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Database: UniProt
Entry: H0VHD0_CAVPO
LinkDB: H0VHD0_CAVPO
Original site: H0VHD0_CAVPO 
ID   H0VHD0_CAVPO            Unreviewed;      1287 AA.
AC   H0VHD0;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 2.
DT   24-JAN-2024, entry version 70.
DE   SubName: Full=Collagen type I alpha 2 chain {ECO:0000313|Ensembl:ENSCPOP00000009557.3};
GN   Name=COL1A2 {ECO:0000313|Ensembl:ENSCPOP00000009557.3};
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000009557.3, ECO:0000313|Proteomes:UP000005447};
RN   [1] {ECO:0000313|Proteomes:UP000005447}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSCPOP00000009557.3}
RP   IDENTIFICATION.
RC   STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000009557.3};
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
CC   -!- FUNCTION: Type I collagen is a member of group I collagen (fibrillar
CC       forming collagen). {ECO:0000256|ARBA:ARBA00003647}.
CC   -!- SUBUNIT: Trimers of one alpha 2(I) and two alpha 1(I) chains.
CC       {ECO:0000256|ARBA:ARBA00011231}.
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DR   EMBL; AAKN02016852; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 10141.ENSCPOP00000009557; -.
DR   Ensembl; ENSCPOT00000010743.3; ENSCPOP00000009557.3; ENSCPOG00000010646.4.
DR   VEuPathDB; HostDB:ENSCPOG00000010646; -.
DR   GeneTree; ENSGT00940000155639; -.
DR   HOGENOM; CLU_001074_2_3_1; -.
DR   InParanoid; H0VHD0; -.
DR   OMA; SFYWIDP; -.
DR   TreeFam; TF344135; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   Bgee; ENSCPOG00000010646; Expressed in uterine cervix and 12 other cell types or tissues.
DR   GO; GO:0005584; C:collagen type I trimer; IEA:Ensembl.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; IEA:InterPro.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0048407; F:platelet-derived growth factor binding; IEA:Ensembl.
DR   GO; GO:0002020; F:protease binding; IEA:Ensembl.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; IEA:Ensembl.
DR   GO; GO:0046332; F:SMAD binding; IEA:Ensembl.
DR   GO; GO:0001568; P:blood vessel development; IEA:Ensembl.
DR   GO; GO:0030282; P:bone mineralization; IEA:Ensembl.
DR   GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
DR   GO; GO:0030199; P:collagen fibril organization; IEA:Ensembl.
DR   GO; GO:0032963; P:collagen metabolic process; IEA:Ensembl.
DR   GO; GO:0085029; P:extracellular matrix assembly; IEA:Ensembl.
DR   GO; GO:0070208; P:protein heterotrimerization; IEA:Ensembl.
DR   GO; GO:0008217; P:regulation of blood pressure; IEA:Ensembl.
DR   GO; GO:0007266; P:Rho protein signal transduction; IEA:Ensembl.
DR   GO; GO:0001501; P:skeletal system development; IEA:Ensembl.
DR   GO; GO:0043589; P:skin morphogenesis; IEA:Ensembl.
DR   GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR   Gene3D; 2.60.120.1000; -; 1.
DR   InterPro; IPR008160; Collagen.
DR   InterPro; IPR000885; Fib_collagen_C.
DR   PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR   PANTHER; PTHR24023:SF966; ZMP:0000000760; 1.
DR   Pfam; PF01410; COLFI; 1.
DR   Pfam; PF01391; Collagen; 10.
DR   SMART; SM00038; COLFI; 1.
DR   PROSITE; PS51461; NC1_FIB; 1.
PE   4: Predicted;
KW   Collagen {ECO:0000256|ARBA:ARBA00023119};
KW   Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005447};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..1287
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012836224"
FT   DOMAIN          1054..1287
FT                   /note="Fibrillar collagen NC1"
FT                   /evidence="ECO:0000259|PROSITE:PS51461"
FT   REGION          28..686
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          734..1048
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..70
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1287 AA;  123053 MW;  EC306289ECF98DA7 CRC64;
     MLSFVDTRTV LLLAVTSCLA TCQSKCLRCG GEDRGPRGER GPPGSPGLDG EDGPPGPPGP
     PGPPGPPGLG GGLMGPRGPP GAVGAPGPQG FQGPAGEPGE PGQTGPAGSR GPAGPPGKAG
     EDGHPGKPGR PGERGVVGPQ GARGFPGTPG LPGFKGPRGH NGMDGLKGQA GAPGVKGEPG
     APGENGTPGQ AGARGLPGER GRVGAPGPTG ARGSDGSVGP VGPAGPIGAA GPPGFPGAPG
     AKGEIGPVGN PGPSGPAGPR GEVGLPGLSG PVGPPGNPGA NGLPGSKGAT VNGPPCAPSQ
     GLPGVAGAPG LPGPRGIPGP VGAAGATGAR GLVGSAGAQG PPGPSGEEGK RGPNGEVGSA
     GPPGPPGLRG SPGSRGLPGA DGRSGVMGPP GSRGATGPAG VRGPNGDTGR PGEPGLMGPR
     GLPGSPGNAG PAGKEGPMGL PGIDGRPGPI GPAGPRGEAG NIGFPGPKGP TGDPGKSGDK
     GHPGLAGARG APGPDGNNGA QGPPGPQGVQ GGKGEQGPAG PPGFQGLPGP SGPAGEVGKP
     GERGLPGEFG LPGPAGARGE RGPPGESGAV GPAGPIGNRG PSGPPGPDGN KGEPGVVGAP
     GTAGASGPGG LPGERGAAGI PGGKGEKGET GHRGEPGNTG RDGARGAPGA IGAPGPAGAT
     GDRGEAGPAG PAGPAGPRGS PVSKNLGHLD TKTLKLLDVH GLRVAKGERG EVGPAGPNGF
     AGPAVNQSEN NATATVCSPQ GAGITGPPGP PGPAGKEGIR GPRGDQGPVG RTGDTGAGGP
     PGFAGEKGPS GEPGTAGPPG TPGPQGLLGA PGILGLPGSR GERGLPGIAG ASGEPGPLGL
     AGPPGARGPP GNVGSPGVNG PPGEAGRDGN PGNDGPPGRD GQPGHKGERG YPGNIGPVGA
     AGAPGPHGPV GPTGKHGNRG EPGPAGSVGP VGAVGPRGPS GPQGIRGDKG EVGDKGPRGL
     PGIKGHNGLQ GLPGLALISE MGSGKDGHAG QPGPVGPAGV RGSQGSQGPA GPPGPPGPPG
     PAGASGGGYD FGFDGDFYRA DQPRSAPALR PKDYEVDATL KSLNNQIETL LTPEGSRKNP
     ARTCRDLRLS HPEWSSGYYW IDPNQGCTMD AIKVYCDFST GQTCIRAQPE SIMPKSWYKN
     SKPKKHIWLG ETINGGSQFE YNMEGVTSKE MATQLAFMRL LANHASQNIT YHCRNSIAYM
     DEETGSLNKA VILQGSNDVE LIPEGNSRFT YTVLVDGCSK KTNEWEKTII EYKTNKPSRL
     PFLDIAPLDI GDADQEIRVD VGPVCFK
//
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