSG00000168542. [P02461-2]
GeneID; 1281; -.
KEGG; hsa:1281; -.
UCSC; uc002uqj.2; human. [P02461-1]
CTD; 1281; -.
DisGeNET; 1281; -.
EuPathDB; HostDB:ENSG00000168542.12; -.
GeneCards; COL3A1; -.
GeneCards; MIR3606; -.
GeneReviews; COL3A1; -.
HGNC; HGNC:2201; COL3A1.
HPA; CAB016766; -.
HPA; CAB059993; -.
HPA; HPA007583; -.
MalaCards; COL3A1; -.
MIM; 120180; gene.
MIM; 130020; phenotype.
MIM; 130050; phenotype.
neXtProt; NX_P02461; -.
OpenTargets; ENSG00000168542; -.
Orphanet; 2500; Acrogeria.
Orphanet; 286; Ehlers-Danlos syndrome, vascular type.
Orphanet; 86; Familial abdominal aortic aneurysm.
Orphanet; 231160; Familial cerebral saccular aneurysm.
PharmGKB; PA26716; -.
eggNOG; KOG3544; Eukaryota.
eggNOG; ENOG410XNMM; LUCA.
GeneTree; ENSGT00840000129673; -.
HOVERGEN; HBG004933; -.
InParanoid; P02461; -.
KO; K19720; -.
OMA; CRDLKFC; -.
OrthoDB; EOG091G03LV; -.
PhylomeDB; P02461; -.
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-3000170; Syndecan interactions.
Reactome; R-HSA-3000171; Non-integrin membrane-ECM interactions.
Reactome; R-HSA-3000178; ECM proteoglycans.
Reactome; R-HSA-3000480; Scavenging by Class A Receptors.
Reactome; R-HSA-419037; NCAM1 interactions.
Reactome; R-HSA-8874081; MET activates PTK2 signaling.
Reactome; R-HSA-8948216; Collagen chain trimerization.
ChiTaRS; COL3A1; human.
EvolutionaryTrace; P02461; -.
GeneWiki; Collagen,_type_III,_alpha_1; -.
GenomeRNAi; 1281; -.
PRO; PR:P02461; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000168542; -.
ExpressionAtlas; P02461; baseline and differential.
Genevisible; P02461; HS.
GO; GO:0005586; C:collagen type III trimer; IDA:CAFA.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0031012; C:extracellular matrix; IMP:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005201; F:extracellular matrix structural constituent; IMP:UniProtKB.
GO; GO:0005178; F:integrin binding; IMP:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0048407; F:platelet-derived growth factor binding; IDA:MGI.
GO; GO:0002020; F:protease binding; IPI:CAFA.
GO; GO:0046332; F:SMAD binding; IEA:Ensembl.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0060414; P:aorta smooth muscle tissue morphogenesis; IEA:Ensembl.
GO; GO:0007160; P:cell-matrix adhesion; IDA:UniProtKB.
GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
GO; GO:0021987; P:cerebral cortex development; ISS:UniProtKB.
GO; GO:0030574; P:collagen catabolic process; TAS:Reactome.
GO; GO:0030199; P:collagen fibril organization; IMP:UniProtKB.
GO; GO:0048565; P:digestive tract development; IEA:Ensembl.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0007507; P:heart development; IMP:UniProtKB.
GO; GO:0007229; P:integrin-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0050777; P:negative regulation of immune response; IMP:UniProtKB.
GO; GO:2001223; P:negative regulation of neuron migration; ISS:UniProtKB.
GO; GO:0018149; P:peptide cross-linking; IDA:UniProtKB.
GO; GO:0030168; P:platelet activation; NAS:UniProtKB.
GO; GO:0035025; P:positive regulation of Rho protein signal transduction; ISS:UniProtKB.
GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
GO; GO:0034097; P:response to cytokine; IDA:UniProtKB.
GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
GO; GO:0009314; P:response to radiation; IDA:UniProtKB.
GO; GO:0001501; P:skeletal system development; IEA:Ensembl.
GO; GO:0043588; P:skin development; IMP:UniProtKB.
GO; GO:0097435; P:supramolecular fiber organization; IMP:UniProtKB.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IDA:UniProtKB.
