CORA1_RAT
ID CORA1_RAT Reviewed; 1855 AA.
AC Q80ZF0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Collagen alpha-1(XXVII) chain;
DE Flags: Precursor;
GN Name=Col27a1;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Pace J.M., Byers P.H.;
RT "Characterization of the rat col27a1 gene and its predicted protein
RT product, proa1(XXVII).";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
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. Note=Found on some small banded collagen fibrils and meshworks.
CC {ECO:0000250}.
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; AY232999; AAO43184.1; -; mRNA.
DR RefSeq; NP_942042.1; NM_198747.1.
DR AlphaFoldDB; Q80ZF0; -.
DR SMR; Q80ZF0; -.
DR STRING; 10116.ENSRNOP00000010333; -.
DR GlyGen; Q80ZF0; 3 sites.
DR PaxDb; Q80ZF0; -.
DR PRIDE; Q80ZF0; -.
DR GeneID; 298101; -.
DR KEGG; rno:298101; -.
DR UCSC; RGD:735115; rat.
DR CTD; 85301; -.
DR RGD; 735115; Col27a1.
DR VEuPathDB; HostDB:ENSRNOG00000007657; -.
DR eggNOG; KOG3544; Eukaryota.
DR HOGENOM; CLU_001074_19_1_1; -.
DR InParanoid; Q80ZF0; -.
DR OMA; YSYPDRL; -.
DR OrthoDB; 200318at2759; -.
DR PhylomeDB; Q80ZF0; -.
DR TreeFam; TF344135; -.
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-8874081; MET activates PTK2 signaling.
DR Reactome; R-RNO-8948216; Collagen chain trimerization.
DR PRO; PR:Q80ZF0; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000007657; Expressed in frontal cortex and 18 other tissues.
DR Genevisible; Q80ZF0; RN.
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; ISO:RGD.
DR GO; GO:0005201; F:extracellular matrix structural constituent; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; ISO:RGD.
DR GO; GO:0003431; P:growth plate cartilage chondrocyte development; ISO:RGD.
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; 8.
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..48
FT /evidence="ECO:0000255"
FT PROPEP 49..618
FT /note="N-terminal propeptide"
FT /id="PRO_0000314672"
FT CHAIN 619..1615
FT /note="Collagen alpha-1(XXVII) chain"
FT /id="PRO_0000314673"
FT PROPEP 1616..1855
FT /note="C-terminal propeptide"
FT /id="PRO_0000314674"
FT DOMAIN 81..246
FT /note="Laminin G-like"
FT DOMAIN 619..673
FT /note="Collagen-like 1"
FT DOMAIN 682..741
FT /note="Collagen-like 2"
FT DOMAIN 751..810
FT /note="Collagen-like 3"
FT DOMAIN 826..885
FT /note="Collagen-like 4"
FT DOMAIN 886..945
FT /note="Collagen-like 5"
FT DOMAIN 946..1005
FT /note="Collagen-like 6"
FT DOMAIN 1006..1047
FT /note="Collagen-like 7"
FT DOMAIN 1048..1105
FT /note="Collagen-like 8"
FT DOMAIN 1108..1155
FT /note="Collagen-like 9"
FT DOMAIN 1156..1215
FT /note="Collagen-like 10"
FT DOMAIN 1216..1275
FT /note="Collagen-like 11"
FT DOMAIN 1276..1330
FT /note="Collagen-like 12"
FT DOMAIN 1334..1393
FT /note="Collagen-like 13"
FT DOMAIN 1433..1492
FT /note="Collagen-like 14"
FT DOMAIN 1493..1552
FT /note="Collagen-like 15"
FT DOMAIN 1553..1612
FT /note="Collagen-like 16"
FT DOMAIN 1655..1855
FT /note="Fibrillar collagen NC1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT REGION 317..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 511..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 617..787
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 619..1612
