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Collagen alpha-1(V) chain

 CO5A1_HUMAN             Reviewed;        1838 AA.
P20908; Q15094; Q5SUX4;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
13-SEP-2005, sequence version 3.
27-SEP-2017, entry version 192.
RecName: Full=Collagen alpha-1(V) chain;
Flags: Precursor;
Name=COL5A1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 556-565.
PubMed=2071595;
Takahara K., Seto Y., Okasawa K., Okamoto N., Noda A., Yaoi Y.,
Kato I.;
"Complete primary structure of human collagen alpha 1 (V) chain.";
J. Biol. Chem. 266:13124-13129(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1722213;
Greenspan D.S., Cheng W., Hoffman G.G.;
"The pro-alpha-1(V) collagen chain: complete primary structure,
distribution of expression, and comparison with the pro-alpha-1(XI)
collagen chain.";
J. Biol. Chem. 266:24727-24733(1991).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[4]
PROTEIN SEQUENCE OF 621-822, AND HYDROXYLATION.
TISSUE=Chorioamniotic membrane;
PubMed=2496661; DOI=10.1016/0003-9861(89)90262-2;
Seyer J.M., Kang A.H.;
"Covalent structure of collagen: amino acid sequence of three cyanogen
bromide-derived peptides from human alpha 1(V) collagen chain.";
Arch. Biochem. Biophys. 271:120-129(1989).
[5]
PROTEIN SEQUENCE OF 823-950, AND HEPARIN-BINDING.
PubMed=2203476; DOI=10.1016/0304-4165(90)90108-9;
Yaoi Y., Hashimoto K., Koitabashi H., Takahara K., Ito M., Kato I.;
"Primary structure of the heparin-binding site of type V collagen.";
Biochim. Biophys. Acta 1035:139-145(1990).
[6]
PROTEIN SEQUENCE OF 556-571.
TISSUE=Placenta;
PubMed=1571108;
Mann K.;
"Isolation of the alpha 3-chain of human type V collagen and
characterization by partial sequencing.";
Biol. Chem. Hoppe-Seyler 373:69-75(1992).
[7]
PROTEIN SEQUENCE OF 565-576; 756-772; 1012-1029; 1219-1232 AND
1465-1477.
TISSUE=Chorioamniotic membrane;
PubMed=8181482; DOI=10.1111/j.1432-1033.1994.tb18815.x;
Moradi-Ameli M., Rousseau J.C., Kleman J.P., Champliaud M.-F.,
Boutillon M.-M., Bernillon J., Wallach J.M., van der Rest M.;
"Diversity in the processing events at the N-terminus of type-V
collagen.";
Eur. J. Biochem. 221:987-995(1994).
[8]
INTERACTION WITH CSPG4.
PubMed=9099729; DOI=10.1074/jbc.272.16.10769;
Tillet E., Ruggiero F., Nishiyama A., Stallcup W.B.;
"The membrane-spanning proteoglycan NG2 binds to collagens V and VI
through the central nonglobular domain of its core protein.";
J. Biol. Chem. 272:10769-10776(1997).
[9]
DISEASE, AND VARIANT EDS SER-1639.
PubMed=9042913;
de Paepe A., Nuytinck L., Hausser I., Anton-Lamprecht I.,
Naeyaert J.-M.;
"Mutations in the COL5A1 gene are causal in the Ehlers-Danlos
syndromes I and II.";
Am. J. Hum. Genet. 60:547-554(1997).
[10]
VARIANT ASN-229, AND ASSOCIATION WITH INCREASED RISK OF CERVICAL
ARTERY DISSECTION.
PubMed=10471441; DOI=10.1161/01.STR.30.9.1887;
Grond-Ginsbach C., Weber R., Haas J., Orberk E., Kunz S., Busse O.,
Hausser I., Brandt T., Wildemann B.;
"Mutations in the COL5A1 coding sequence are not common in patients
with spontaneous cervical artery dissections.";
Stroke 30:1887-1890(1999).
[11]
VARIANTS EDS SER-530 AND ASP-1489.