GO; GO:0042060; P:wound healing; IDA:UniProtKB.
Gene3D; 3.90.215.10; -; 1.
InterPro; IPR008160; Collagen.
InterPro; IPR000885; Fib_collagen_C.
InterPro; IPR014716; Fibrinogen_a/b/g_C_1.
InterPro; IPR001007; VWF_dom.
Pfam; PF01410; COLFI; 1.
Pfam; PF01391; Collagen; 8.
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; Aortic aneurysm; Calcium;
Collagen; Complete proteome; Direct protein sequencing;
Disease mutation; Disulfide bond; Ehlers-Danlos syndrome;
Extracellular matrix; Glycoprotein; Hydroxylation; Metal-binding;
Polymorphism; Reference proteome; Repeat; Secreted; Signal.
SIGNAL 1 23
PROPEP 24 153 N-terminal propeptide.
/FTId=PRO_0000005740.
CHAIN 154 1221 Collagen alpha-1(III) chain.
/FTId=PRO_0000005741.
PROPEP 1222 1466 C-terminal propeptide.
/FTId=PRO_0000005742.
DOMAIN 30 89 VWFC. {ECO:0000255|PROSITE-
ProRule:PRU00220}.
DOMAIN 1232 1466 Fibrillar collagen NC1.
{ECO:0000255|PROSITE-ProRule:PRU00793}.
REGION 149 167 Nonhelical region (N-terminal).
REGION 168 1196 Triple-helical region.
REGION 1197 1205 Nonhelical region (C-terminal).
METAL 1280 1280 Calcium.
METAL 1282 1282 Calcium.
METAL 1283 1283 Calcium; via carbonyl oxygen.
METAL 1285 1285 Calcium; via carbonyl oxygen.
METAL 1288 1288 Calcium.
MOD_RES 263 263 5-hydroxylysine; alternate.
MOD_RES 284 284 5-hydroxylysine.
MOD_RES 860 860 5-hydroxylysine.
MOD_RES 977 977 5-hydroxylysine.
MOD_RES 1094 1094 5-hydroxylysine; partial.
MOD_RES 1106 1106 5-hydroxylysine.
CARBOHYD 263 263 O-linked (Gal...) hydroxylysine;
alternate.
DISULFID 1196 1196 Interchain. {ECO:0000255|PROSITE-
ProRule:PRU00793,
ECO:0000269|PubMed:23001006}.
DISULFID 1197 1197 Interchain. {ECO:0000255|PROSITE-
ProRule:PRU00793,
ECO:0000269|PubMed:23001006}.
DISULFID 1262 1294 {ECO:0000255|PROSITE-ProRule:PRU00793,
ECO:0000269|PubMed:23001006}.
DISULFID 1268 1268 Interchain (with C-1285).
{ECO:0000255|PROSITE-ProRule:PRU00793,
ECO:0000269|PubMed:23001006}.
DISULFID 1285 1285 Interchain (with C-1268).
{ECO:0000255|PROSITE-ProRule:PRU00793,
ECO:0000269|PubMed:23001006}.
DISULFID 1302 1464 {ECO:0000255|PROSITE-ProRule:PRU00793,
ECO:0000269|PubMed:23001006}.
DISULFID 1372 1417 {ECO:0000255|PROSITE-ProRule:PRU00793,
ECO:0000269|PubMed:23001006}.
VAR_SEQ 847 1149 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_022502.
VARIANT 169 169 L -> F (in dbSNP:rs111391222).
/FTId=VAR_001767.
VARIANT 183 183 G -> C (in EDS4; dbSNP:rs121912926).
{ECO:0000269|PubMed:9036918,
ECO:0000269|Ref.51}.
/FTId=VAR_001768.
VARIANT 183 183 G -> D (in EDS4; dbSNP:rs587779420).
/FTId=VAR_011095.
VARIANT 183 183 G -> S (in EDS4; dbSNP:rs121912926).
/FTId=VAR_011096.
VARIANT 192 192 G -> V (in EDS4; dbSNP:rs587779710).
/FTId=VAR_011097.
VARIANT 201 201 G -> R (in EDS4; dbSNP:rs587779436).
{ECO:0000269|PubMed:9036918,
ECO:0000269|Ref.51}.
