GenomeNet

Database: UniProt
Entry: D4AC70_RAT
LinkDB: D4AC70_RAT
Original site: D4AC70_RAT 
ID   D4AC70_RAT              Unreviewed;       744 AA.
AC   D4AC70;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 3.
DT   27-MAR-2024, entry version 93.
DE   SubName: Full=Collagen type VIII alpha 1 chain {ECO:0000313|Ensembl:ENSRNOP00000057564.4};
GN   Name=Col8a1 {ECO:0000313|Ensembl:ENSRNOP00000057564.4,
GN   ECO:0000313|RGD:1309361};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000057564.4, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000057564.4, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000057564.4,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0000313|Ensembl:ENSRNOP00000057564.4}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000057564.4};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR   RefSeq; XP_006248270.1; XM_006248208.3.
DR   RefSeq; XP_017453500.1; XM_017598011.1.
DR   AlphaFoldDB; D4AC70; -.
DR   SMR; D4AC70; -.
DR   STRING; 10116.ENSRNOP00000057564; -.
DR   jPOST; D4AC70; -.
DR   PaxDb; 10116-ENSRNOP00000057564; -.
DR   PeptideAtlas; D4AC70; -.
DR   Ensembl; ENSRNOT00000060838.5; ENSRNOP00000057564.4; ENSRNOG00000039668.5.
DR   GeneID; 304021; -.
DR   UCSC; RGD:1309361; rat.
DR   AGR; RGD:1309361; -.
DR   CTD; 1295; -.
DR   RGD; 1309361; Col8a1.
DR   eggNOG; ENOG502QRFR; Eukaryota.
DR   GeneTree; ENSGT00940000158272; -.
DR   HOGENOM; CLU_001074_21_0_1; -.
DR   InParanoid; D4AC70; -.
DR   OMA; PMGKEMP; -.
DR   OrthoDB; 5267071at2759; -.
DR   PhylomeDB; D4AC70; -.
DR   TreeFam; TF334029; -.
DR   Reactome; R-RNO-1442490; Collagen degradation.
DR   Reactome; R-RNO-1650814; Collagen biosynthesis and modifying enzymes.
DR   Reactome; R-RNO-2022090; Assembly of collagen fibrils and other multimeric structures.
DR   Reactome; R-RNO-216083; Integrin cell surface interactions.
DR   Reactome; R-RNO-8948216; Collagen chain trimerization.
DR   Proteomes; UP000002494; Chromosome 11.
DR   Bgee; ENSRNOG00000039668; Expressed in heart and 17 other cell types or tissues.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IBA:GO_Central.
DR   GO; GO:0048593; P:camera-type eye morphogenesis; ISO:RGD.
DR   GO; GO:0035987; P:endodermal cell differentiation; ISO:RGD.
DR   GO; GO:0001935; P:endothelial cell proliferation; ISO:RGD.
DR   GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR   GO; GO:0010811; P:positive regulation of cell-substrate adhesion; ISO:RGD.
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   PANTHER; PTHR15427:SF33; EMI DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR15427; EMILIN ELASTIN MICROFIBRIL INTERFACE-LOCATED PROTEIN ELASTIN MICROFIBRIL INTERFACER; 1.
DR   Pfam; PF00386; C1q; 1.
DR   Pfam; PF01391; Collagen; 1.
DR   PRINTS; PR00007; COMPLEMNTC1Q.
DR   SMART; SM00110; C1Q; 1.
DR   SUPFAM; SSF49842; TNF-like; 1.
DR   PROSITE; PS50871; C1Q; 1.
PE   1: Evidence at protein level;
KW   Proteomics identification {ECO:0007829|PeptideAtlas:D4AC70};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..744
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003053374"
FT   DOMAIN          611..744
FT                   /note="C1q"
FT                   /evidence="ECO:0000259|PROSITE:PS50871"
FT   REGION          102..394
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          466..608
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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..583
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   744 AA;  73507 MW;  E66262CC83CBE873 CRC64;
     MAVPPRPLQL LGILFILSLS SVRLAQAGAY YGIKPLPPQI PPQIPPQIPQ YQPLGQQVPH
     MPLGKDGLSM GKEMPHMQYG KEYPHLPQYM KEIQPVPRVG KEVVPKKGKG EIPLASLRGE
     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 ALGPRGEKGP VGAPGIGGPP GEPGLPGIPG PMGPPGAIGF PGPKGEGGIV
     GPQGPPGPKG EPGLQGFPGK PGFLGEVGPP GMRGLPGPIG PKGEAGHKGL PGLPGVPGLL
     GPKGEPGIPG DQGLQGPPGI PGIAGPSGPI GPPGIPGPKG EPGLPGPPGF PGVGKPGVAG
     LHGPPGKPGA LGPQGQPGLP GPPGPPGPPG PPAVMPPTPS PQGEYLPDMG LGIDGVKPPH
     AYAGKKGKNG GPYEMPAFTA ELTVPFPPVG APVKFDKLLY NGRQNYNPQT GVFTCEVPGV
     YYFAYHVHCK GGNVWVALFK NNEPMMYTYD EYKKGFLDQA SGSAVLLLRP GDRVFLQMPS
     EQAAGLYAGQ YVHSSFSGYL LYPM
//
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