PubMed=10602121;
DOI=10.1002/(SICI)1096-8628(20000103)90:1<72::AID-AJMG13>3.0.CO;2-C;
Giunta C., Steinmann B.;
"Compound heterozygosity for a disease-causing G1489E and disease-
modifying G530S substitution in COL5A1 of a patient with the classical
type of Ehlers-Danlos syndrome: an explanation of intrafamilial
variability?";
Am. J. Med. Genet. 90:72-79(2000).
[12]
ERRATUM.
Giunta C., Steinmann B.;
Am. J. Med. Genet. 93:342-342(2000).
[13]
VARIANT EDS SER-530.
PubMed=11992482; DOI=10.1002/ajmg.10373;
Giunta C., Nuytinck L., Raghunath M., Hausser I., De Paepe A.,
Steinmann B.;
"Homozygous Gly530Ser substitution in COL5A1 causes mild classical
Ehlers-Danlos syndrome.";
Am. J. Med. Genet. 109:284-290(2002).
[14]
VARIANTS EDS SER-530 AND CYS-1486, AND VARIANTS ASP-114; ASN-192;
SER-393 AND SER-951.
PubMed=15580559; DOI=10.1002/humu.20107;
Malfait F., Coucke P., Symoens S., Loeys B., Nuytinck L., De Paepe A.;
"The molecular basis of classic Ehlers-Danlos syndrome: a
comprehensive study of biochemical and molecular findings in 48
unrelated patients.";
Hum. Mutat. 25:28-37(2005).
[15]
VARIANTS EDS ARG-25 AND PRO-25, AND CHARACTERIZATION OF VARIANTS EDS
ARG-25 AND PRO-25.
PubMed=18972565; DOI=10.1002/humu.20887;
Symoens S., Malfait F., Renard M., Andre J., Hausser I., Loeys B.,
Coucke P., De Paepe A.;
"COL5A1 signal peptide mutations interfere with protein secretion and
cause classic Ehlers-Danlos syndrome.";
Hum. Mutat. 30:E395-E403(2009).
[16]
VARIANT LEU-908.
PubMed=21248752; DOI=10.1038/nature09639;
Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P.,
Davies H., Jones D., Lin M.L., Teague J., Bignell G., Butler A.,
Cho J., Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C.,
Jia M., Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A.,
Mudie L., Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S.,
Kahnoski R.J., Anema J., Tuveson D.A., Perez-Mancera P.A.,
Mustonen V., Fischer A., Adams D.J., Rust A., Chan-On W., Subimerb C.,
Dykema K., Furge K., Campbell P.J., Teh B.T., Stratton M.R.,
Futreal P.A.;
"Exome sequencing identifies frequent mutation of the SWI/SNF complex
gene PBRM1 in renal carcinoma.";
Nature 469:539-542(2011).
[17]
VARIANTS VAL-863 AND MET-1140.
PubMed=26477546; DOI=10.1016/j.ajhg.2015.09.009;
Care4Rare Canada Consortium;
Srour M., Hamdan F.F., McKnight D., Davis E., Mandel H.,
Schwartzentruber J., Martin B., Patry L., Nassif C.,
Dionne-Laporte A., Ospina L.H., Lemyre E., Massicotte C.,
Laframboise R., Maranda B., Labuda D., Decarie J.C., Rypens F.,
Goldsher D., Fallet-Bianco C., Soucy J.F., Laberge A.M., Maftei C.,
Boycott K., Brais B., Boucher R.M., Rouleau G.A., Katsanis N.,
Majewski J., Elpeleg O., Kukolich M.K., Shalev S., Michaud J.L.;
"Joubert Syndrome in French Canadians and Identification of Mutations
in CEP104.";
Am. J. Hum. Genet. 97:744-753(2015).
-!- FUNCTION: Type V collagen is a member of group I collagen
(fibrillar forming collagen). It is a minor connective tissue
component of nearly ubiquitous distribution. Type V collagen binds
to DNA, heparan sulfate, thrombospondin, heparin, and insulin.
-!- SUBUNIT: Trimers of two alpha 1(V) and one alpha 2(V) chains in
most tissues and trimers of one alpha 1(V), one alpha 2(V), and
one alpha 3(V) chains in placenta. Interacts with CSPG4.
