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Collagen alpha-1(VIII) chain (Endothelial collagen) [Cleaved into: Vastatin]

 CO8A1_HUMAN             Reviewed;         744 AA.
P27658; D3DN42; Q53XI6; Q96D07;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
11-JUL-2002, sequence version 2.
27-SEP-2017, entry version 169.
RecName: Full=Collagen alpha-1(VIII) chain;
AltName: Full=Endothelial collagen;
Contains:
RecName: Full=Vastatin;
Flags: Precursor;
Name=COL8A1; Synonyms=C3orf7;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2029894; DOI=10.1111/j.1432-1033.1991.tb15951.x;
Muragaki Y., Mattei M.-G., Yamaguchi N., Olsen B.R., Ninomiya Y.;
"The complete primary structure of the human alpha 1 (VIII) chain and
assignment of its gene (COL8A1) to chromosome 3.";
Eur. J. Biochem. 197:615-622(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
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).
[5]
TISSUE SPECIFICITY.
PubMed=2376131; DOI=10.3109/03008209009152157;
Kittelberger R., Davis P.F., Flynn D.W., Greenhill N.S.;
"Distribution of type VIII collagen in tissues: an immunohistochemical
study.";
Connect. Tissue Res. 24:303-318(1990).
[6]
PROTEOLYTIC PROCESSING.
PubMed=1515454; DOI=10.1016/0925-4439(92)90103-T;
Kittelberger R., Neale T.J., Francky K.T., Greenhill N.S.,
Gibson G.J.;
"Cleavage of type VIII collagen by human neutrophil elastase.";
Biochim. Biophys. Acta 1139:295-299(1992).
[7]
TISSUE SPECIFICITY, AND POSSIBLE FUNCTION.
PubMed=7734329;
Ruger B., Dunbar P.R., Hasan Q., Sawada H., Kittelberger R.,
Greenhill N., Neale T.J.;
"Human mast cells produce type VIII collagen in vivo.";
Int. J. Exp. Pathol. 75:397-404(1994).
[8]
TISSUE SPECIFICITY.
PubMed=10686422; DOI=10.1016/S0945-053X(99)00053-0;
Greenhill N.S., Ruger B.M., Hasan Q., Davis P.F.;
"The alpha1(VIII) and alpha2(VIII) collagen chains form two distinct
homotrimeric proteins in vivo.";
Matrix Biol. 19:19-28(2000).
[9]
FUNCTION OF VASTATIN.
PubMed=11708810; DOI=10.1006/bbrc.2001.5970;
Xu R., Yao Z.-Y., Xin L., Zhang Q., Li T.-P., Gan R.-B.;
"NC1 domain of human type VIII collagen (alpha 1) inhibits bovine
aortic endothelial cell proliferation and causes cell apoptosis.";
Biochem. Biophys. Res. Commun. 289:264-268(2001).
[10]
SUBUNIT.
PubMed=14990571; DOI=10.1074/jbc.M305805200;
Stephan S., Sherratt M.J., Hodson N., Shuttleworth C.A., Kielty C.M.;
"Expression and supramolecular assembly of recombinant alpha1(viii)
and alpha2(viii) collagen homotrimers.";
J. Biol. Chem. 279:21469-21477(2004).
[11]
INDUCTION.
PubMed=17888087; DOI=10.1111/j.1365-2362.2007.01864.x;
Gerth J., Cohen C.D., Hopfer U., Lindenmeyer M.T., Sommer M.,
Grone H.J., Wolf G.;
"Collagen type VIII expression in human diabetic nephropathy.";
Eur. J. Clin. Invest. 37:767-773(2007).
-!- FUNCTION: Macromolecular component of the subendothelium. Major
component of the Descemet's membrane (basement membrane) of
corneal endothelial cells. Also component of the endothelia of
blood vessels. Necessary for migration and proliferation of
vascular smooth muscle cells and thus, has a potential role in the
maintenance of vessel wall integrity and structure, in particular
in atherogenesis. {ECO:0000269|PubMed:11708810}.
-!- FUNCTION: Vastatin, the C-terminal fragment comprising the NC1
domain, inhibits aortic endothelial cell proliferation and causes
cell apoptosis. {ECO:0000269|PubMed:11708810}.
-!- SUBUNIT: Homotrimers, or heterotrimers in association with alpha
2(VIII) type collagens. Four homotrimers can form a tetrhedron
stabilized by central interacting C-terminal NC1 trimers.
{ECO:0000269|PubMed:14990571}.
