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CO8A1_CHICK
ID   CO8A1_CHICK             Reviewed;         744 AA.
AC   Q7LZR2;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Collagen alpha-1(VIII) chain;
DE   Flags: Precursor;
GN   Name=COL8A1;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Ninomiya Y., Castagnola P., Gerecke D., Gordon M.K., Jacenko O.,
RA   LuValle P., McCarthy M., Muragaki Y., Nishimura I., Oh S., Rosenblum N.,
RA   Sato N., Sugrue S., Taylor R., Vasios G., Yamaguchi N., Olsen B.R.;
RT   "The molecular biology of collagens with short triple-helical domains.";
RL   (In) Sandell L.J., Boyd C.D. (eds.);
RL   Extracellular Matrix Genes, pp.79-114, Academic Press, San Diego (1990).
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   -!- 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. {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.
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DR   PIR; S23298; S23298.
DR   AlphaFoldDB; Q7LZR2; -.
DR   SMR; Q7LZR2; -.
DR   VEuPathDB; HostDB:geneid_418378; -.
DR   VEuPathDB; HostDB:geneid_419504; -.
DR   InParanoid; Q7LZR2; -.
DR   PhylomeDB; Q7LZR2; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR   GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR   GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
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   3: Inferred from homology;
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_0000285969"
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..434
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          118..571
FT                   /note="Triple-helical region"
FT   REGION          463..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;  73372 MW;  F00822D5248A7C07 CRC64;
     MAVQPGPPQL 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 GDRVFLQNPS
     EQAAGLYAGQ YVHSSFSGYL LYPM
 
 
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