{ECO:0000269|PubMed:9099729}.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
-!- 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: Prolines at the third position of the tripeptide repeating
unit (G-X-Y) are hydroxylated in some or all of the chains.
{ECO:0000269|PubMed:2496661}.
-!- PTM: Sulfated on 40% of tyrosines.
-!- DISEASE: Ehlers-Danlos syndrome, classic type (EDS) [MIM:130000]:
A connective tissue disorder characterized by hyperextensible
skin, atrophic cutaneous scars due to tissue fragility and joint
hyperlaxity. {ECO:0000269|PubMed:10602121,
ECO:0000269|PubMed:11992482, ECO:0000269|PubMed:15580559,
ECO:0000269|PubMed:18972565, ECO:0000269|PubMed:9042913}. 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}.
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EMBL; D90279; BAA14323.1; -; mRNA.
EMBL; M76729; AAA59993.1; -; mRNA.
EMBL; AL591890; CAI15483.1; -; Genomic_DNA.
EMBL; AL603650; CAI15483.1; JOINED; Genomic_DNA.
EMBL; AL645768; CAI15483.1; JOINED; Genomic_DNA.
EMBL; AL645768; CAI17261.1; -; Genomic_DNA.
EMBL; AL591890; CAI17261.1; JOINED; Genomic_DNA.
EMBL; AL603650; CAI17261.1; JOINED; Genomic_DNA.
EMBL; AL603650; CAI39859.1; -; Genomic_DNA.
EMBL; AL591890; CAI39859.1; JOINED; Genomic_DNA.
EMBL; AL645768; CAI39859.1; JOINED; Genomic_DNA.
CCDS; CCDS6982.1; -.
PIR; S18802; CGHU1V.
RefSeq; NP_000084.3; NM_000093.4.
UniGene; Hs.210283; -.
PDB; 1A89; Model; -; A/B/C=904-924.
PDB; 1A9A; Model; -; A/C=904-924.
PDBsum; 1A89; -.
PDBsum; 1A9A; -.
ProteinModelPortal; P20908; -.
SMR; P20908; -.
BioGrid; 107686; 24.
IntAct; P20908; 10.
STRING; 9606.ENSP00000360882; -.
ChEMBL; CHEMBL2364188; -.
iPTMnet; P20908; -.
PhosphoSitePlus; P20908; -.
DMDM; 85687376; -.
EPD; P20908; -.
MaxQB; P20908; -.
PaxDb; P20908; -.
PeptideAtlas; P20908; -.
PRIDE; P20908; -.
Ensembl; ENST00000371817; ENSP00000360882; ENSG00000130635.
GeneID; 1289; -.
KEGG; hsa:1289; -.
UCSC; uc004cfe.5; human.
CTD; 1289; -.
DisGeNET; 1289; -.
EuPathDB; HostDB:ENSG00000130635.15; -.
GeneCards; COL5A1; -.
GeneReviews; COL5A1; -.
H-InvDB; HIX0008519; -.
HGNC; HGNC:2209; COL5A1.
HPA; HPA030769; -.
MalaCards; COL5A1; -.
MIM; 120215; gene.
MIM; 130000; phenotype.
neXtProt; NX_P20908; -.
OpenTargets; ENSG00000130635; -.
Orphanet; 90309; Ehlers-Danlos syndrome type 1.
Orphanet; 90318; Ehlers-Danlos syndrome type 2.
PharmGKB; PA26724; -.
eggNOG; KOG3544; Eukaryota.
eggNOG; ENOG410XNMM; LUCA.
GeneTree; ENSGT00840000129673; -.
HOGENOM; HOG000085654; -.
HOVERGEN; HBG004933; -.
InParanoid; P20908; -.
KO; K19721; -.
OMA; PIGVVQM; -.
PhylomeDB; P20908; -.
TreeFam; TF323987; -.
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-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-419037; NCAM1 interactions.
Reactome; R-HSA-8874081; MET activates PTK2 signaling.
Reactome; R-HSA-8948216; Collagen chain trimerization.
ChiTaRS; COL5A1; human.
