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CORA1_MOUSE
ID   CORA1_MOUSE             Reviewed;        1845 AA.
AC   Q5QNQ9; Q69Z83; Q80UA8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=Collagen alpha-1(XXVII) chain;
DE   Flags: Precursor;
GN   Name=Col27a1; Synonyms=Kiaa1870;
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 [MRNA], DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6J;
RX   PubMed=12714037; DOI=10.1016/s0945-053x(03)00007-6;
RA   Pace J.M., Corrado M., Missero C., Byers P.H.;
RT   "Identification, characterization and expression analysis of a new
RT   fibrillar collagen gene, COL27A1.";
RL   Matrix Biol. 22:3-14(2003).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 989-1845.
RC   TISSUE=Thymus;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT   The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [4]
RP   SUBCELLULAR LOCATION.
RX   PubMed=17693149; DOI=10.1016/j.bone.2007.06.024;
RA   Hjorten R., Hansen U., Underwood R.A., Telfer H.E., Fernandes R.J.,
RA   Krakow D., Sebald E., Wachsmann-Hogiu S., Bruckner P., Jacquet R.,
RA   Landis W.J., Byers P.H., Pace J.M.;
RT   "Type XXVII collagen at the transition of cartilage to bone during
RT   skeletogenesis.";
RL   Bone 41:535-542(2007).
RN   [5]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=17331945; DOI=10.1074/jbc.c700021200;
RA   Plumb D.A., Dhir V., Mironov A., Ferrara L., Poulsom R., Kadler K.E.,
RA   Thornton D.J., Briggs M.D., Boot-Handford R.P.;
RT   "Collagen XXVII is developmentally regulated and forms thin fibrillar
RT   structures distinct from those of classical vertebrate fibrillar
RT   collagens.";
RL   J. Biol. Chem. 282:12791-12795(2007).
CC   -!- FUNCTION: Plays a role during the calcification of cartilage and the
CC       transition of cartilage to bone. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000255|PROSITE-ProRule:PRU00793,
CC       ECO:0000269|PubMed:17693149}. Note=Found on some small banded collagen
CC       fibrils and filamentous meshworks.
CC   -!- TISSUE SPECIFICITY: Highly expressed in cartilage, eye and ear.
CC       {ECO:0000269|PubMed:12714037}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in 14.5 dpc in several cartilaginous
CC       structures including anlagen of several bones and the developing lungs
CC       as well as in the eye, ear and colon. First detectable at 12.5 dpc. At
CC       14.5 dpc localizes to cartilage, developing dermis, cornea, the inner
CC       limiting membrane of the retina, and major arteries of the heart. At
CC       18.5 dpc appears restricted mainly to cartilage where expression
CC       continued into adulthood. {ECO:0000269|PubMed:12714037,
CC       ECO:0000269|PubMed:17331945}.
CC   -!- DOMAIN: The C-terminal propeptide, also known as COLFI domain, have
CC       crucial roles in tissue growth and repair by controlling both the
CC       intracellular assembly of procollagen molecules and the extracellular
CC       assembly of collagen fibrils. It binds a calcium ion which is essential
CC       for its function (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the fibrillar collagen family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00793}.
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DR   EMBL; AY167568; AAN87341.2; -; mRNA.
DR   EMBL; AL683828; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL691496; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK173283; BAD32561.1; -; mRNA.
DR   CCDS; CCDS18250.1; -.
DR   RefSeq; NP_079961.3; NM_025685.3.
DR   AlphaFoldDB; Q5QNQ9; -.
DR   SMR; Q5QNQ9; -.
DR   BioGRID; 237540; 2.
DR   ComplexPortal; CPX-3030; Collagen type XXVII trimer.
DR   IntAct; Q5QNQ9; 1.
DR   STRING; 10090.ENSMUSP00000043816; -.
DR   GlyGen; Q5QNQ9; 3 sites.
DR   iPTMnet; Q5QNQ9; -.
DR   PhosphoSitePlus; Q5QNQ9; -.
DR   PaxDb; Q5QNQ9; -.
DR   PeptideAtlas; Q5QNQ9; -.
DR   PRIDE; Q5QNQ9; -.
DR   ProteomicsDB; 285266; -.
DR   Antibodypedia; 65300; 29 antibodies from 15 providers.
DR   DNASU; 373864; -.
DR   Ensembl; ENSMUST00000036300; ENSMUSP00000043816; ENSMUSG00000045672.
DR   GeneID; 373864; -.
DR   KEGG; mmu:373864; -.
DR   UCSC; uc008tfs.1; mouse.
DR   CTD; 85301; -.
DR   MGI; MGI:2672118; Col27a1.
DR   VEuPathDB; HostDB:ENSMUSG00000045672; -.
