CO8A1_MOUSE
ID CO8A1_MOUSE Reviewed; 744 AA.
AC Q00780; B8JJL9; Q3TWU7; Q8BGL6; Q921S8; Q9D2V4;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 3.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Collagen alpha-1(VIII) chain;
DE Contains:
DE RecName: Full=Vastatin;
DE Flags: Precursor;
GN Name=Col8a1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BALB/cJ;
RX PubMed=1499564; DOI=10.1111/j.1432-1033.1992.tb17122.x;
RA Muragaki Y., Shiota C., Inoue M., Ooshima A., Olsen B.R., Ninomiya Y.;
RT "Alpha 1(VIII)-collagen gene transcripts encode a short-chain collagen
RT polypeptide and are expressed by various epithelial, endothelial and
RT mesenchymal cells in newborn mouse tissues.";
RL Eur. J. Biochem. 207:895-902(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Corpora quadrigemina, Kidney, and Medulla oblongata;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP TISSUE SPECIFICITY, FUNCTION, AND INDUCTION.
RX PubMed=15063777; DOI=10.1016/j.bbrc.2004.03.049;
RA Hirano S., Yonezawa T., Hasegawa H., Hattori S., Greenhill N.S.,
RA Davis P.F., Sage E.H., Ninomiya Y.;
RT "Astrocytes express type VIII collagen during the repair process of brain
RT cold injury.";
RL Biochem. Biophys. Res. Commun. 317:437-443(2004).
RN [6]
RP FUNCTION.
RX PubMed=16269661; DOI=10.1161/01.atv.0000194155.96456.b7;
RA Adiguzel E., Hou G., Mulholland D., Hopfer U., Fukai N., Olsen B.,
RA Bendeck M.;
RT "Migration and growth are attenuated in vascular smooth muscle cells with
RT type VIII collagen-null alleles.";
RL Arterioscler. Thromb. Vasc. Biol. 26:56-61(2006).
RN [7]
RP TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, FUNCTION, AND INDUCTION.
RX PubMed=19401424; DOI=10.2337/db08-0183;
RA Hopfer U., Hopfer H., Meyer-Schwesinger C., Loeffler I., Fukai N.,
RA Olsen B.R., Stahl R.A., Wolf G.;
RT "Lack of type VIII collagen in mice ameliorates diabetic nephropathy.";
RL Diabetes 58:1672-1681(2009).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 573-744.
RX PubMed=12782141; DOI=10.1016/s0945-053x(02)00119-1;
RA Kvansakul M., Bogin O., Hohenester E., Yayon A.;
RT "Crystal structure of the collagen alpha1(VIII) NC1 trimer.";
RL Matrix Biol. 22:145-152(2003).
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.
CC {ECO:0000269|PubMed:15063777, ECO:0000269|PubMed:16269661,
CC ECO:0000269|PubMed:19401424}.
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 -!- TISSUE SPECIFICITY: High levels in calvarium, eye and skin of newborn
CC mice; also in various epithelial, endothelial and mesenchymal cells.
CC {ECO:0000269|PubMed:15063777, ECO:0000269|PubMed:19401424}.
CC -!- INDUCTION: Up-regulated in astrocytes during the repair process and in
CC mesangial cells in diabetic animals. {ECO:0000269|PubMed:15063777,
CC ECO:0000269|PubMed:19401424}.
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 -!- DISRUPTION PHENOTYPE: COL8A1(-)/COL8A2(-) mice exhibit decreased
CC proliferation of measngial cells, reduced phosphorylation of ERK1/2 and
CC increased p27(KIP1) expression. Diabetic COL8A1(-)/COL8A2(-) mice
CC reveal reduced mesangial expansion and cellularity and extracellular
CC matrix expansion. {ECO:0000269|PubMed:19401424}.
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DR EMBL; X66976; CAA47387.1; -; Genomic_DNA.
DR EMBL; X66977; CAA47387.1; JOINED; Genomic_DNA.
DR EMBL; AK018742; BAB31383.1; -; mRNA.
DR EMBL; AK032048; BAC27670.1; -; mRNA.