GeneWiki; Collagen,_type_V,_alpha_1; -.
GenomeRNAi; 1289; -.
PMAP-CutDB; P20908; -.
PRO; PR:P20908; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000130635; -.
CleanEx; HS_COL5A1; -.
ExpressionAtlas; P20908; baseline and differential.
Genevisible; P20908; HS.
GO; GO:0005604; C:basement membrane; IEA:Ensembl.
GO; GO:0005588; C:collagen type V trimer; IMP:UniProtKB.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031012; C:extracellular matrix; IMP:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005201; F:extracellular matrix structural constituent; IEA:Ensembl.
GO; GO:0008201; F:heparin binding; IDA:UniProtKB.
GO; GO:0005178; F:integrin binding; NAS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0048407; F:platelet-derived growth factor binding; IDA:MGI.
GO; GO:0043394; F:proteoglycan binding; IPI:UniProtKB.
GO; GO:0001568; P:blood vessel development; IEA:Ensembl.
GO; GO:0007155; P:cell adhesion; IMP:UniProtKB.
GO; GO:0016477; P:cell migration; IMP:UniProtKB.
GO; GO:0032964; P:collagen biosynthetic process; IMP:UniProtKB.
GO; GO:0030574; P:collagen catabolic process; TAS:Reactome.
GO; GO:0030199; P:collagen fibril organization; IMP:UniProtKB.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0048592; P:eye morphogenesis; IMP:UniProtKB.
GO; GO:0003007; P:heart morphogenesis; IEA:Ensembl.
GO; GO:0045112; P:integrin biosynthetic process; IMP:UniProtKB.
GO; GO:1903225; P:negative regulation of endodermal cell differentiation; IDA:UniProtKB.
GO; GO:0051128; P:regulation of cellular component organization; IEA:Ensembl.
GO; GO:0043588; P:skin development; IMP:UniProtKB.
GO; GO:0097435; P:supramolecular fiber organization; IMP:UniProtKB.
GO; GO:0035989; P:tendon development; IEA:Ensembl.
GO; GO:0035313; P:wound healing, spreading of epidermal cells; IMP:UniProtKB.
Gene3D; 3.90.215.10; -; 1.
InterPro; IPR008160; Collagen.
InterPro; IPR013320; ConA-like_dom.
InterPro; IPR000885; Fib_collagen_C.
InterPro; IPR014716; Fibrinogen_a/b/g_C_1.
InterPro; IPR001791; Laminin_G.
Pfam; PF01410; COLFI; 1.
Pfam; PF01391; Collagen; 5.
ProDom; PD002078; Fib_collagen_C; 1.
SMART; SM00038; COLFI; 1.
SMART; SM00282; LamG; 1.
SMART; SM00210; TSPN; 1.
SUPFAM; SSF49899; SSF49899; 1.
PROSITE; PS51461; NC1_FIB; 1.
1: Evidence at protein level;
3D-structure; Calcium; Collagen; Complete proteome;
Direct protein sequencing; Disease mutation; Disulfide bond;
Ehlers-Danlos syndrome; Extracellular matrix; Heparin-binding;
Hydroxylation; Metal-binding; Polymorphism; Reference proteome;
Repeat; Secreted; Signal; Sulfation.
SIGNAL 1 37 {ECO:0000255}.
CHAIN 38 1605 Collagen alpha-1(V) chain.
/FTId=PRO_0000005756.
PROPEP 1606 1838 C-terminal propeptide.
/FTId=PRO_0000005757.
DOMAIN 72 244 Laminin G-like.
DOMAIN 1609 1837 Fibrillar collagen NC1.
{ECO:0000255|PROSITE-ProRule:PRU00793}.
REGION 231 443 Nonhelical region.
REGION 444 558 Interrupted collagenous region.
REGION 559 1570 Triple-helical region.
REGION 1571 1605 Nonhelical region.
METAL 1657 1657 Calcium. {ECO:0000250}.
METAL 1659 1659 Calcium. {ECO:0000250}.
METAL 1660 1660 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 1662 1662 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 1665 1665 Calcium. {ECO:0000250}.
MOD_RES 234 234 Sulfotyrosine. {ECO:0000255}.
