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