/FTId=VAR_001769.
VARIANT 204 204 G -> D (in EDS4; dbSNP:rs587779626).
{ECO:0000269|PubMed:10923041}.
/FTId=VAR_011098.
VARIANT 204 204 G -> S (in EDS4; dbSNP:rs587779711).
/FTId=VAR_011099.
VARIANT 210 210 G -> D (in EDS4).
{ECO:0000269|PubMed:10923041}.
/FTId=VAR_011100.
VARIANT 219 219 G -> C (in EDS4; dbSNP:rs587779624).
/FTId=VAR_011101.
VARIANT 225 225 G -> V (in EDS4; dbSNP:rs587779533).
/FTId=VAR_011102.
VARIANT 228 228 G -> E (in EDS4; dbSNP:rs587779555).
{ECO:0000269|PubMed:9036918,
ECO:0000269|Ref.51}.
/FTId=VAR_001770.
VARIANT 240 240 G -> R (in EDS4; dbSNP:rs587779468).
/FTId=VAR_011103.
VARIANT 243 243 G -> V (in EDS4; dbSNP:rs587779629).
/FTId=VAR_011104.
VARIANT 249 249 G -> D (in EDS4; dbSNP:rs121912927).
/FTId=VAR_011105.
VARIANT 249 249 G -> V (in EDS4; dbSNP:rs121912927).
/FTId=VAR_011106.
VARIANT 252 252 G -> D (in EDS4; dbSNP:rs587779464).
/FTId=VAR_011107.
VARIANT 252 252 G -> R (in EDS4; dbSNP:rs587779705).
/FTId=VAR_011108.
VARIANT 252 252 G -> V (in EDS4; dbSNP:rs587779464).
/FTId=VAR_011109.
VARIANT 255 255 G -> V (in EDS4; dbSNP:rs587779605).
/FTId=VAR_011110.
VARIANT 264 264 G -> R (in EDS4).
{ECO:0000269|PubMed:10923041}.
/FTId=VAR_011111.
VARIANT 267 267 G -> V (in EDS4; dbSNP:rs587779427).
/FTId=VAR_011112.
VARIANT 297 297 G -> R (in EDS4).
{ECO:0000269|PubMed:12694234}.
/FTId=VAR_037007.
VARIANT 303 303 G -> R (in EDS4; dbSNP:rs121912919).
{ECO:0000269|PubMed:8514866}.
/FTId=VAR_001771.
VARIANT 321 321 G -> V (in EDS4; dbSNP:rs587779588).
/FTId=VAR_011113.
VARIANT 327 327 G -> D (in EDS4).
{ECO:0000269|PubMed:10923041}.
/FTId=VAR_011114.
VARIANT 345 345 G -> R (in EDS4; dbSNP:rs587779419).
/FTId=VAR_011115.
VARIANT 417 417 G -> R (in EDS4; dbSNP:rs587779637).
/FTId=VAR_011116.
VARIANT 420 420 G -> S (in a colorectal cancer sample;
somatic mutation; dbSNP:rs587779692).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035738.
VARIANT 444 444 G -> R (in EDS4; dbSNP:rs587779489).
/FTId=VAR_011117.
VARIANT 489 489 G -> E (in EDS4; dbSNP:rs587779476).
/FTId=VAR_011118.
VARIANT 501 501 G -> R (in EDS4; dbSNP:rs587779523).
/FTId=VAR_011119.
VARIANT 519 519 G -> V (in EDS4).
/FTId=VAR_011120.
VARIANT 534 534 G -> E (in dbSNP:rs41263744).
/FTId=VAR_055665.
VARIANT 540 540 G -> R (in EDS4; dbSNP:rs587779584).
{ECO:0000269|PubMed:9036918,
ECO:0000269|Ref.51}.
/FTId=VAR_001772.
VARIANT 549 549 G -> E (in EDS4; dbSNP:rs587779679).
/FTId=VAR_011121.
VARIANT 552 552 G -> E (in EDS4; dbSNP:rs121912928).
/FTId=VAR_011122.
VARIANT 567 567 G -> E (in EDS4).
{ECO:0000269|PubMed:8884076}.
/FTId=VAR_001773.
