CO8A2_MOUSE
ID CO8A2_MOUSE Reviewed; 699 AA.
AC P25318; A3KFY2; Q68ED0; Q6KAQ4; Q6P1C4;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Collagen alpha-2(VIII) chain;
DE AltName: Full=Endothelial collagen;
DE Flags: Precursor;
GN Name=Col8a2;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 60-699 (ISOFORM 1).
RC TISSUE=Embryonic tail;
RX PubMed=15449545; DOI=10.1093/dnares/11.2.127;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of FLJ genes: the
RT complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified
RT by screening of terminal sequences of cDNA clones randomly sampled from
RT size-fractionated libraries.";
RL DNA Res. 11:127-135(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 530-699.
RX PubMed=2019595; DOI=10.1016/s0021-9258(20)89508-8;
RA Muragaki Y., Jacenko O., Apte S., Mattei M.-G., Ninomiya Y., Olsen B.R.;
RT "The alpha 2(VIII) collagen gene. A novel member of the short chain
RT collagen family located on the human chromosome 1.";
RL J. Biol. Chem. 266:7721-7727(1991).
RN [5]
RP TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND FUNCTION.
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).
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, ECO:0000269|PubMed:19401424}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P25318-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P25318-2; Sequence=VSP_014975;
CC -!- TISSUE SPECIFICITY: In the kidney, expressed in mesangial cells,
CC glomerular endothelial cells, and tubular epithelial cells.
CC {ECO:0000269|PubMed:19401424}.
CC -!- PTM: Proteolytically cleaved by neutrophil elastase, in vitro.
CC {ECO:0000250}.
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 -!- DISRUPTION PHENOTYPE: COL8A1(-)/COL8A2(-) mice exhibit decreased
CC proliferation of mesangial 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}.
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; AL606976; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC065148; AAH65148.1; -; mRNA.
DR EMBL; BC080317; AAH80317.1; -; mRNA.
DR EMBL; AK131153; BAD21403.1; -; mRNA.
DR EMBL; M60833; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS18649.1; -. [P25318-1]
DR PIR; B57131; B57131.
DR RefSeq; NP_955767.1; NM_199473.2. [P25318-1]
DR AlphaFoldDB; P25318; -.
DR SMR; P25318; -.
DR ComplexPortal; CPX-2967; Collagen type VIII trimer variant I.
DR ComplexPortal; CPX-2969; Collagen type VIII trimer variant 3.
DR STRING; 10090.ENSMUSP00000070270; -.
DR iPTMnet; P25318; -.
DR PhosphoSitePlus; P25318; -.
DR MaxQB; P25318; -.
DR PaxDb; P25318; -.
DR PRIDE; P25318; -.
DR ProteomicsDB; 283413; -. [P25318-1]
DR ProteomicsDB; 283414; -. [P25318-2]
DR Antibodypedia; 56213; 165 antibodies from 24 providers.
DR DNASU; 329941; -.
DR Ensembl; ENSMUST00000070132; ENSMUSP00000070270; ENSMUSG00000056174. [P25318-1]
DR GeneID; 329941; -.
DR KEGG; mmu:329941; -.
DR UCSC; uc008utd.1; mouse. [P25318-1]
DR CTD; 1296; -.
DR MGI; MGI:88464; Col8a2.
DR VEuPathDB; HostDB:ENSMUSG00000056174; -.
DR eggNOG; ENOG502QRST; Eukaryota.
DR GeneTree; ENSGT00940000154317; -.
DR HOGENOM; CLU_001074_21_0_1; -.
DR InParanoid; P25318; -.
DR OMA; IPHMKYM; -.
DR OrthoDB; 1167208at2759; -.
DR PhylomeDB; P25318; -.
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; 329941; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Col8a2; mouse.
DR PRO; PR:P25318; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P25318; protein.
DR Bgee; ENSMUSG00000056174; Expressed in humerus cartilage element and 137 other tissues.
DR ExpressionAtlas; P25318; baseline and differential.
DR Genevisible; P25318; MM.
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:0048593; P:camera-type eye morphogenesis; IGI:MGI.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0050673; P:epithelial cell proliferation; IGI:MGI.
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; 1.
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 Alternative splicing; Angiogenesis; Basement membrane; Cell adhesion;
KW Collagen; Extracellular matrix; Hydroxylation; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..699
FT /note="Collagen alpha-2(VIII) chain"
FT /id="PRO_0000005836"
FT DOMAIN 566..699
FT /note="C1q"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT REGION 25..72
FT /note="Nonhelical region (NC2)"
FT REGION 66..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 73..532
FT /note="Triple-helical region (COL1)"
FT REGION 533..699
FT /note="Nonhelical region (NC1)"
FT COMPBIAS 70..96
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..230
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..529
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 168..223
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014975"
FT CONFLICT 609
FT /note="T -> S (in Ref. 4; M60833)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 699 AA; 66943 MW; FCBD4FBB44642646 CRC64;
MQGALMPLPS LLLLLLGCGP RVSSGGGAGG AAGYAPVKYV QPMQKGPVGP PFREGKGQYL
EMPLPMLPMD LKGEPGPPGK PGPRGPPGPP GFPGKPGTGK PGVHGQPGPA GPPGFSRMGK
AGPPGLPGKV GPPGQPGLRG EPGIRGDQGL RGPPGPPGLP GPSGITVPGK PGAQGAPGPP
GFRGEPGPQG EPGPRGDRGL KGDNGVGQPG LPGAPGQAGA PGPPGLPGPA GLGKPGLDGI
PGAPGDKGDS GPPGVPGSRG EPGAVGPKGP PGVDGVGIPG AAGVPGPQGP VGAKGEPGLR
GPPGLIGPVG YGMPGKPGPK GDRGPVGAPG LLGDRGEPGE DGKPGEQGPQ GLGGPPGLPG
SAGLPGRRGP PGSKGEVGPG GPPGVPGIRG DQGPNGLAGK PGLPGERGLP GAHGPPGPTG
PKGEPGFTGR PGGPGVAGAL GQKGDLGLPG QPGLRGPSGI PGLQGPAGPI GPQGLPGLKG
EPGLPGPPGE GKVGEPGSAG PTGPPGVPGS PGLTGPPGPP GPPGPPGAPG ALDETGIAGL
HLPNGGVEGA VLGKGGKPQF GLGELSAHAT PAFTAVLTSP FPASGMPVRF DRTLYNGHSG
YNPATGIFTC PVGGVYYFAY HVHVKGTNVW VALYKNNVPA TYTYDEYKKG YLDQASGGAV
LQLRPNDQVW VQMPSDQANG LYSTEYIHSS FSGFLLCPT