MOD_RES 236 236 Sulfotyrosine. {ECO:0000255}.
MOD_RES 240 240 Sulfotyrosine. {ECO:0000255}.
MOD_RES 262 262 Sulfotyrosine. {ECO:0000255}.
MOD_RES 263 263 Sulfotyrosine. {ECO:0000255}.
MOD_RES 338 338 Sulfotyrosine. {ECO:0000255}.
MOD_RES 340 340 Sulfotyrosine. {ECO:0000255}.
MOD_RES 346 346 Sulfotyrosine. {ECO:0000255}.
MOD_RES 347 347 Sulfotyrosine. {ECO:0000255}.
MOD_RES 416 416 Sulfotyrosine. {ECO:0000255}.
MOD_RES 417 417 Sulfotyrosine. {ECO:0000255}.
MOD_RES 420 420 Sulfotyrosine. {ECO:0000255}.
MOD_RES 421 421 Sulfotyrosine. {ECO:0000255}.
MOD_RES 570 570 Hydroxyproline.
{ECO:0000269|PubMed:2496661}.
MOD_RES 576 576 Hydroxyproline.
{ECO:0000269|PubMed:2496661}.
MOD_RES 621 621 Hydroxyproline.
{ECO:0000269|PubMed:2496661}.
MOD_RES 627 627 5-hydroxylysine.
{ECO:0000269|PubMed:2496661}.
MOD_RES 639 639 Hydroxyproline.
{ECO:0000269|PubMed:2496661}.
MOD_RES 642 642 5-hydroxylysine.
{ECO:0000269|PubMed:2496661}.
MOD_RES 648 648 Hydroxyproline.
{ECO:0000269|PubMed:2496661}.
MOD_RES 654 654 Hydroxyproline.
{ECO:0000269|PubMed:2496661}.
MOD_RES 657 657 Hydroxyproline.
{ECO:0000269|PubMed:2496661}.
MOD_RES 675 675 Hydroxyproline.
{ECO:0000269|PubMed:2496661}.
MOD_RES 678 678 Hydroxyproline.
{ECO:0000269|PubMed:2496661}.
MOD_RES 680 680 Hydroxyproline.
{ECO:0000269|PubMed:2496661}.
MOD_RES 686 686 Hydroxyproline.
{ECO:0000269|PubMed:2496661}.
MOD_RES 690 690 Hydroxyproline.
{ECO:0000269|PubMed:2496661}.
MOD_RES 696 696 Hydroxyproline.
{ECO:0000269|PubMed:2496661}.
MOD_RES 705 705 Hydroxyproline.
{ECO:0000269|PubMed:2496661}.
MOD_RES 708 708 5-hydroxylysine.
{ECO:0000269|PubMed:2496661}.
MOD_RES 717 717 Hydroxyproline.
{ECO:0000269|PubMed:2496661}.
MOD_RES 720 720 Hydroxyproline.
{ECO:0000269|PubMed:2496661}.
MOD_RES 726 726 Hydroxyproline.
{ECO:0000269|PubMed:2496661}.
MOD_RES 732 732 Hydroxyproline.
{ECO:0000269|PubMed:2496661}.
MOD_RES 744 744 5-hydroxylysine.
{ECO:0000269|PubMed:2496661}.
MOD_RES 750 750 Hydroxyproline.
{ECO:0000269|PubMed:2496661}.
MOD_RES 756 756 Hydroxyproline.
{ECO:0000269|PubMed:2496661}.
MOD_RES 762 762 Hydroxyproline.
{ECO:0000269|PubMed:2496661}.
MOD_RES 765 765 Hydroxyproline.
{ECO:0000269|PubMed:2496661}.
MOD_RES 771 771 Hydroxyproline.
{ECO:0000269|PubMed:2496661}.
MOD_RES 774 774 5-hydroxylysine.
{ECO:0000269|PubMed:2496661}.
MOD_RES 780 780 Hydroxyproline.
{ECO:0000269|PubMed:2496661}.
MOD_RES 789 789 Hydroxyproline.
{ECO:0000269|PubMed:2496661}.
MOD_RES 795 795 5-hydroxylysine.