DR   eggNOG; KOG3544; Eukaryota.
DR   GeneTree; ENSGT00940000163466; -.
DR   HOGENOM; CLU_001074_19_1_1; -.
DR   InParanoid; Q5QNQ9; -.
DR   OMA; YSYPDRL; -.
DR   OrthoDB; 200318at2759; -.
DR   PhylomeDB; Q5QNQ9; -.
DR   TreeFam; TF344135; -.
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-8874081; MET activates PTK2 signaling.
DR   Reactome; R-MMU-8948216; Collagen chain trimerization.
DR   BioGRID-ORCS; 373864; 1 hit in 74 CRISPR screens.
DR   ChiTaRS; Col27a1; mouse.
DR   PRO; PR:Q5QNQ9; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; Q5QNQ9; protein.
DR   Bgee; ENSMUSG00000045672; Expressed in humerus cartilage element and 225 other tissues.
DR   ExpressionAtlas; Q5QNQ9; baseline and differential.
DR   Genevisible; Q5QNQ9; MM.
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; IBA:GO_Central.
DR   GO; GO:0005583; C:fibrillar collagen trimer; IDA:MGI.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; IDA:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030198; P:extracellular matrix organization; IMP:MGI.
DR   GO; GO:0003431; P:growth plate cartilage chondrocyte development; IMP:MGI.
DR   InterPro; IPR008160; Collagen.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000885; Fib_collagen_C.
DR   InterPro; IPR001791; Laminin_G.
DR   Pfam; PF01410; COLFI; 2.
DR   Pfam; PF01391; Collagen; 9.
DR   SMART; SM00038; COLFI; 1.
DR   SMART; SM00210; TSPN; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS51461; NC1_FIB; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Collagen; Disulfide bond; Extracellular matrix; Glycoprotein;
KW   Metal-binding; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..39
FT                   /evidence="ECO:0000255"
FT   PROPEP          40..609
FT                   /note="N-terminal propeptide"
FT                   /id="PRO_0000314669"
FT   CHAIN           610..1606
FT                   /note="Collagen alpha-1(XXVII) chain"
FT                   /id="PRO_0000314670"
FT   PROPEP          1607..1845
FT                   /note="C-terminal propeptide"
FT                   /id="PRO_0000314671"
FT   DOMAIN          72..237
FT                   /note="Laminin G-like"
FT   DOMAIN          610..664
FT                   /note="Collagen-like 1"
FT   DOMAIN          673..732
FT                   /note="Collagen-like 2"
FT   DOMAIN          742..801
FT                   /note="Collagen-like 3"
FT   DOMAIN          817..876
FT                   /note="Collagen-like 4"
FT   DOMAIN          877..936
FT                   /note="Collagen-like 5"
FT   DOMAIN          937..996
FT                   /note="Collagen-like 6"
FT   DOMAIN          997..1038
FT                   /note="Collagen-like 7"
FT   DOMAIN          1039..1096
FT                   /note="Collagen-like 8"
FT   DOMAIN          1117..1176
FT                   /note="Collagen-like 9"
FT   DOMAIN          1177..1236
FT                   /note="Collagen-like 10"
FT   DOMAIN          1240..1299
FT                   /note="Collagen-like 11"
FT   DOMAIN          1325..1384
FT                   /note="Collagen-like 12"
FT   DOMAIN          1424..1483
FT                   /note="Collagen-like 13"
FT   DOMAIN          1484..1543
FT                   /note="Collagen-like 14"
FT   DOMAIN          1544..1603
FT                   /note="Collagen-like 15"
FT   DOMAIN          1645..1845
FT                   /note="Fibrillar collagen NC1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT   REGION          299..478
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          502..572
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          608..774
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          610..1603
FT                   /note="Triple-helical"
FT   REGION          827..1608
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        308..344
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        351..394
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        405..423
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        440..478