-!- INTERACTION:
Q02930-3:CREB5; NbExp=5; IntAct=EBI-747133, EBI-10192698;
A8MQ03:CYSRT1; NbExp=4; IntAct=EBI-747133, EBI-3867333;
P49639:HOXA1; NbExp=4; IntAct=EBI-747133, EBI-740785;
Q0VD86:INCA1; NbExp=5; IntAct=EBI-747133, EBI-6509505;
Q53G59:KLHL12; NbExp=3; IntAct=EBI-747133, EBI-740929;
Q6A162:KRT40; NbExp=3; IntAct=EBI-747133, EBI-10171697;
P60409:KRTAP10-7; NbExp=3; IntAct=EBI-747133, EBI-10172290;
P60410:KRTAP10-8; NbExp=5; IntAct=EBI-747133, EBI-10171774;
Q6PEX3:KRTAP26-1; NbExp=4; IntAct=EBI-747133, EBI-3957672;
Q9BYQ4:KRTAP9-2; NbExp=3; IntAct=EBI-747133, EBI-1044640;
Q96MT4:LINC01600; NbExp=4; IntAct=EBI-747133, EBI-12804988;
Q6IA69:NADSYN1; NbExp=4; IntAct=EBI-747133, EBI-748610;
Q7Z3S9:NOTCH2NL; NbExp=7; IntAct=EBI-747133, EBI-945833;
P32242:OTX1; NbExp=4; IntAct=EBI-747133, EBI-740446;
Q04864:REL; NbExp=3; IntAct=EBI-747133, EBI-307352;
Q02446:SP4; NbExp=3; IntAct=EBI-747133, EBI-10198587;
Q08AM6:VAC14; NbExp=5; IntAct=EBI-747133, EBI-2107455;
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix, basement membrane.
-!- TISSUE SPECIFICITY: Expressed primarily in the subendothelium of
large blood vessels. Also expressed in arterioles and venules in
muscle, heart, kidney, spleen, umbilical cord, liver and lung and
is also found in connective tissue layers around hair follicles,
around nerve bundles in muscle, in the dura of the optic nerve, in
cornea and sclera, and in the perichondrium of cartilaginous
tissues. In the kidney, expressed in mesangial cells, glomerular
endothelial cells, and tubular epithelial cells. Also expressed in
mast cells, and in astrocytes during the repair process. Expressed
in Descemet's membrane. Specifically expressed in peritoneal
fibroblasts and mesothelial cells. {ECO:0000269|PubMed:10686422,
ECO:0000269|PubMed:2376131, ECO:0000269|PubMed:7734329}.
-!- INDUCTION: Up-regulated during vascular injury, in atherosclerosis
and in diabetes. {ECO:0000269|PubMed:17888087}.
-!- PTM: Prolines at the third position of the tripeptide repeating
unit (G-X-Y) are hydroxylated in some or all of the chains.
-!- PTM: Proteolytically cleaved by neutrophil elastase, in vitro.
Proteolytic processing produces the C-terminal NC1 domain
fragment, vastatin. {ECO:0000269|PubMed:1515454}.
-!- MISCELLANEOUS: Four consecutive Gly-Pro-Pro triplets are present
at the C-terminus of the triple-helical region. These may provide
the high thermal stability of this region.
-----------------------------------------------------------------------
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EMBL; X57527; CAA40748.1; -; mRNA.
EMBL; BT009917; AAP88919.1; -; mRNA.
EMBL; CH471052; EAW79837.1; -; Genomic_DNA.
EMBL; CH471052; EAW79838.1; -; Genomic_DNA.
EMBL; CH471052; EAW79840.1; -; Genomic_DNA.
EMBL; BC013581; AAH13581.1; -; mRNA.
CCDS; CCDS2934.1; -.
PIR; S15435; S15435.
RefSeq; NP_001841.2; NM_001850.4.
RefSeq; NP_065084.2; NM_020351.3.
UniGene; Hs.654548; -.
UniGene; Hs.740613; -.
UniGene; Hs.740617; -.
ProteinModelPortal; P27658; -.
SMR; P27658; -.
BioGrid; 107692; 19.
IntAct; P27658; 60.
MINT; MINT-2857732; -.
STRING; 9606.ENSP00000261037; -.
iPTMnet; P27658; -.
PhosphoSitePlus; P27658; -.
BioMuta; COL8A1; -.
DMDM; 21903375; -.
EPD; P27658; -.
PaxDb; P27658; -.
PeptideAtlas; P27658; -.
PRIDE; P27658; -.
DNASU; 1295; -.
Ensembl; ENST00000261037; ENSP00000261037; ENSG00000144810.
Ensembl; ENST00000273342; ENSP00000273342; ENSG00000144810.
GeneID; 1295; -.
KEGG; hsa:1295; -.
UCSC; uc003dtg.3; human.
CTD; 1295; -.
DisGeNET; 1295; -.
EuPathDB; HostDB:ENSG00000144810.15; -.
GeneCards; COL8A1; -.
HGNC; HGNC:2215; COL8A1.
HPA; HPA053107; -.
MIM; 120251; gene.
neXtProt; NX_P27658; -.
OpenTargets; ENSG00000144810; -.
PharmGKB; PA26731; -.
eggNOG; ENOG410IE8J; Eukaryota.
eggNOG; ENOG410Y928; LUCA.
GeneTree; ENSGT00760000118830; -.
HOGENOM; HOG000085653; -.
HOVERGEN; HBG108220; -.
InParanoid; P27658; -.
OMA; TCEVPGV; -.
OrthoDB; EOG091G0L3Y; -.
PhylomeDB; P27658; -.
TreeFam; TF334029; -.
Reactome; R-HSA-1442490; Collagen degradation.
Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes.