VARIANT 582 582 G -> S (in EDS4; dbSNP:rs121912923).
{ECO:0000269|PubMed:8990011}.
/FTId=VAR_001774.
VARIANT 588 588 G -> D (in EDS4; dbSNP:rs587779691).
/FTId=VAR_011123.
VARIANT 602 602 P -> T (in dbSNP:rs35795890).
{ECO:0000269|PubMed:8255472}.
/FTId=VAR_001775.
VARIANT 635 635 P -> L. {ECO:0000269|PubMed:8255472}.
/FTId=VAR_001776.
VARIANT 636 636 G -> R (in EDS4; dbSNP:rs587779522).
/FTId=VAR_011124.
VARIANT 657 657 G -> E (in EDS4; dbSNP:rs587779699).
/FTId=VAR_011125.
VARIANT 660 660 G -> D (in EDS4; dbSNP:rs587779493).
/FTId=VAR_011126.
VARIANT 666 666 G -> D (in EDS4; dbSNP:rs121912921).
{ECO:0000269|PubMed:8664902}.
/FTId=VAR_001777.
VARIANT 668 668 P -> T (in dbSNP:rs1801183).
{ECO:0000269|PubMed:8514866}.
/FTId=VAR_011127.
VARIANT 679 679 A -> T (in dbSNP:rs41263773).
{ECO:0000269|PubMed:18272325}.
/FTId=VAR_055666.
VARIANT 686 686 P -> A (in dbSNP:rs41263775).
/FTId=VAR_055667.
VARIANT 698 698 A -> T (in dbSNP:rs1800255).
{ECO:0000269|PubMed:18272325,
ECO:0000269|PubMed:2235526}.
/FTId=VAR_001778.
VARIANT 699 699 G -> R (in EDS4; dbSNP:rs587779668).
/FTId=VAR_011128.
VARIANT 726 726 G -> R (in EDS4; dbSNP:rs587779638).
{ECO:0000269|PubMed:9452103,
ECO:0000269|Ref.3}.
/FTId=VAR_001779.
VARIANT 738 738 G -> S (in EDS4; dbSNP:rs121912925).
/FTId=VAR_011129.
VARIANT 738 738 G -> V (in EDS4; dbSNP:rs587779615).
/FTId=VAR_011130.
VARIANT 744 744 G -> V (in EDS4; dbSNP:rs587779697).
/FTId=VAR_011131.
VARIANT 756 756 G -> E (in EDS4).
{ECO:0000269|PubMed:7912131}.
/FTId=VAR_001780.
VARIANT 762 762 G -> C (in EDS4).
{ECO:0000269|PubMed:8884076}.
/FTId=VAR_001781.
VARIANT 786 786 G -> R (in EDS4; dbSNP:rs113485686).
{ECO:0000269|PubMed:2243125}.
/FTId=VAR_001782.
VARIANT 804 804 G -> S (in EDS3; dbSNP:rs121912920).
{ECO:0000269|PubMed:7833919}.
/FTId=VAR_001783.
VARIANT 828 828 G -> R (in EDS4).
{ECO:0000269|PubMed:8411057}.
/FTId=VAR_001784.
VARIANT 828 828 G -> W (in EDS4; dbSNP:rs587779486).
/FTId=VAR_011132.
VARIANT 830 838 Missing (in EDS4).
{ECO:0000269|PubMed:1370809}.
/FTId=VAR_037008.
VARIANT 852 852 G -> C (in EDS4; dbSNP:rs587779690).
/FTId=VAR_011133.
VARIANT 879 879 G -> V (in EDS4; dbSNP:rs587779645).
/FTId=VAR_011134.
VARIANT 882 882 G -> D (in EDS4; dbSNP:rs587779622).
/FTId=VAR_011135.
VARIANT 900 900 G -> D (in EDS4; dbSNP:rs587779599).
/FTId=VAR_011136.
VARIANT 903 903 G -> E (in EDS4; dbSNP:rs587779505).
/FTId=VAR_011137.
VARIANT 909 909 G -> D (in EDS4).
{ECO:0000269|PubMed:8680408}.
/FTId=VAR_001785.
VARIANT 909 909 G -> V (in EDS4; dbSNP:rs587779483).