{ECO:0000269|PubMed:2496661}.
MOD_RES 804 804 5-hydroxylysine.
{ECO:0000269|PubMed:2496661}.
MOD_RES 807 807 5-hydroxylysine.
{ECO:0000269|PubMed:2496661}.
MOD_RES 810 810 5-hydroxylysine.
{ECO:0000269|PubMed:2496661}.
MOD_RES 816 816 Hydroxyproline.
{ECO:0000269|PubMed:2496661}.
MOD_RES 819 819 5-hydroxylysine.
{ECO:0000269|PubMed:2496661}.
MOD_RES 834 834 Hydroxyproline.
{ECO:0000269|PubMed:2496661}.
MOD_RES 846 846 5-hydroxylysine.
{ECO:0000269|PubMed:2496661}.
MOD_RES 861 861 Hydroxyproline.
{ECO:0000269|PubMed:2496661}.
MOD_RES 864 864 5-hydroxylysine.
{ECO:0000269|PubMed:2496661}.
MOD_RES 870 870 Hydroxyproline.
{ECO:0000269|PubMed:2496661}.
MOD_RES 873 873 Hydroxyproline.
{ECO:0000269|PubMed:2496661}.
MOD_RES 876 876 Hydroxyproline.
{ECO:0000269|PubMed:2496661}.
MOD_RES 882 882 5-hydroxylysine.
{ECO:0000269|PubMed:2496661}.
MOD_RES 888 888 Hydroxyproline.
{ECO:0000269|PubMed:2496661}.
MOD_RES 891 891 Hydroxyproline.
{ECO:0000269|PubMed:2496661}.
MOD_RES 897 897 5-hydroxylysine.
{ECO:0000269|PubMed:2496661}.
MOD_RES 903 903 Hydroxyproline.
{ECO:0000269|PubMed:2496661}.
MOD_RES 906 906 Hydroxyproline.
{ECO:0000269|PubMed:2496661}.
MOD_RES 930 930 Hydroxyproline.
{ECO:0000269|PubMed:2496661}.
MOD_RES 945 945 Hydroxyproline.
{ECO:0000269|PubMed:2496661}.
MOD_RES 1017 1017 Hydroxyproline.
{ECO:0000269|PubMed:2496661}.
MOD_RES 1020 1020 Hydroxyproline.
{ECO:0000269|PubMed:2496661}.
MOD_RES 1023 1023 Hydroxyproline.
{ECO:0000269|PubMed:2496661}.
MOD_RES 1029 1029 Hydroxyproline.
{ECO:0000269|PubMed:2496661}.
MOD_RES 1221 1221 Hydroxyproline.
{ECO:0000269|PubMed:2496661}.
MOD_RES 1224 1224 Hydroxyproline.
{ECO:0000269|PubMed:2496661}.
MOD_RES 1467 1467 Hydroxyproline.
{ECO:0000269|PubMed:2496661}.
MOD_RES 1470 1470 Hydroxyproline.
{ECO:0000269|PubMed:2496661}.
MOD_RES 1601 1601 Sulfotyrosine. {ECO:0000255}.
MOD_RES 1604 1604 Sulfotyrosine. {ECO:0000255}.
DISULFID 1639 1671 {ECO:0000255|PROSITE-ProRule:PRU00793}.
DISULFID 1645 1645 Interchain (with C-1662).
{ECO:0000255|PROSITE-ProRule:PRU00793}.
DISULFID 1662 1662 Interchain (with C-1645).
{ECO:0000255|PROSITE-ProRule:PRU00793}.
DISULFID 1680 1835 {ECO:0000255|PROSITE-ProRule:PRU00793}.
DISULFID 1746 1789 {ECO:0000255|PROSITE-ProRule:PRU00793}.
VARIANT 25 25 L -> P (in EDS; not or less efficiently
secreted into the extracellular matrix).
{ECO:0000269|PubMed:18972565}.
/FTId=VAR_057902.
VARIANT 25 25 L -> R (in EDS; not or less efficiently
secreted into the extracellular matrix).
{ECO:0000269|PubMed:18972565}.
/FTId=VAR_057903.
