CRA1B_DANRE
ID CRA1B_DANRE Reviewed; 1658 AA.
AC A0MSJ1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Collagen alpha-1(XXVII) chain B;
DE Flags: Precursor;
GN Name=col27a1b; Synonyms=col27a1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryo;
RA Malen R.C., Telfer H.E., Byers P.H., Pace J.M.;
RT "Characterization of the Danio rerio type XXVII collagen gene, col27a1.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=20041163; DOI=10.1371/journal.pone.0008481;
RA Christiansen H.E., Lang M.R., Pace J.M., Parichy D.M.;
RT "Critical early roles for col27a1a and col27a1b in zebrafish notochord
RT morphogenesis, vertebral mineralization and post-embryonic axial growth.";
RL PLoS ONE 4:E8481-E8481(2009).
CC -!- FUNCTION: May play a role during the calcification of cartilage and the
CC transition of cartilage to bone (By similarity). Together with
CC col27a1a, plays a role in development of the notochord and axial
CC skeleton. {ECO:0000250, ECO:0000269|PubMed:20041163}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
CC -!- TISSUE SPECIFICITY: Weakly expressed in the notochord from the 6 somite
CC stage. Expressed throughout the notochord at 13 somites, then becomes
CC restricted to the distal tip of the notochord by 24 hpf. Also expressed
CC in head cartilages by 48 hpf. {ECO:0000269|PubMed:20041163}.
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; EF032484; ABK32518.1; -; mRNA.
DR RefSeq; NP_001074044.1; NM_001080575.1.
DR AlphaFoldDB; A0MSJ1; -.
DR STRING; 7955.ENSDARP00000088068; -.
DR PaxDb; A0MSJ1; -.
DR GeneID; 560145; -.
DR KEGG; dre:560145; -.
DR CTD; 560145; -.
DR ZFIN; ZDB-GENE-100119-2; col27a1b.
DR eggNOG; KOG3544; Eukaryota.
DR InParanoid; A0MSJ1; -.
DR OrthoDB; 200318at2759; -.
DR PhylomeDB; A0MSJ1; -.
DR Reactome; R-DRE-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-DRE-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-DRE-8874081; MET activates PTK2 signaling.
DR Reactome; R-DRE-8948216; Collagen chain trimerization.
DR PRO; PR:A0MSJ1; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030282; P:bone mineralization; IGI:ZFIN.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0048570; P:notochord morphogenesis; IGI:ZFIN.
DR GO; GO:0001501; P:skeletal system development; IGI:ZFIN.
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; 7.
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; Developmental protein; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Metal-binding; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..38
FT /evidence="ECO:0000255"
FT PROPEP 39..?
FT /note="N-terminal propeptide"
FT /id="PRO_0000314675"
FT CHAIN ?..1420
FT /note="Collagen alpha-1(XXVII) chain B"
FT /id="PRO_0000314676"
FT PROPEP 1421..1658
FT /note="C-terminal propeptide"
FT /id="PRO_0000314677"
FT DOMAIN 66..229
FT /note="Laminin G-like"
FT DOMAIN 425..478
FT /note="Collagen-like 1"
FT DOMAIN 493..552
FT /note="Collagen-like 2"
FT DOMAIN 556..615
FT /note="Collagen-like 3"
FT DOMAIN 622..681
FT /note="Collagen-like 4"
FT DOMAIN 685..744
FT /note="Collagen-like 5"
FT DOMAIN 748..807
FT /note="Collagen-like 6"
FT DOMAIN 811..870
FT /note="Collagen-like 7"
FT DOMAIN 892..951
FT /note="Collagen-like 8"
FT DOMAIN 952..1011
FT /note="Collagen-like 9"
FT DOMAIN 1024..1083
FT /note="Collagen-like 10"
FT DOMAIN 1084..1137
FT /note="Collagen-like 11"
FT DOMAIN 1139..1198