/FTId=VAR_011138.
VARIANT 918 918 G -> E (in EDS4; dbSNP:rs587779662).
/FTId=VAR_011139.
VARIANT 924 924 G -> C (in EDS4; dbSNP:rs587779471).
/FTId=VAR_011140.
VARIANT 936 936 G -> R (in EDS4; dbSNP:rs587779566).
{ECO:0000269|PubMed:9036918,
ECO:0000269|Ref.51}.
/FTId=VAR_001786.
VARIANT 936 936 G -> S (in EDS4).
/FTId=VAR_001787.
VARIANT 939 939 G -> D (in EDS4; dbSNP:rs112978464).
{ECO:0000269|PubMed:8680408}.
/FTId=VAR_001788.
VARIANT 942 942 G -> E (in EDS4; dbSNP:rs587779517).
/FTId=VAR_011141.
VARIANT 957 957 G -> S (in EDS4; severe variant;
dbSNP:rs121912913).
{ECO:0000269|PubMed:2492273}.
/FTId=VAR_001789.
VARIANT 960 960 G -> V (in EDS4; severe variant;
dbSNP:rs121912922).
{ECO:0000269|PubMed:7749417}.
/FTId=VAR_001790.
VARIANT 966 966 G -> V (in EDS4; dbSNP:rs587779571).
/FTId=VAR_011142.
VARIANT 972 972 G -> A (in EDS4; dbSNP:rs587779559).
/FTId=VAR_011143.
VARIANT 984 984 G -> T (in EDS4; requires 2 nucleotide
substitutions).
/FTId=VAR_011144.
VARIANT 996 996 G -> E (in EDS4; dbSNP:rs587779576).
{ECO:0000269|Ref.51}.
/FTId=VAR_001791.
VARIANT 999 999 G -> R (in EDS4; dbSNP:rs587779548).
/FTId=VAR_011145.
VARIANT 1011 1011 G -> E (in EDS4; dbSNP:rs587779552).
/FTId=VAR_011146.
VARIANT 1014 1014 G -> E (in EDS4; dbSNP:rs121912916).
{ECO:0000269|PubMed:1352273}.
/FTId=VAR_001792.
VARIANT 1032 1032 G -> V (in EDS4; dbSNP:rs587779428).
/FTId=VAR_011147.
VARIANT 1035 1035 G -> C (in EDS4; dbSNP:rs587779704).
/FTId=VAR_011148.
VARIANT 1044 1044 G -> D (in EDS4).
{ECO:0000269|PubMed:11168790}.
/FTId=VAR_011149.
VARIANT 1050 1050 G -> D (in EDS4; mild variant;
dbSNP:rs121912914).
{ECO:0000269|PubMed:2808425}.
/FTId=VAR_001793.
VARIANT 1050 1050 G -> V (in EDS4; dbSNP:rs121912914).
{ECO:0000269|PubMed:12786757}.
/FTId=VAR_011150.
VARIANT 1071 1071 G -> V (in EDS4; dbSNP:rs587779709).
{ECO:0000269|Ref.51}.
/FTId=VAR_001794.
VARIANT 1077 1077 G -> V (in EDS4; dbSNP:rs121912915).
{ECO:0000269|PubMed:1895316}.
/FTId=VAR_001795.
VARIANT 1089 1089 G -> D (in EDS4; dbSNP:rs587779672).
/FTId=VAR_011151.
VARIANT 1098 1098 G -> D (in EDS4).
{ECO:0000269|PubMed:10923041}.
/FTId=VAR_011152.
VARIANT 1098 1098 G -> V (in EDS4; dbSNP:rs587779614).
/FTId=VAR_011153.
VARIANT 1101 1101 G -> E (in EDS4; dbSNP:rs121912924).
{ECO:0000269|PubMed:9147870}.
/FTId=VAR_001796.
VARIANT 1104 1104 G -> A (in EDS4). {ECO:0000269|Ref.51}.
/FTId=VAR_001797.
VARIANT 1161 1161 G -> V (in EDS4; dbSNP:rs587779473).
/FTId=VAR_011154.
VARIANT 1164 1164 G -> E (in EDS4; dbSNP:rs587779431).