DR EMBL; AK046370; BAC32693.1; -; mRNA.
DR EMBL; AK159542; BAE35169.1; -; mRNA.
DR EMBL; CT025753; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC011061; AAH11061.1; -; mRNA.
DR CCDS; CCDS37367.1; -.
DR PIR; S23779; S23779.
DR RefSeq; NP_031765.2; NM_007739.2.
DR PDB; 1O91; X-ray; 1.90 A; A/B/C=573-744.
DR PDBsum; 1O91; -.
DR AlphaFoldDB; Q00780; -.
DR SMR; Q00780; -.
DR BioGRID; 198827; 1.
DR ComplexPortal; CPX-2967; Collagen type VIII trimer variant I.
DR ComplexPortal; CPX-2968; Collagen type VIII trimer variant 2.
DR STRING; 10090.ENSMUSP00000086745; -.
DR iPTMnet; Q00780; -.
DR PhosphoSitePlus; Q00780; -.
DR MaxQB; Q00780; -.
DR PaxDb; Q00780; -.
DR PeptideAtlas; Q00780; -.
DR PRIDE; Q00780; -.
DR ProteomicsDB; 283672; -.
DR Antibodypedia; 32194; 202 antibodies from 28 providers.
DR DNASU; 12837; -.
DR Ensembl; ENSMUST00000089332; ENSMUSP00000086745; ENSMUSG00000068196.
DR GeneID; 12837; -.
DR KEGG; mmu:12837; -.
DR UCSC; uc007znl.1; mouse.
DR CTD; 1295; -.
DR MGI; MGI:88463; Col8a1.
DR VEuPathDB; HostDB:ENSMUSG00000068196; -.
DR eggNOG; ENOG502QRFR; Eukaryota.
DR GeneTree; ENSGT00940000158272; -.
DR HOGENOM; CLU_001074_21_0_1; -.
DR InParanoid; Q00780; -.
DR OMA; KEIPMRS; -.
DR OrthoDB; 1167208at2759; -.
DR PhylomeDB; Q00780; -.
DR TreeFam; TF334029; -.
DR Reactome; R-MMU-1442490; Collagen degradation.
DR Reactome; R-MMU-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-MMU-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-MMU-216083; Integrin cell surface interactions.
DR Reactome; R-MMU-8948216; Collagen chain trimerization.
DR BioGRID-ORCS; 12837; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Col8a1; mouse.
DR EvolutionaryTrace; Q00780; -.
DR PRO; PR:Q00780; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q00780; protein.
DR Bgee; ENSMUSG00000068196; Expressed in pineal body and 230 other tissues.
DR Genevisible; Q00780; MM.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0048593; P:camera-type eye morphogenesis; IGI:MGI.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0035987; P:endodermal cell differentiation; IEA:Ensembl.
DR GO; GO:0050673; P:epithelial cell proliferation; IGI:MGI.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IDA:MGI.
DR DisProt; DP02369; -.
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; 3.
DR PRINTS; PR00007; COMPLEMNTC1Q.
DR SMART; SM00110; C1Q; 1.
DR SUPFAM; SSF49842; SSF49842; 1.
