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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}.
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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
 
 
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