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 16-SEP-2015, entry version 137. 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; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=BALB/c; 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA 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., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the 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 RT project: 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 RT brain 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 RT with 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 RT 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 CC corneal endothelial cells. Also component of the endothelia of CC blood vessels. Necessary for migration and proliferation of CC vascular smooth muscle cells and thus, has a potential role in the CC maintenance of vessel wall integrity and structure, in particular CC in atherogenesis. {ECO:0000269|PubMed:15063777, CC ECO:0000269|PubMed:16269661, ECO:0000269|PubMed:19401424}. CC -!- FUNCTION: Vastatin, the C-terminal fragment comprising the NC1 CC domain, inhibits aortic endothelial cell proliferation and causes CC cell apoptosis. {ECO:0000250}. CC -!- SUBUNIT: Homotrimers, or heterotrimers in association with alpha CC 2(VIII) type collagens. Four homotrimers can form a tetrhedron 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 CC newborn mice; also in various epithelial, endothelial and CC mesenchymal cells. {ECO:0000269|PubMed:15063777, CC ECO:0000269|PubMed:19401424}. CC -!- INDUCTION: Up-regulated in astrocytes during the repair process CC and in mesangial cells in diabetic animals. CC {ECO:0000269|PubMed:15063777, ECO:0000269|PubMed:19401424}. CC -!- PTM: Prolines at the third position of the tripeptide repeating CC unit (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 CC fragment, vastatin (By similarity). {ECO:0000250}. CC -!- DISRUPTION PHENOTYPE: COL8A1(-)/COL8A2(-) mice exhibit decreased CC proliferation of measngial cells, reduced phosphorylation of CC ERK1/2 and increased p27(KIP1) expression. Diabetic CC COL8A1(-)/COL8A2(-) mice reveal reduced mesangial expansion and CC cellularity and extracellular matrix expansion. CC {ECO:0000269|PubMed:19401424}. CC -!- SIMILARITY: Contains 1 C1q domain. {ECO:0000255|PROSITE- CC ProRule:PRU00368}. 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; 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; CAX16095.1; -; 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 UniGene; Mm.130388; -. DR PDB; 1O91; X-ray; 1.90 A; A/B/C=573-744. DR PDBsum; 1O91; -. DR ProteinModelPortal; Q00780; -. DR SMR; Q00780; 614-744. DR BioGrid; 198827; 1. DR STRING; 10090.ENSMUSP00000086745; -. DR PhosphoSite; Q00780; -. DR MaxQB; Q00780; -. DR PaxDb; Q00780; -. DR PRIDE; Q00780; -. 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 eggNOG; NOG114228; -. DR GeneTree; ENSGT00760000118830; -. DR HOGENOM; HOG000085653; -. DR HOVERGEN; HBG108220; -. DR InParanoid; Q00780; -. DR OMA; TCEVPGV; -. DR OrthoDB; EOG70ZZPW; -. 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 EvolutionaryTrace; Q00780; -. DR NextBio; 282360; -. DR PRO; PR:Q00780; -. DR Proteomes; UP000000589; Chromosome 16. DR Bgee; Q00780; -. DR CleanEx; MM_COL8A1; -. 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:0070062; C:extracellular exosome; ISO:MGI. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI. 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:0010811; P:positive regulation of cell-substrate adhesion; IDA:MGI. 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; KW Collagen; Complete proteome; Extracellular matrix; Hydroxylation; KW Reference proteome; Repeat; Secreted; Signal. FT SIGNAL 1 24 {ECO:0000255}. FT CHAIN 25 744 Collagen alpha-1(VIII) chain. FT /FTId=PRO_0000005763. FT CHAIN 573 744 Vastatin. FT /FTId=PRO_0000390485. FT DOMAIN 611 744 C1q. {ECO:0000255|PROSITE- FT ProRule:PRU00368}. FT REGION 29 118 Nonhelical region (NC2). FT REGION 119 572 Triple-helical region (COL1). FT REGION 573 744 Nonhelical region (NC1). FT CONFLICT 3 3 V -> L (in Ref. 4; AAH11061). FT {ECO:0000305}. FT CONFLICT 6 6 R -> G (in Ref. 1; CAA47387). FT {ECO:0000305}. FT CONFLICT 85 85 H -> Y (in Ref. 1; CAA47387). FT {ECO:0000305}. FT CONFLICT 110 110 Missing (in Ref. 1; CAA47387). FT {ECO:0000305}. FT CONFLICT 249 249 P -> L (in Ref. 1; CAA47387). FT {ECO:0000305}. FT CONFLICT 314 314 P -> A (in Ref. 2; BAB31383). FT {ECO:0000305}. FT CONFLICT 324 325 IP -> SR (in Ref. 1; CAA47387). FT {ECO:0000305}. FT CONFLICT 362 362 D -> H (in Ref. 1; CAA47387). FT {ECO:0000305}. FT CONFLICT 597 597 P -> T (in Ref. 1; CAA47387). FT {ECO:0000305}. FT CONFLICT 635 635 F -> L (in Ref. 2; BAE35169). FT {ECO:0000305}. FT CONFLICT 718 720 MPS -> NPF (in Ref. 1; CAA47387). FT {ECO:0000305}. FT STRAND 617 622 {ECO:0000244|PDB:1O91}. FT STRAND 637 642 {ECO:0000244|PDB:1O91}. FT TURN 648 650 {ECO:0000244|PDB:1O91}. FT STRAND 659 680 {ECO:0000244|PDB:1O91}. FT STRAND 683 690 {ECO:0000244|PDB:1O91}. FT STRAND 698 708 {ECO:0000244|PDB:1O91}. FT STRAND 713 717 {ECO:0000244|PDB:1O91}. FT HELIX 721 723 {ECO:0000244|PDB:1O91}. FT STRAND 724 727 {ECO:0000244|PDB:1O91}. FT STRAND 734 743 {ECO:0000244|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 //