FT /note="Triple-helical region"
FT REGION 838..1617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..660
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1129..1143
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1199..1218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1599..1615
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1703
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1705
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1708
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1711
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 349
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1764
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 1685..1717
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1691
FT /note="Interchain (with C-1285)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1708
FT /note="Interchain (with C-1268)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1726..1853
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1762..1806
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
SQ SEQUENCE 1855 AA; 187812 MW; 36E7B2C258D26AAB CRC64;
MGLARATAGL GPCCPPAPAL LGAGLRWGGF LFAWILVSFS CHLASTQGAP EDVDVLQRLG
LSWTKAGGGR SPAPPGVIPF PSGFIFTQRA KLQAPTTNVL PTTLGRELAL VLSLCSHRVN
HAFLFAIRSR KHRLQLGLQF LPGRTLVHLG PRQSVAFDLD VHDGRWHHLA LELRGRTVTL
VTACGQHRVP VPLPSRRDSM LDPQGSFLLG KMNPRAVQFE GALCQFSIHP VAQVAHNYCA
HLRERCRQVD TYGPQVGALF PWDSGPAFAL HPEPALLGLG NLTRNPATLG SRPISRGLMV
TMAPAVPTKP LRMVHQDVSK LGSSQTPLVP AKQSARKTPS PFPSAALANS TRVFHSAPAQ
PRQITATSPT KRPPTKPSVS SLSVTPMKSP QAIQKAGTPS FSRPIPTTQK PTPLTSHPSP
SKVSSATVRP VQKTFMTPQP PTLSPQALHP ITGLPKKFTI PTVAKPQSKM TSWASKPVLA
RTNVPKALEQ TVVAQSSVSY LGSQTLATAL PPLGVGNSRM MPSTRDSTST PAGSKKITGL
EASKKTRHKS SPRKPIPLSS GKTARDASPR DLTTKPSQLS TPALVLAPAH LLSSSPQPTS
SSFSFFHLPE PTPFLMLMGP PGSKGDCGLP GPPGLPGLPG SPGPRGPRGP PGPFGNPGLP
GPPGAKGQKG DPGLSPGQAH DGAKGNMGLP GLAGNPGPMG RKGHKGHPGA AGHPGEQGQP
GPEGSPGAKG YPGRQGFPGP VGDPGPKGSR GYIGLPGLFG LPGSDGERGL PGIPGKRGEM
GRPGFPGDFG ERGPPGLDGN PGEIGLPGPP GVLGLLGDMG ALGPVGYPGP KGMKGLMGGV
GEPGLKGDKG EQGVPGVSGD PGFQGDKGSH GLPGFPGARG KPGPMGKAGD KGSLGLPGPP
GPEGFPGDIG PPGDNGPEGM KGKPGARGLP GPPGQLGPEG DEGPMGPPGV PGLEGQPGRK
GFPGRPGLDG SKGEPGDPGR PGPVGEQGLM GFVGLVGEPG IVGEKGDRGV MGPPGAPGPK
GSMGHPGTPG GVGDPGEPGP WGPPGSRGLP GMRGAKGHRG PRGPDGPAGE QGSKGLKGRV
GPRGRPGQPG QQGAAGERGH SGAKGFLGIP GPSGPPGAKG LPGEPGSQGP QGPVGPPGEM
GPKGPPGAVG EPGLPGDSGM KGDLGPLGPP GEQGLIGQRG EPGLEGDLGP VGPDGLKGDR
GDPGPDGEHG EKGQEGLKGE EGLPGPPGIT GVRGREGKPG SQGEKGQRGA KGAKGYQGQL
GEMGIPGDPG PPGTPGPKGS RGTLGPMGAP GRMGAQGEPG LAGYNGHKGI TGPLGPPGPK
GEKGEQGEDG KTEGAPGPPG ERGPVGDRGD RGEPGDPGYP GQEGVQGLRG EPGQQGQPGH
PGPRGRPGPK GSKGEEGPKG KPGKAGASGR RGTQGLQGLP GPRGVVGRQG PEGMAGQDGN
PGRDGRPGYQ GEQGNDGDPG PVGPAGRRGN PGVAGLPGAQ GPPGFKGESG LPGQLGPPGK
RGTEGGTGLP GNQGEPGSKG QPGDSGEMGF PGVAGLFGPK GPPGDIGFKG IQGPRGPPGL
MGKEGIIGPP GMLGPSGLPG PKGDRGSRGD WGLQGPRGPP GPRGRPGPPG PPWHPVQFQQ
DDLEAAFQTW MDAHGAVRLE QGYSYPDQLM LDQGGEIFKT LHYLSNLIQS IKTPLGTKEN
PARVCRDLMD CEQKMADGIY WVDPNLGCSS DTIEVSCNFT HGGQTCLKPI TASKAEFAVS
RVQMNFLHLL SSEGTQHITI HCLNMTVWQE GPARPSARQA VRFRAWNGQV FEAGGQFRPE
VSMDGCKVHD GRWHQTLFTF RTQDPQQLPI VSVDNLPPVS SGKQYRLEVG PACFL