DR PROSITE; PS50871; C1Q; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Angiogenesis; Basement membrane; Cell adhesion; Collagen;
KW Extracellular matrix; Hydroxylation; Reference proteome; Repeat; Secreted;
KW Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..744
FT /note="Collagen alpha-1(VIII) chain"
FT /id="PRO_0000005763"
FT CHAIN 573..744
FT /note="Vastatin"
FT /id="PRO_0000390485"
FT DOMAIN 611..744
FT /note="C1q"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT REGION 29..118
FT /note="Nonhelical region (NC2)"
FT REGION 101..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..572
FT /note="Triple-helical region (COL1)"
FT REGION 412..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..744
FT /note="Nonhelical region (NC1)"
FT COMPBIAS 126..140
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..207
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..270
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..299
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..532
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..579
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 3
FT /note="V -> L (in Ref. 4; AAH11061)"
FT /evidence="ECO:0000305"
FT CONFLICT 6
FT /note="R -> G (in Ref. 1; CAA47387)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="H -> Y (in Ref. 1; CAA47387)"
FT /evidence="ECO:0000305"
FT CONFLICT 110
FT /note="Missing (in Ref. 1; CAA47387)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="P -> L (in Ref. 1; CAA47387)"
FT /evidence="ECO:0000305"
FT CONFLICT 314
FT /note="P -> A (in Ref. 2; BAB31383)"
FT /evidence="ECO:0000305"
FT CONFLICT 324..325
FT /note="IP -> SR (in Ref. 1; CAA47387)"
FT /evidence="ECO:0000305"
FT CONFLICT 362
FT /note="D -> H (in Ref. 1; CAA47387)"
FT /evidence="ECO:0000305"
FT CONFLICT 597
FT /note="P -> T (in Ref. 1; CAA47387)"
FT /evidence="ECO:0000305"
FT CONFLICT 635
FT /note="F -> L (in Ref. 2; BAE35169)"
FT /evidence="ECO:0000305"
FT CONFLICT 718..720
FT /note="MPS -> NPF (in Ref. 1; CAA47387)"
FT /evidence="ECO:0000305"
FT STRAND 617..622
FT /evidence="ECO:0007829|PDB:1O91"
FT STRAND 637..642
FT /evidence="ECO:0007829|PDB:1O91"
FT TURN 648..650
FT /evidence="ECO:0007829|PDB:1O91"
FT STRAND 659..680
FT /evidence="ECO:0007829|PDB:1O91"
FT STRAND 683..690
FT /evidence="ECO:0007829|PDB:1O91"
FT STRAND 698..708
FT /evidence="ECO:0007829|PDB:1O91"
FT STRAND 713..717
FT /evidence="ECO:0007829|PDB:1O91"
FT HELIX 721..723
FT /evidence="ECO:0007829|PDB:1O91"
FT STRAND 724..727
FT /evidence="ECO:0007829|PDB:1O91"
FT STRAND 734..743
FT /evidence="ECO:0007829|PDB:1O91"
SQ SEQUENCE 744 AA; 73607 MW; 88F31CD20BDC8372 CRC64;
MAVPPRPLQL LGILFIISLN SVRLIQAGAY YGIKPLPPQI PPQIPPQIPQ YQPLGQQVPH
MPLGKDGLSM GKEMPHMQYG KEYPHLPQYM KEIPPVPRMG KEVVPKKGKG EVPLASLRGE
QGPRGEPGPR GPPGPPGLPG HGMPGIKGKP GPQGYPGIGK PGMPGMPGKP GAMGMPGAKG
EIGPKGEIGP MGIPGPQGPP GPHGLPGIGK PGGPGLPGQP GAKGERGPKG PPGPPGLQGP
KGEKGFGMPG LPGLKGPPGM HGPPGPVGLP GVGKPGVTGF PGPQGPLGKP GPPGEPGPQG
LIGVPGVQGP PGMPGVGKPG QDGIPGQPGF PGGKGEQGLP GLPGPPGLPG VGKPGFPGPK
GDRGIGGVPG VLGPRGEKGP IGAPGMGGPP GEPGLPGIPG PMGPPGAIGF PGPKGEGGVV
GPQGPPGPKG EPGLQGFPGK PGFLGEVGPP GMRGLPGPIG PKGEGGHKGL PGLPGVPGLL
GPKGEPGIPG DQGLQGPPGI PGIVGPSGPI GPPGIPGPKG EPGLPGPPGF PGVGKPGVAG
LHGPPGKPGA LGPQGQPGLP GPPGPPGPPG PPAVMPTPSP QGEYLPDMGL GIDGVKPPHA
YAGKKGKHGG PAYEMPAFTA ELTVPFPPVG APVKFDKLLY NGRQNYNPQT GIFTCEVPGV
YYFAYHVHCK GGNVWVALFK NNEPMMYTYD EYKKGFLDQA SGSAVLLLRP GDQVFLQMPS
EQAAGLYAGQ YVHSSFSGYL LYPM