FT /note="Collagen-like 12"
FT DOMAIN 1199..1258
FT /note="Collagen-like 13"
FT DOMAIN 1268..1327
FT /note="Collagen-like 14"
FT DOMAIN 1361..1420
FT /note="Collagen-like 15"
FT DOMAIN 1458..1658
FT /note="Fibrillar collagen NC1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT REGION 308..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..1417
FT /note="Triple-helical region"
FT REGION 427..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 571..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 637..1332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1377..1415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..448
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..471
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1043..1057
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1506
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1508
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1511
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1514
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 1567
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 1488..1520
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1494
FT /note="Interchain (with C-1285)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1511
FT /note="Interchain (with C-1268)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1529..1656
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1565..1609
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
SQ SEQUENCE 1658 AA; 168249 MW; EAFEEAD3A5EF9FCF CRC64;
MEPDNTPSSR LRAAGVGGRA VFFCMVLYCT CCLRLAQAQS ADVDVLQRLG LVGKRPPQGF
IPIKSGVILT TRARIDVPVS SVIPVSLGST FSIILSVCSH RINNAFLFTI VTKRKRLHLG
VQFIPGQILV YLGQNSSVNF DYNVHNGQWH NLALEIQGQK VTLYTSCGNT SIQANLDFQN
EETLDSEGSF RLGKMSQNSV QFEGAICQFD IHPSAQAAHN YCKYIKKQCR EADTYRPNLP
PLLPLLPLDP NRSTIQTPKV VTDINERHLS LTRDKMNINH EGQTTVPPMI TQPTLQLPLQ
TTAQTTASIR NRTSQISPKP TQQNRKKAKK ERNKLHILKE HQISVTDSPT SQQQNQVDIP
TTTTPELSST FRVSEMTTLA AQRPLPKETS FFEAKATFFE SVTPAAMDGL QTFDLEPTQY
SLLELTGLKG EPGLPGPPGP PGQPGLPGKR GPRGPSGPHG KPGPPGTPGP KGKKGNPGIS
PGRAPSGIKG DPGLVGLPGQ PGQPGRKGQK GHPGPSGHPG DQGIRGPDGS PGAKGYPGRQ
GLPGPIGNMG PKGVRGFIGI PGIFGLPGAD GERGLPGVPG KKGKMGRPGF PGDFGERGPP
GPDGNPGEIG APGPVGIPGF IGDMGPVGMV GPPGLIGPKG VPGNPGEPGL KGDKGELGLP
GEPGEPGFQG DKGIQGSPGL PGVQGKPGPQ GKIGDRGPDG LPGPLGPEGF PGDIGPPGQN
GVEGPKGNAG VRGIPGPGGL PGLEGDQGPV GPAGAPGLEG RPGRKGISGN PGEEGMKGEP
GMTGNPGMLG ERGPVGFVGP FGEMGLAGEK GDRGETGQPG PPGEKGAMGH PGAPGERGLS
GPAGAPGPHG SRGLSGTRGP KGTRGARGPD GPVGEKGMMG MKGPEGPPGK QGLSGQMGKI
GETGEAGPTG FTGVQGPTGP PGAKGILGEP GPQGSPGVLG PLGEIGAIGL PGKAGDQGLP
GEPGEKGAVG SPGNIGEQGL IGPRGDPGVD GEAGPSGPDG AKGEQGDVGL EGESGEKGVI
GFKGTEGRTG DPGLIGVKGP EGKPGKIGER GKPGEKGSKG HQGQLGEMGA LGEQGDTGFI
GPKGSRGTTG FMGAPGKMGQ QGEPGLVGYE GHQGPQGSLG SPGPKGEKGE QGDDGKVEGP
PGPSGDIGPV GNRGDRGEPG DPGYPGLEGV QGERGKEGAP GVPGNSGPRG FPGPKGSKGN
KGPKGKNSPR GESGNRGSPG PVGVPGPRGV IGREGFEGEP GLDGAAGKDG AKGMPGDLGR
DGDVGLPGKP GPQGNAGAPG LPGVQGSFGP KGERGITGHS GPPGKRGLNG GMGFPGKQGD
QGFKGQPGDA GEQGFPGVLG IFGPQGPPGD FGPVGIQGPK GPQGLMGMQG AIGPVGIIGP
SGNPGPQGDK GNKGEMGVQG PRGPPGPRGP PGPPGLPAVA FSHENEALGA ALHVFDSRSA
LRSEMYQDTD LPLLDQGSEI FKTLHYLSIL IHSIKNPLGT QENPARMCRD LLECEHRLND
GTYWIDPNLG CSSDNIEVTC SFTSGGQTCL KPVTASKLEI GVSLIQMNFI HLLSSEAVQI
ITVHCLNVSV WASEDSKTPS SSMVYFKAWD GQIIEAGGFI EPDLLKDECW ITDGRWHQTQ
FIFRTQDPNL LPIVEIYNLP STKPGSHYHL EVGPVCFL
