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 24-JAN-2024, entry version 153. 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}. 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; 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 GlyCosmos; Q5QNQ9; 3 sites, No reported glycans. DR GlyGen; Q5QNQ9; 3 sites. DR iPTMnet; Q5QNQ9; -. DR PhosphoSitePlus; Q5QNQ9; -. DR PaxDb; 10090-ENSMUSP00000043816; -. DR PeptideAtlas; Q5QNQ9; -. DR ProteomicsDB; 285266; -. DR Antibodypedia; 65300; 29 antibodies from 15 providers. DR DNASU; 373864; -. DR Ensembl; ENSMUST00000036300.13; ENSMUSP00000043816.7; ENSMUSG00000045672.16. DR GeneID; 373864; -. DR KEGG; mmu:373864; -. DR UCSC; uc008tfs.1; mouse. DR AGR; MGI:2672118; -. 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; HQHIAVG; -. DR OrthoDB; 2915342at2759; -. 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 79 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 226 other cell types or tissues. DR ExpressionAtlas; Q5QNQ9; baseline and differential. DR GO; GO:0005581; C:collagen trimer; IBA:GO_Central. DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL. 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:0030020; F:extracellular matrix structural constituent conferring tensile strength; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0001525; P:angiogenesis; IBA:GO_Central. DR GO; GO:0030199; P:collagen fibril organization; IBA:GO_Central. DR GO; GO:0001886; P:endothelial cell morphogenesis; IBA:GO_Central. DR GO; GO:0030198; P:extracellular matrix organization; IMP:MGI. DR GO; GO:0003431; P:growth plate cartilage chondrocyte development; IMP:MGI. DR GO; GO:0030903; P:notochord development; IBA:GO_Central. DR GO; GO:0001501; P:skeletal system development; IBA:GO_Central. DR Gene3D; 2.60.120.1000; -; 1. DR Gene3D; 2.60.120.200; -; 1. DR InterPro; IPR008160; Collagen. DR InterPro; IPR013320; ConA-like_dom_sf. DR InterPro; IPR000885; Fib_collagen_C. DR InterPro; IPR048287; TSPN-like_N. DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1. DR PANTHER; PTHR24023:SF844; COLLAGEN ALPHA-1(XXVII) CHAIN; 1. DR Pfam; PF01410; COLFI; 2. DR Pfam; PF01391; Collagen; 7. DR SMART; SM00038; COLFI; 1. DR SMART; SM00210; TSPN; 1. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1. DR PROSITE; PS51461; NC1_FIB; 1. DR Genevisible; Q5QNQ9; MM. 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 //