Reactome; R-HSA-2022090; Assembly of collagen fibrils and other multimeric structures.
Reactome; R-HSA-216083; Integrin cell surface interactions.
Reactome; R-HSA-8948216; Collagen chain trimerization.
GeneWiki; Collagen,_type_VIII,_alpha_1; -.
GenomeRNAi; 1295; -.
PRO; PR:P27658; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000144810; -.
CleanEx; HS_COL8A1; -.
ExpressionAtlas; P27658; baseline and differential.
Genevisible; P27658; HS.
GO; GO:0005591; C:collagen type VIII trimer; TAS:ProtInc.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031012; C:extracellular matrix; IDA:BHF-UCL.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0048593; P:camera-type eye morphogenesis; IEA:Ensembl.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0030574; P:collagen catabolic process; TAS:Reactome.
GO; GO:0035987; P:endodermal cell differentiation; IEP:UniProtKB.
GO; GO:0050673; P:epithelial cell proliferation; IEA:Ensembl.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IEA:Ensembl.
Gene3D; 2.60.120.40; -; 1.
InterPro; IPR001073; C1q_dom.
InterPro; IPR008160; Collagen.
InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
Pfam; PF00386; C1q; 1.
Pfam; PF01391; Collagen; 2.
PRINTS; PR00007; COMPLEMNTC1Q.
SMART; SM00110; C1Q; 1.
SUPFAM; SSF49842; SSF49842; 1.
PROSITE; PS50871; C1Q; 1.
1: Evidence at protein level;
Angiogenesis; Basement membrane; Cell adhesion; Collagen;
Complete proteome; Extracellular matrix; Hydroxylation;
Reference proteome; Repeat; Secreted; Signal.
SIGNAL 1 27 {ECO:0000255}.
CHAIN 28 744 Collagen alpha-1(VIII) chain.
/FTId=PRO_0000005762.
CHAIN 572 744 Vastatin.
/FTId=PRO_0000390484.
DOMAIN 611 744 C1q. {ECO:0000255|PROSITE-
ProRule:PRU00368}.
REGION 29 117 Nonhelical region (NC2).
REGION 118 571 Triple-helical region (COL1).
REGION 572 744 Nonhelical region (NC1).
CONFLICT 262 262 P -> L (in Ref. 1; CAA40748).
{ECO:0000305}.
CONFLICT 297 297 P -> R (in Ref. 1; CAA40748).
{ECO:0000305}.
CONFLICT 344 344 P -> A (in Ref. 1; CAA40748).
{ECO:0000305}.
CONFLICT 382 382 A -> S (in Ref. 1; CAA40748).
{ECO:0000305}.
CONFLICT 388 388 P -> S (in Ref. 1; CAA40748).
{ECO:0000305}.
CONFLICT 454 454 L -> F (in Ref. 1; CAA40748).
{ECO:0000305}.
CONFLICT 464 464 A -> H (in Ref. 1; CAA40748).
{ECO:0000305}.
CONFLICT 601 601 Y -> T (in Ref. 1; CAA40748).
{ECO:0000305}.
CONFLICT 631 631 A -> G (in Ref. 1; CAA40748).
{ECO:0000305}.
SEQUENCE 744 AA; 73364 MW; 2BC1B0955DE2C9A3 CRC64;
MAVLPGPLQL LGVLLTISLS SIRLIQAGAY YGIKPLPPQI PPQMPPQIPQ YQPLGQQVPH
MPLAKDGLAM GKEMPHLQYG KEYPHLPQYM KEIQPAPRMG KEAVPKKGKE IPLASLRGEQ
GPRGEPGPRG PPGPPGLPGH GIPGIKGKPG PQGYPGVGKP GMPGMPGKPG AMGMPGAKGE
IGQKGEIGPM GIPGPQGPPG PHGLPGIGKP GGPGLPGQPG PKGDRGPKGL PGPQGLRGPK
GDKGFGMPGA PGVKGPPGMH GPPGPVGLPG VGKPGVTGFP GPQGPLGKPG APGEPGPQGP
IGVPGVQGPP GIPGIGKPGQ DGIPGQPGFP GGKGEQGLPG LPGPPGLPGI GKPGFPGPKG
DRGMGGVPGA LGPRGEKGPI GAPGIGGPPG EPGLPGIPGP MGPPGAIGFP GPKGEGGIVG
PQGPPGPKGE PGLQGFPGKP GFLGEVGPPG MRGLPGPIGP KGEAGQKGVP GLPGVPGLLG
PKGEPGIPGD QGLQGPPGIP GIGGPSGPIG PPGIPGPKGE PGLPGPPGFP GIGKPGVAGL
HGPPGKPGAL GPQGQPGLPG PPGPPGPPGP PAVMPPTPPP QGEYLPDMGL GIDGVKPPHA
YGAKKGKNGG PAYEMPAFTA ELTAPFPPVG APVKFNKLLY NGRQNYNPQT GIFTCEVPGV
YYFAYHVHCK GGNVWVALFK NNEPVMYTYD EYKKGFLDQA SGSAVLLLRP GDRVFLQMPS
EQAAGLYAGQ YVHSSFSGYL LYPM


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