/FTId=VAR_011155.
VARIANT 1164 1164 G -> R (in EDS4; dbSNP:rs587779553).
/FTId=VAR_011156.
VARIANT 1164 1164 G -> S (in spondyloepiphyseal dysplasia).
/FTId=VAR_001798.
VARIANT 1167 1167 G -> V (in EDS4; dbSNP:rs587779578).
{ECO:0000269|Ref.46}.
/FTId=VAR_001799.
VARIANT 1170 1170 G -> D (in EDS4; dbSNP:rs587779465).
{ECO:0000269|PubMed:8884076,
ECO:0000269|Ref.46}.
/FTId=VAR_001800.
VARIANT 1170 1170 G -> V (in EDS4; dbSNP:rs587779465).
/FTId=VAR_011157.
VARIANT 1173 1173 G -> E (in EDS4; dbSNP:rs121912918).
{ECO:0000269|PubMed:10923041,
ECO:0000269|PubMed:1357232,
ECO:0000269|Ref.46}.
/FTId=VAR_001801.
VARIANT 1173 1173 G -> R (in EDS4; Gottron type acrogeria;
dbSNP:rs587779521).
{ECO:0000269|PubMed:10819545}.
/FTId=VAR_011158.
VARIANT 1176 1176 G -> V (in EDS4; severe).
{ECO:0000269|PubMed:8019562}.
/FTId=VAR_001802.
VARIANT 1179 1179 G -> R (in EDS4; dbSNP:rs587779574).
/FTId=VAR_011159.
VARIANT 1182 1182 G -> E (in EDS4; dbSNP:rs111505097).
{ECO:0000269|Ref.51}.
/FTId=VAR_001803.
VARIANT 1185 1185 G -> D (in EDS4; severe variant;
dbSNP:rs121912917).
{ECO:0000269|PubMed:1496983}.
/FTId=VAR_001804.
VARIANT 1185 1185 G -> V (in EDS4; dbSNP:rs121912917).
{ECO:0000269|Ref.51}.
/FTId=VAR_001805.
VARIANT 1188 1188 G -> E (in EDS4; severe variant;
dbSNP:rs112456072).
{ECO:0000269|PubMed:8098182,
ECO:0000269|Ref.51}.
/FTId=VAR_001806.
VARIANT 1188 1188 G -> R (in EDS4; dbSNP:rs587779504).
{ECO:0000269|Ref.51}.
/FTId=VAR_001807.
VARIANT 1205 1205 I -> V (in dbSNP:rs2271683).
{ECO:0000269|PubMed:18272325}.
/FTId=VAR_020012.
VARIANT 1353 1353 H -> Q (in dbSNP:rs1516446).
{ECO:0000269|PubMed:11566270,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:18272325,
ECO:0000269|PubMed:2579949,
ECO:0000269|PubMed:2764886,
ECO:0000269|PubMed:3357782,
ECO:0000269|Ref.6}.
/FTId=VAR_030115.
VARIANT 1434 1434 R -> C (in a colorectal cancer sample;
somatic mutation; dbSNP:rs747324731).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035739.
CONFLICT 163 163 G -> GG (in Ref. 10; CAA33387).
{ECO:0000305}.
CONFLICT 168 168 G -> V (in Ref. 11; AA sequence).
{ECO:0000305}.
CONFLICT 226 228 Missing (in Ref. 11; AA sequence).
{ECO:0000305}.
CONFLICT 241 241 E -> D (in Ref. 10; CAA33387).
{ECO:0000305}.
CONFLICT 278 278 T -> A (in Ref. 11; AA sequence).
{ECO:0000305}.
CONFLICT 293 295 NGA -> DGS (in Ref. 11; AA sequence).
{ECO:0000305}.
CONFLICT 401 401 A -> L (in Ref. 15; AA sequence).
{ECO:0000305}.
CONFLICT 409 409 L -> P (in Ref. 15; AA sequence).
{ECO:0000305}.
CONFLICT 472 472 E -> D (in Ref. 10; CAA33387).
{ECO:0000305}.
CONFLICT 488 490 PGF -> LGS (in Ref. 10; CAA33387).
{ECO:0000305}.
CONFLICT 589 589 A -> E (in Ref. 15; AA sequence).
