CO8A1_RABIT
ID CO8A1_RABIT Reviewed; 744 AA.
AC P14282;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Collagen alpha-1(VIII) chain;
DE AltName: Full=Endothelial collagen;
DE Contains:
DE RecName: Full=Vastatin;
DE Flags: Precursor;
GN Name=COL8A1;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2476437; DOI=10.1016/s0021-9258(18)71582-2;
RA Yamaguchi N., Benya P.D., van der Rest M., Ninomiya Y.;
RT "The cloning and sequencing of alpha 1(VIII) collagen cDNAs demonstrate
RT that type VIII collagen is a short chain collagen and contains triple-
RT helical and carboxyl-terminal non-triple-helical domains similar to those
RT of type X collagen.";
RL J. Biol. Chem. 264:16022-16029(1989).
CC -!- FUNCTION: Macromolecular component of the subendothelium. Major
CC component of the Descemet's membrane (basement membrane) of corneal
CC endothelial cells. Also a component of the endothelia of blood vessels.
CC Necessary for migration and proliferation of vascular smooth muscle
CC cells and thus, has a potential role in the maintenance of vessel wall
CC integrity and structure, in particular in atherogenesis (By
CC similarity). {ECO:0000250}.
CC -!- FUNCTION: Vastatin, the C-terminal fragment comprising the NC1 domain,
CC inhibits aortic endothelial cell proliferation and causes cell
CC apoptosis. {ECO:0000250}.
CC -!- SUBUNIT: Homotrimers, or heterotrimers in association with alpha
CC 2(VIII) type collagens. Four homotrimers can form a tetrahedron
CC stabilized by central interacting C-terminal NC1 trimers (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane.
CC -!- PTM: Prolines at the third position of the tripeptide repeating unit
CC (G-X-Y) are hydroxylated in some or all of the chains.
CC -!- PTM: Proteolytically cleaved by neutrophil elastase, in vitro.
CC Proteolytic processing produces the C-terminal NC1 domain fragment,
CC vastatin (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: 4 consecutive G-P-P tripeptides are present at the C-
CC terminus of the triple-helical region. These may provide high thermal
CC stability of this region.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; J05042; AAA31204.1; -; mRNA.
DR PIR; A34246; A34246.
DR RefSeq; NP_001076135.1; NM_001082666.1.
DR AlphaFoldDB; P14282; -.
DR SMR; P14282; -.
DR STRING; 9986.ENSOCUP00000023659; -.
DR PRIDE; P14282; -.
DR GeneID; 100009383; -.
DR KEGG; ocu:100009383; -.
DR CTD; 1295; -.
DR eggNOG; ENOG502QRFR; Eukaryota.
DR InParanoid; P14282; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.40; -; 1.
DR InterPro; IPR001073; C1q_dom.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
DR Pfam; PF00386; C1q; 1.
DR Pfam; PF01391; Collagen; 2.
DR PRINTS; PR00007; COMPLEMNTC1Q.
DR SMART; SM00110; C1Q; 1.
DR SUPFAM; SSF49842; SSF49842; 1.
DR PROSITE; PS50871; C1Q; 1.
PE 2: Evidence at transcript level;
KW Angiogenesis; Basement membrane; Cell adhesion; Collagen;
KW Extracellular matrix; Hydroxylation; Reference proteome; Repeat; Secreted;
KW Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..744
FT /note="Collagen alpha-1(VIII) chain"
FT /id="PRO_0000005764"
FT CHAIN 572..744
FT /note="Vastatin"
FT /id="PRO_0000390486"
FT DOMAIN 611..744
FT /note="C1q"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT REGION 29..117
FT /note="Nonhelical region (NC2)"
FT REGION 101..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..571
FT /note="Triple-helical region"
FT REGION 478..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..744
FT /note="Nonhelical region (NC1)"
FT COMPBIAS 125..139
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..206
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..269
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..307
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..407
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..531
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..582
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 744 AA; 73358 MW; 2A8CEF1EF8274E99 CRC64;
MAVPPGPPQL LQVLLTISLG SIRLIQAGAY YGIKPLPPQI PPQMPPQIPQ YQPLGQQVPH
MPLAKDGLTM GKEMPHAQYG KEYPHLPQYM KEVQPVPRMG KEAVPKKGKE IPLASLRGEQ
GPRGEPGPRG PPGPPGLPGQ GIPGIKGKPG PQGYPGVGKP GMPGMPGKPG AMGMPGAKGE
IGPKGEIGPM GIPGPQGPPG PHGLPGIGKP GGPGLPGQPG AKGDRGPKGP PGPPGLQGPK
GEKGFGMPGL PGLKGPPGMH GPPGPVGLPG VGKPGVTGFP GPQGPLGKPG PPGEPGPQGP
IGVPGVQGPP GLPGVGKPGQ DGIPGQPGFP GGKGEQGLPG LPGPPGLPGV GKPGFPGPKG
DRGIGGVPGA LGPRGEKGPV GAPGMGGPPG EPGLPGIPGP MGPPGAIGFP GPKGEGGIVG
PQGPPGPKGE PGLQGFPGKP GFLGEVGPPG IRGLPGPIGP KGEAGHKGLP GLPGVPGLLG
PKGEPGIPGD QGLQGPPGIP GITGPSGPIG PPGIPGPKGE PGLPGPPGFP GVGKPGVAGL
HGPPGKPGAL GPQGQPGLPG PPGPPGPPGP PAVMPPTPAP QGEYLPDMGL GIDGVKTPHA
YAAKKGKNGG PAYEMPAFTA ELTAPFPPVG APIKFDRLLY NGRQNYNPQT GIFTCEVPGV
YYFAYHVHCK GGNVWVALFK NNEPVMYTYD EYKKGFLDQA SGSAVLLLRP GDRVFLQMPS
EQAAGLYAGQ YVHSSFSGYL LYPM