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        529..543
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        623..657
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1120..1134
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1183..1209
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1590..1606
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1693
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         1695
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         1698
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         1701
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        272
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        340
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1754
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        1675..1707
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT   DISULFID        1681
FT                   /note="Interchain (with C-1285)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT   DISULFID        1698
FT                   /note="Interchain (with C-1268)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT   DISULFID        1716..1843
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT   DISULFID        1752..1796
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT   CONFLICT        293..295
FT                   /note="LAP -> VAR (in Ref. 1; AAN87341)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        302..306
FT                   /note="LRTVH -> VRSVR (in Ref. 1; AAN87341)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        312..314
FT                   /note="HSS -> RSC (in Ref. 1; AAN87341)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1845 AA;  186319 MW;  F5D7F43D834BB770 CRC64;
     MGTGFARGAR GTAASGPGGG FLFAWILVSF TCHLASTQGA PEDVDVLQRL GLSWTKAGGG
     RSPTPPGVIP FPSGFIFTQR AKLQAPTANV LPTTLGRELA LVLSLCSHRV NHAFLFAIRS
     RKHKLQLGLQ FLPGRTIIHL GPRQSVAFDL DVHDGRWHHL ALELRGRTVT MVTACGQHRV
     PVPLPSRRDS MLDPQGSFLL GKVNPRAVQF EGALCQFSIH PVAQVAHNYC AHLRERCRQV
     DTYSPQVGTL FPWDSGPAFA LHPEPALLGL GNLTRTPATL GARPVSRALA VTLAPAMPTK
     PLRTVHPDVS EHSSSQTPLS PAKQSARKTP SPSSSASLAN STRVYRPAAA QPRQITTTSP
     TKRSPTKPSV SPLSVTPMKS PHATQKTGVP SFTKPVPPTQ KPAPFTSYLA PSKASSPTVR
     PVQKTFMTPR PPVPSPQPLR PTTGLSKKFT NPTVAKSKSK TTSWASKPVL ARSSVPKTLQ
     QTVLSQSPVS YLGSQTLAPA LPPLGVGNPR TMPPTRDSAL TPAGSKKFTG RETSKKTRQK
     SSPRKPEPLS PGKSARDASP RDLTTKPSRP STPALVLAPA YLLSSSPQPT SSSFPFFHLL
     GPTPFPMLMG PPGSKGDCGL PGPPGLPGLP GSPGARGPRG PPGPYGNPGP PGPPGAKGQK
     GDPGLSPGQA HDGAKGNMGL PGLSGNPGPL GRKGHKGHPG AAGHPGEQGQ PGPEGSPGAK
     GYPGRQGFPG PVGDPGPKGS RGYIGLPGLF GLPGSDGERG LPGVPGKRGE MGRPGFPGDF
     GERGPPGLDG NPGEIGLPGP PGVLGLIGDT GALGPVGYPG PKGMKGLMGG VGEPGLKGDK
     GEQGVPGVSG DPGFQGDKGS HGLPGLPGGR GKPGPLGKAG DKGSLGFPGP PGPEGFPGDI
     GPPGDNGPEG MKGKPGARGL PGPPGQLGPE GDEGPMGPPG VPGLEGQPGR KGFPGRPGLD
     GSKGEPGDPG RPGPVGEQGL MGFIGLVGEP GIVGEKGDRG VMGPPGAPGP KGSMGHPGTP
     GGIGNPGEPG PWGPPGSRGL PGMRGAKGHR GPRGPDGPAG EQGSKGLKGR VGPRGRPGQP
     GQQGAAGERG HSGAKGFLGI PGPSGPPGAK GLPGEPGSQG PQGPVGPPGE MGPKGPPGAV
     GEPGLPGDSG MKGDLGPLGP PGEQGLIGQR GEPGLEGDHG PVGPDGLKGD RGDPGPDGEH
     GEKGQEGLKG EDGSPGPPGI TGVPGREGKP GKQGEKGQRG AKGAKGHQGY LGEMGIPGEP
     GPPGTPGPKG SRGTLGPTGA PGRMGAQGEP GLAGYNGHKG ITGPLGPPGP KGEKGDQGED
     GKTEGPPGPP GDRGPVGDRG DRGEPGDPGY PGQEGVQGLR GEPGQQGQPG HPGPRGRPGP
     KGSKGEEGPK GKPGKAGPSG RRGTQGLQGL PGPRGVVGRQ GPEGTAGSDG IPGRDGRPGY
     QGDQGNDGDP GPVGPAGRRG NPGVAGLPGA QGPPGFKGES GLPGQLGPPG KRGTEGGTGL
     PGNQGEPGSK GQPGDSGEMG FPGVAGLFGP KGPPGDIGFK GIQGPRGPPG LMGKEGIIGP
     PGMLGPSGLP GPKGDRGSRG DLGLQGPRGP PGPRGRPGPP GPPWHPIQFQ QDDLGAAFQT
     WMDAQGAVRS EGYSYPDQLA LDQGGEIFKT LHYLSNLIQS IKTPLGTKEN PARVCRDLMD
     CEQRMADGTY WVDPNLGCSS DTIEVSCNFT QGGQTCLKPI TASKAEFAVS RVQMNFLHLL
     SSEGTQHITI HCLNMTVWQE GPGRSSARQA VRFRAWNGQV FEAGGQFRPE VSMDGCKVHD
     GRWHQTLFTF RTQDPQQLPI VSVDNLPPVS SGKQYRLEVG PACFL
 
 
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