{ECO:0000305}.
CONFLICT 614 614 T -> Y (in Ref. 10; CAA33387).
{ECO:0000305}.
CONFLICT 635 635 P -> R (in Ref. 10; CAA33387).
{ECO:0000305}.
CONFLICT 664 664 D -> E (in Ref. 10; CAA33387).
{ECO:0000305}.
CONFLICT 676 676 D -> N (in Ref. 16; AA sequence).
{ECO:0000305}.
CONFLICT 803 803 T -> P (in Ref. 15; AA sequence).
{ECO:0000305}.
CONFLICT 896 896 S -> A (in Ref. 18; AA sequence).
{ECO:0000305}.
CONFLICT 980 980 S -> A (in Ref. 22; AA sequence).
{ECO:0000305}.
CONFLICT 985 989 ANGLS -> PSGQN (in Ref. 22; AA sequence).
{ECO:0000305}.
CONFLICT 1019 1019 D -> Y (in Ref. 20; CAA29886).
{ECO:0000305}.
CONFLICT 1067 1067 S -> P (in Ref. 15; AA sequence).
{ECO:0000305}.
CONFLICT 1070 1070 A -> P (in Ref. 15; AA sequence).
{ECO:0000305}.
CONFLICT 1097 1097 T -> P (in Ref. 22; AA sequence).
{ECO:0000305}.
CONFLICT 1153 1154 TS -> AT (in Ref. 22; AA sequence).
{ECO:0000305}.
CONFLICT 1156 1156 H -> S (in Ref. 22; AA sequence).
{ECO:0000305}.
CONFLICT 1184 1184 P -> S (in Ref. 10; CAA33387).
{ECO:0000305}.
CONFLICT 1203 1203 A -> P (in Ref. 10; CAA33387).
{ECO:0000305}.
CONFLICT 1210 1210 G -> A (in Ref. 10; CAA33387).
{ECO:0000305}.
CONFLICT 1222 1222 D -> P (in Ref. 26; AAA52002).
{ECO:0000305}.
CONFLICT 1235 1235 M -> I (in Ref. 26; AAA52002).
{ECO:0000305}.
CONFLICT 1241 1241 V -> A (in Ref. 20; CAA29886 and 23;
CAA25879). {ECO:0000305}.
CONFLICT 1274 1274 S -> T (in Ref. 26; AAA52002).
{ECO:0000305}.
CONFLICT 1332 1332 M -> I (in Ref. 26; AAA52002).
{ECO:0000305}.
CONFLICT 1357 1357 L -> P (in Ref. 26; AAA52002).
{ECO:0000305}.
HELIX 1236 1249 {ECO:0000244|PDB:4AK3}.
STRAND 1253 1257 {ECO:0000244|PDB:4AE2}.
HELIX 1262 1268 {ECO:0000244|PDB:4AE2}.
STRAND 1274 1279 {ECO:0000244|PDB:4AE2}.
HELIX 1286 1288 {ECO:0000244|PDB:4AE2}.
STRAND 1290 1295 {ECO:0000244|PDB:4AE2}.
TURN 1296 1299 {ECO:0000244|PDB:4AE2}.
STRAND 1300 1303 {ECO:0000244|PDB:4AE2}.
STRAND 1305 1307 {ECO:0000244|PDB:4AE2}.
STRAND 1309 1313 {ECO:0000244|PDB:4AE2}.
STRAND 1320 1322 {ECO:0000244|PDB:4AK3}.
HELIX 1328 1331 {ECO:0000244|PDB:4AE2}.
STRAND 1339 1341 {ECO:0000244|PDB:4AEJ}.
STRAND 1343 1345 {ECO:0000244|PDB:4AK3}.
HELIX 1347 1360 {ECO:0000244|PDB:4AE2}.
STRAND 1364 1374 {ECO:0000244|PDB:4AE2}.
TURN 1381 1384 {ECO:0000244|PDB:4AE2}.
STRAND 1391 1393 {ECO:0000244|PDB:4AE2}.
STRAND 1395 1397 {ECO:0000244|PDB:4AE2}.
STRAND 1399 1404 {ECO:0000244|PDB:4AE2}.
