CRA1A_DANRE
ID CRA1A_DANRE Reviewed; 1783 AA.
AC C7DZK3;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Collagen alpha-1(XXVII) chain A {ECO:0000250|UniProtKB:Q8IZC6, ECO:0000303|PubMed:20041163};
DE Flags: Precursor;
GN Name=col27a1a {ECO:0000303|PubMed:20041163, ECO:0000312|EMBL:ACT31326.1};
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] {ECO:0000305, ECO:0000312|EMBL:ACT31326.1}
RP NUCLEOTIDE SEQUENCE [MRNA], 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 col27a1b, plays a role in development of the notochord and axial
CC skeleton. {ECO:0000250|UniProtKB:Q8IZC6, ECO:0000269|PubMed:20041163}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250|UniProtKB:Q5QNQ9, ECO:0000255|PROSITE-
CC ProRule:PRU00793}.
CC -!- TISSUE SPECIFICITY: Expressed dynamically in the notochord from late
CC epiboly, spreading to the anterior notochord by 24 hpf, and then
CC throughout the notochord by 30 hpf. Subsequently, notochordal
CC expression becomes restricted to the distal tip of the tail by 48 hpf
CC and is no longer detectable by 72 hpf. Also expressed throughout the
CC floor plate and hypochord at 24 hpf, and in forming head cartilages and
CC the first forming tooth. {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}.
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; GQ229459; ACT31326.1; -; mRNA.
DR RefSeq; NP_001156766.1; NM_001163294.1.
DR AlphaFoldDB; C7DZK3; -.
DR STRING; 7955.ENSDARP00000057303; -.
DR PaxDb; C7DZK3; -.
DR PRIDE; C7DZK3; -.
DR GeneID; 100004688; -.
DR KEGG; dre:100004688; -.
DR CTD; 100004688; -.
DR ZFIN; ZDB-GENE-100119-1; col27a1a.
DR eggNOG; KOG3544; Eukaryota.
DR InParanoid; C7DZK3; -.
DR OrthoDB; 200318at2759; -.
DR PhylomeDB; C7DZK3; -.
DR PRO; PR:C7DZK3; -.
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; IMP:ZFIN.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0048570; P:notochord morphogenesis; IMP:ZFIN.
DR GO; GO:0001501; P:skeletal system development; IMP:ZFIN.
DR CDD; cd00110; LamG; 1.
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; 5.
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..35
FT /evidence="ECO:0000255"
FT PROPEP 36..?
FT /note="N-terminal propeptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000397218"
FT CHAIN ?..1550
FT /note="Collagen alpha-1(XXVII) chain A"
FT /evidence="ECO:0000269|PubMed:20041163"
FT /id="PRO_0000397219"
FT PROPEP 1551..1783
FT /note="C-terminal propeptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000397220"
FT DOMAIN 73..235
FT /note="Laminin G-like"
FT /evidence="ECO:0000255"
FT DOMAIN 554..608
FT /note="Collagen-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 818..873
FT /note="Collagen-like 2"
FT /evidence="ECO:0000255"
FT DOMAIN 845..902
FT /note="Collagen-like 3"
FT /evidence="ECO:0000255"
FT DOMAIN 986..1043
FT /note="Collagen-like 4"
FT /evidence="ECO:0000255"
FT DOMAIN 1269..1326
FT /note="Collagen-like 5"
FT /evidence="ECO:0000255"
FT DOMAIN 1446..1503
FT /note="Collagen-like 6"
FT /evidence="ECO:0000255"
FT DOMAIN 1497..1549
FT /note="Collagen-like 7"
FT /evidence="ECO:0000255"
FT DOMAIN 1589..1783
FT /note="Fibrillar collagen NC1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT REGION 288..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..1547