VARIANT 114 114 A -> D (unclassified mutation;
dbSNP:rs147589613).
{ECO:0000269|PubMed:15580559}.
/FTId=VAR_057904.
VARIANT 192 192 D -> N (unclassified mutation;
dbSNP:rs138579182).
{ECO:0000269|PubMed:15580559}.
/FTId=VAR_057905.
VARIANT 229 229 D -> N (associated with increased risk of
cervical artery dissection).
{ECO:0000269|PubMed:10471441}.
/FTId=VAR_057906.
VARIANT 393 393 P -> S (unclassified mutation).
{ECO:0000269|PubMed:15580559}.
/FTId=VAR_057907.
VARIANT 530 530 G -> S (in EDS; dbSNP:rs61735045).
{ECO:0000269|PubMed:10602121,
ECO:0000269|PubMed:11992482,
ECO:0000269|PubMed:15580559}.
/FTId=VAR_015412.
VARIANT 863 863 E -> V (found in a patient with Joubert
syndrome; unknown pathological
significance; dbSNP:rs139788610).
{ECO:0000269|PubMed:26477546}.
/FTId=VAR_075702.
VARIANT 908 908 P -> L (found in a renal cell carcinoma
case; somatic mutation;
dbSNP:rs772211736).
{ECO:0000269|PubMed:21248752}.
/FTId=VAR_064702.
VARIANT 951 951 N -> S (unclassified mutation;
dbSNP:rs61736966).
{ECO:0000269|PubMed:15580559}.
/FTId=VAR_057908.
VARIANT 1140 1140 V -> M (found in a patient with Joubert
syndrome; unknown pathological
significance; dbSNP:rs149616140).
{ECO:0000269|PubMed:26477546}.
/FTId=VAR_075703.
VARIANT 1486 1486 G -> C (in EDS).
{ECO:0000269|PubMed:15580559}.
/FTId=VAR_057909.
VARIANT 1489 1489 G -> D (in EDS).
{ECO:0000269|PubMed:10602121}.
/FTId=VAR_015413.
VARIANT 1639 1639 C -> S (in EDS; dbSNP:rs80338764).
{ECO:0000269|PubMed:9042913}.
/FTId=VAR_001808.
CONFLICT 82 83 QL -> HV (in Ref. 2; AAA59993).
{ECO:0000305}.
CONFLICT 390 390 A -> R (in Ref. 2; AAA59993).
{ECO:0000305}.
CONFLICT 641 641 E -> G (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 650 650 P -> L (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 663 663 R -> E (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 668 668 E -> Q (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 677 677 E -> K (in Ref. 1; BAA14323).
{ECO:0000305}.
CONFLICT 677 677 E -> Q (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 684 684 L -> P (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 692 699 PPGPPGVT -> VTGEPGAP (in Ref. 4; AA
sequence). {ECO:0000305}.
CONFLICT 727 727 G -> Q (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 741 741 P -> L (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 747 747 L -> Q (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 753 753 P -> A (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 759 759 D -> N (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 776 777 GQ -> QK (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 849 855 GGPNGDP -> IGPPGPR (in Ref. 5; AA
sequence). {ECO:0000305}.
CONFLICT 894 894 N -> D (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 1295 1299 LPGEG -> PSGRS (in Ref. 1; BAA14323).
{ECO:0000305}.
CONFLICT 1554 1554 K -> R (in Ref. 1; BAA14323).
{ECO:0000305}.
CONFLICT 1813 1813 V -> A (in Ref. 2; AAA59993).
{ECO:0000305}.