HELIX 1406 1408 {ECO:0000244|PDB:4AK3}.
STRAND 1411 1415 {ECO:0000244|PDB:4AE2}.
STRAND 1422 1434 {ECO:0000244|PDB:4AE2}.
HELIX 1436 1438 {ECO:0000244|PDB:4AE2}.
STRAND 1443 1445 {ECO:0000244|PDB:4AE2}.
STRAND 1455 1465 {ECO:0000244|PDB:4AE2}.
SEQUENCE 1466 AA; 138564 MW; B904B4E05E17D339 CRC64;
MMSFVQKGSW LLLALLHPTI ILAQQEAVEG GCSHLGQSYA DRDVWKPEPC QICVCDSGSV
LCDDIICDDQ ELDCPNPEIP FGECCAVCPQ PPTAPTRPPN GQGPQGPKGD PGPPGIPGRN
GDPGIPGQPG SPGSPGPPGI CESCPTGPQN YSPQYDSYDV KSGVAVGGLA GYPGPAGPPG
PPGPPGTSGH PGSPGSPGYQ GPPGEPGQAG PSGPPGPPGA IGPSGPAGKD GESGRPGRPG
ERGLPGPPGI KGPAGIPGFP GMKGHRGFDG RNGEKGETGA PGLKGENGLP GENGAPGPMG
PRGAPGERGR PGLPGAAGAR GNDGARGSDG QPGPPGPPGT AGFPGSPGAK GEVGPAGSPG
SNGAPGQRGE PGPQGHAGAQ GPPGPPGING SPGGKGEMGP AGIPGAPGLM GARGPPGPAG
ANGAPGLRGG AGEPGKNGAK GEPGPRGERG EAGIPGVPGA KGEDGKDGSP GEPGANGLPG
AAGERGAPGF RGPAGPNGIP GEKGPAGERG APGPAGPRGA AGEPGRDGVP GGPGMRGMPG
SPGGPGSDGK PGPPGSQGES GRPGPPGPSG PRGQPGVMGF PGPKGNDGAP GKNGERGGPG
GPGPQGPPGK NGETGPQGPP GPTGPGGDKG DTGPPGPQGL QGLPGTGGPP GENGKPGEPG
PKGDAGAPGA PGGKGDAGAP GERGPPGLAG APGLRGGAGP PGPEGGKGAA GPPGPPGAAG
TPGLQGMPGE RGGLGSPGPK GDKGEPGGPG ADGVPGKDGP RGPTGPIGPP GPAGQPGDKG
EGGAPGLPGI AGPRGSPGER GETGPPGPAG FPGAPGQNGE PGGKGERGAP GEKGEGGPPG
VAGPPGGSGP AGPPGPQGVK GERGSPGGPG AAGFPGARGL PGPPGSNGNP GPPGPSGSPG
KDGPPGPAGN TGAPGSPGVS GPKGDAGQPG EKGSPGAQGP PGAPGPLGIA GITGARGLAG
PPGMPGPRGS PGPQGVKGES GKPGANGLSG ERGPPGPQGL PGLAGTAGEP GRDGNPGSDG
LPGRDGSPGG KGDRGENGSP GAPGAPGHPG PPGPVGPAGK SGDRGESGPA GPAGAPGPAG
SRGAPGPQGP RGDKGETGER GAAGIKGHRG FPGNPGAPGS PGPAGQQGAI GSPGPAGPRG
PVGPSGPPGK DGTSGHPGPI GPPGPRGNRG ERGSEGSPGH PGQPGPPGPP GAPGPCCGGV
GAAAIAGIGG EKAGGFAPYY GDEPMDFKIN TDEIMTSLKS VNGQIESLIS PDGSRKNPAR
NCRDLKFCHP ELKSGEYWVD PNQGCKLDAI KVFCNMETGE TCISANPLNV PRKHWWTDSS
AEKKHVWFGE SMDGGFQFSY GNPELPEDVL DVHLAFLRLL SSRASQNITY HCKNSIAYMD
QASGNVKKAL KLMGSNEGEF KAEGNSKFTY TVLEDGCTKH TGEWSKTVFE YRTRKAVRLP
IVDIAPYDIG GPDQEFGVDV GPVCFL


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