FT /note="Triple-helical region"
FT /evidence="ECO:0000255"
FT REGION 553..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 772..1461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1512..1546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..407
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..451
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..593
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 965..979
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1326..1344
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1637
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1639
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1642
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1645
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 1698
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 1619..1651
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1625
FT /note="Interchain (with C-1285)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1642
FT /note="Interchain (with C-1268)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1660..1781
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1696..1734
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
SQ SEQUENCE 1783 AA; 179841 MW; FD67E429E1222930 CRC64;
MNLATRRRVR RTSRLVAKRA LLLCILLYCT SFGFTQVLFE DVDVLQRLAL RAELGSRAVP
AGVISLRSGV ILTTRARVTT PTRSLFPPEL FWNCTIILSV RSHRLNSAFL FSVLSGNRIQ
LGLEISPGKL TLHAGPGNAA TFLYNLHDGR WHHLAFVING RSVTLHSPCS ESDSGVTQEL
PVLPERLNPR GTFRLGGSSA LLPGVVPFEG AVCQFDVVPS AQAQQNICSA IRRQCRENDT
YRPAPPALLP LPSRHAPPLL AHTLPPNRTF TFTPTNFLLA PVNGAGGSSS VRMSDGVRPK
PSSTTPPPLA LMQTGIDAPL SLSLVTHKPS LRTPKPTASK PGVWLTPTKP ARPKPTPGKA
SPKLNVSKSF GPKPTARLAA SKLGSKAIGP KPTPLKPSKP VKKPTSVPKP NPTKNASIGP
RPTNSNKKQN AILKPLPAPK PTVPKRPSPT NKKPLQPKNK SHTTPLTPKS TLAPNSTSKK
PLPTLKSTSF TTAAPNKPPK TLETPKVNPD KSKTPVPYST PRTPRFSIQS VTLPAFDDFQ
SFEVEPTRFS LLVGAPGLKG DQGESGLPGP PGKPGQPGMR GPRGPPGPHG KPGRPGPTGL
KGKKGDPGLS PGKAPKGDKG DVGLPGPVGL VGVEGRKGQK GHPGPPGLPG EPGEQGPVGE
AGAKGYPGRQ GLPGPIGPVG PKGARGFIGI PGLFGLPGAD GERGSPGPPG KRGKMGRPGF
PGDFGERGPP GLDGEPGVIG APGPPGVLGL IGDMGPAGTV GVPGLNGLKG VPGNMGESGL
KGDKGDVGLP GEQGEIGFQG DKGVQGLPGL PGPRGKPGPQ GKTGEIGPSG LPGPPGPEGF
PGDIGKPGLN GPEGPKGKPG ARGLPGPRGA AGREGDEGPL GPPGPFGLEG QMGSKGFPGA
LGLEGVKGEQ GVTGKAGPMG ERGLVGFIGP GGEAGLAGEK GDRGEMGLPG PPGEKGSTGH
PGTPGEGGPP GPPGSPGSPG SRGPIGIRGP KGRRGPRGPD GVPGEIGTEG KKGPDGPPGK
IGFPGHAGKI GESGEVGPKG FPGIQGPSGA TGDKGIAGEP GPSGPPGTLG PQGNPGPKGP
AGKVGDSGLP GEPGEKGSIG LAGNAGAAGL IGARGEPGLE GEAGPAGPDG TKGEKGDMGT
EGEQGVRGDP GIKGKDGPPG DPGLTGVRGP EGKSGKSGER GKPGLKGAKG NIGHLGETGS
VGKIGPIGTT GPKGSRGTIG HAGAPGRMGL QGDPGISGYE GHKGPQGPIG PPGPKGAKGE
QGDDGKVEGP TGAPGLRGPV GKRGDRGEPG DPGYVGQQGV DGLRGKPGAP GLPGDPGPRG
TQGPKGSKGE QGQKGKQGQQ GERGSRGSPG VVGLPGPRGT VGREGREGFP GTDGLAGKDG
SRGTPGDQGD DGEFGLPGKP GAPGKVGVIG LPGPQGSFGP KGERGLPGHP GPSGKRGFKG
GMGLPGPQGD RGSKGQPGDI GEPGFPGMLG MFGPKGPPGD FGPKGIQGPK GPQGNMGRGG
LAGPVGVIGP IGNPGSRGDT GNKGELGVQG PRGAPGPRGP PGLPGPPGIP LAMNQDFGLG
VVQPVFRETH TQKIEGRGLL DMPMLDQAPE ILRTLDYLSS LVHSLKNPLG TRDHPARLCR
DLHDCRDTLY DGTYWIDPNL GCSSDSIEVM CNFSSGGRTC LRPITTAKLE FSVGRVQMNF
LHLLSAGAEQ RITIHCLNVT IWSHAPNQPP SQNAVQFHSW IGEVLEPDVL EDTCWQLNGR
WQHADFLFRV LDPALLPVVR ISNLPKVMPS SRFHLEVGPV CFL