SEQUENCE 1838 AA; 183560 MW; 8F18AB0B91B3A0C7 CRC64;
MDVHTRWKAR SALRPGAPLL PPLLLLLLWA PPPSRAAQPA DLLKVLDFHN LPDGITKTTG
FCATRRSSKG PDVAYRVTKD AQLSAPTKQL YPASAFPEDF SILTTVKAKK GSQAFLVSIY
NEQGIQQIGL ELGRSPVFLY EDHTGKPGPE DYPLFRGINL SDGKWHRIAL SVHKKNVTLI
LDCKKKTTKF LDRSDHPMID INGIIVFGTR ILDEEVFEGD IQQLLFVSDH RAAYDYCEHY
SPDCDTAVPD TPQSQDPNPD EYYTEGDGEG ETYYYEYPYY EDPEDLGKEP TPSKKPVEAA
KETTEVPEEL TPTPTEAAPM PETSEGAGKE EDVGIGDYDY VPSEDYYTPS PYDDLTYGEG
EENPDQPTDP GAGAEIPTST ADTSNSSNPA PPPGEGADDL EGEFTEETIR NLDENYYDPY
YDPTSSPSEI GPGMPANQDT IYEGIGGPRG EKGQKGEPAI IEPGMLIEGP PGPEGPAGLP
GPPGTMGPTG QVGDPGERGP PGRPGLPGAD GLPGPPGTML MLPFRFGGGG DAGSKGPMVS
AQESQAQAIL QQARLALRGP AGPMGLTGRP GPVGPPGSGG LKGEPGDVGP QGPRGVQGPP
GPAGKPGRRG RAGSDGARGM PGQTGPKGDR GFDGLAGLPG EKGHRGDPGP SGPPGPPGDD
GERGDDGEVG PRGLPGEPGP RGLLGPKGPP GPPGPPGVTG MDGQPGPKGN VGPQGEPGPP
GQQGNPGAQG LPGPQGAIGP PGEKGPLGKP GLPGMPGADG PPGHPGKEGP PGEKGGQGPP
GPQGPIGYPG PRGVKGADGI RGLKGTKGEK GEDGFPGFKG DMGIKGDRGE IGPPGPRGED
GPEGPKGRGG PNGDPGPLGP PGEKGKLGVP GLPGYPGRQG PKGSIGFPGF PGANGEKGGR
GTPGKPGPRG QRGPTGPRGE RGPRGITGKP GPKGNSGGDG PAGPPGERGP NGPQGPTGFP
GPKGPPGPPG KDGLPGHPGQ RGETGFQGKT GPPGPPGVVG PQGPTGETGP MGERGHPGPP
GPPGEQGLPG LAGKEGTKGD PGPAGLPGKD GPPGLRGFPG DRGLPGPVGA LGLKGNEGPP
GPPGPAGSPG ERGPAGAAGP IGIPGRPGPQ GPPGPAGEKG APGEKGPQGP AGRDGLQGPV
GLPGPAGPVG PPGEDGDKGE IGEPGQKGSK GDKGEQGPPG PTGPQGPIGQ PGPSGADGEP
GPRGQQGLFG QKGDEGPRGF PGPPGPVGLQ GLPGPPGEKG ETGDVGQMGP PGPPGPRGPS
GAPGADGPQG PPGGIGNPGA VGEKGEPGEA GEPGLPGEGG PPGPKGERGE KGESGPSGAA
GPPGPKGPPG DDGPKGSPGP VGFPGDPGPP GEPGPAGQDG PPGDKGDDGE PGQTGSPGPT
GEPGPSGPPG KRGPPGPAGP EGRQGEKGAK GEAGLEGPPG KTGPIGPQGA PGKPGPDGLR
GIPGPVGEQG LPGSPGPDGP PGPMGPPGLP GLKGDSGPKG EKGHPGLIGL IGPPGEQGEK
GDRGLPGPQG SSGPKGEQGI TGPSGPIGPP GPPGLPGPPG PKGAKGSSGP TGPKGEAGHP
GPPGPPGPPG EVIQPLPIQA SRTRRNIDAS QLLDDGNGEN YVDYADGMEE IFGSLNSLKL
EIEQMKRPLG TQQNPARTCK DLQLCHPDFP DGEYWVDPNQ GCSRDSFKVY CNFTAGGSTC
VFPDKKSEGA RITSWPKENP GSWFSEFKRG KLLSYVDAEG NPVGVVQMTF LRLLSASAHQ
NVTYHCYQSV AWQDAATGSY DKALRFLGSN DEEMSYDNNP YIRALVDGCA TKKGYQKTVL
EIDTPKVEQV PIVDIMFNDF GEASQKFGFE VGPACFMG


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