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CCN1_CHICK
ID   CCN1_CHICK              Reviewed;         375 AA.
AC   P19336;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=CCN family member 1;
DE   AltName: Full=Cellular communication network factor 1;
DE   AltName: Full=Protein CEF-10;
DE   AltName: Full=Protein CYR61;
DE   Flags: Precursor;
GN   Name=CCN1; Synonyms=CYR61;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2537491; DOI=10.1073/pnas.86.4.1178;
RA   Simmons D.L., Levy D.B., Yannoni Y., Erikson R.L.;
RT   "Identification of a phorbol ester-repressible v-src-inducible gene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:1178-1182(1989).
CC   -!- FUNCTION: Probable secreted regulatory protein.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- INDUCTION: By V-Src.
CC   -!- SIMILARITY: Belongs to the CCN family. {ECO:0000305}.
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DR   EMBL; J04496; AAA48661.1; -; mRNA.
DR   PIR; A41428; A41428.
DR   RefSeq; NP_001026734.1; NM_001031563.1.
DR   AlphaFoldDB; P19336; -.
DR   SMR; P19336; -.
DR   STRING; 9031.ENSGALP00000014090; -.
DR   PaxDb; P19336; -.
DR   Ensembl; ENSGALT00000014106; ENSGALP00000014090; ENSGALG00000008661.
DR   GeneID; 429089; -.
DR   KEGG; gga:429089; -.
DR   CTD; 429089; -.
DR   VEuPathDB; HostDB:geneid_429089; -.
DR   eggNOG; ENOG502QQQQ; Eukaryota.
DR   GeneTree; ENSGT00940000155151; -.
DR   HOGENOM; CLU_063247_1_0_1; -.
DR   InParanoid; P19336; -.
DR   OMA; CPLEVPK; -.
DR   OrthoDB; 999958at2759; -.
DR   PhylomeDB; P19336; -.
DR   PRO; PR:P19336; -.
DR   Proteomes; UP000000539; Chromosome 8.
DR   Bgee; ENSGALG00000008661; Expressed in spermatocyte and 13 other tissues.
DR   ExpressionAtlas; P19336; baseline and differential.
DR   GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0050840; F:extracellular matrix binding; IEA:Ensembl.
DR   GO; GO:0019838; F:growth factor binding; IEA:UniProtKB-KW.
DR   GO; GO:0008201; F:heparin binding; IBA:GO_Central.
DR   GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR   GO; GO:0003278; P:apoptotic process involved in heart morphogenesis; IEA:Ensembl.
DR   GO; GO:0060413; P:atrial septum morphogenesis; IEA:Ensembl.
DR   GO; GO:0003181; P:atrioventricular valve morphogenesis; IEA:Ensembl.
DR   GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR   GO; GO:0098609; P:cell-cell adhesion; IEA:Ensembl.
DR   GO; GO:0060591; P:chondroblast differentiation; IEA:Ensembl.
DR   GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl.
DR   GO; GO:0002041; P:intussusceptive angiogenesis; IEA:Ensembl.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:0060548; P:negative regulation of cell death; IBA:GO_Central.
DR   GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:0030513; P:positive regulation of BMP signaling pathway; IEA:Ensembl.
DR   GO; GO:0030501; P:positive regulation of bone mineralization; IEA:Ensembl.
DR   GO; GO:0061036; P:positive regulation of cartilage development; IEA:Ensembl.
DR   GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
DR   GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IEA:Ensembl.
DR   GO; GO:2000304; P:positive regulation of ceramide biosynthetic process; IEA:Ensembl.
DR   GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
DR   GO; GO:0045669; P:positive regulation of osteoblast differentiation; IEA:Ensembl.
DR   GO; GO:0033690; P:positive regulation of osteoblast proliferation; IEA:Ensembl.
DR   GO; GO:0010518; P:positive regulation of phospholipase activity; IEA:Ensembl.
DR   GO; GO:0045860; P:positive regulation of protein kinase activity; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0072593; P:reactive oxygen species metabolic process; IEA:Ensembl.
DR   GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   GO; GO:0003281; P:ventricular septum development; IEA:Ensembl.
DR   GO; GO:0044319; P:wound healing, spreading of cells; IEA:Ensembl.
DR   Gene3D; 2.20.100.10; -; 1.
DR   InterPro; IPR006207; Cys_knot_C.
DR   InterPro; IPR006208; Glyco_hormone_CN.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR000867; IGFBP-like.
DR   InterPro; IPR012395; IGFBP_CNN.
DR   InterPro; IPR017891; Insulin_GF-bd_Cys-rich_CS.
DR   InterPro; IPR043973; TSP1_CCN.
DR   InterPro; IPR000884; TSP1_rpt.
DR   InterPro; IPR036383; TSP1_rpt_sf.
DR   InterPro; IPR001007; VWF_dom.
DR   Pfam; PF00007; Cys_knot; 1.
DR   Pfam; PF00219; IGFBP; 1.
DR   Pfam; PF19035; TSP1_CCN; 1.
DR   Pfam; PF00093; VWC; 1.
DR   PIRSF; PIRSF036495; IGFBP_rP_CNN; 1.
DR   SMART; SM00041; CT; 1.
DR   SMART; SM00121; IB; 1.
DR   SMART; SM00209; TSP1; 1.
DR   SMART; SM00214; VWC; 1.
DR   SUPFAM; SSF57184; SSF57184; 1.
DR   SUPFAM; SSF82895; SSF82895; 1.
DR   PROSITE; PS01185; CTCK_1; 1.
DR   PROSITE; PS01225; CTCK_2; 1.
DR   PROSITE; PS00222; IGFBP_N_1; 1.
DR   PROSITE; PS51323; IGFBP_N_2; 1.
DR   PROSITE; PS50092; TSP1; 1.
DR   PROSITE; PS01208; VWFC_1; 1.
DR   PROSITE; PS50184; VWFC_2; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Growth factor binding; Phosphoprotein; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..22
FT   CHAIN           23..375
FT                   /note="CCN family member 1"
FT                   /id="PRO_0000014397"
FT   DOMAIN          23..94
FT                   /note="IGFBP N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DOMAIN          98..164
FT                   /note="VWFC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT   DOMAIN          223..268
FT                   /note="TSP type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          281..355
FT                   /note="CTCK"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT   REGION          274..310
FT                   /note="Heparin-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P18406"
FT   DISULFID        281..318
FT                   /evidence="ECO:0000250"
FT   DISULFID        298..332
FT                   /evidence="ECO:0000250"
FT   DISULFID        309..348
FT                   /evidence="ECO:0000250"
FT   DISULFID        312..350
FT                   /evidence="ECO:0000250"
FT   DISULFID        317..354
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   375 AA;  40652 MW;  95F28553BE35D5AE CRC64;
     MGSAGARPAL AAALLCLARL ALGSPCPAVC QCPAAAPQCA PGVGLVPDGC GCCKVCAKQL
     NEDCSRTQPC DHTKGLECNF GASPAATNGI CRAQSEGRPC EYNSKIYQNG ESFQPNCKHQ
     CTCIDGAVGC IPLCPQELSL PNLGCPSPRL VKVPGQCCEE WVCDESKDAL EELEGFFSKE
     FGLDASEGEL TRNNELIAIV KGGLKMLPVF GSEPQSRAFE NPKCIVQTTS WSQCSKTCGT
     GISTRVTNDN PDCKLIKETR ICEVRPCGQP SYASLKKGKK CTKTKKSPSP VRFTYAGCSS
     VKKYRPKYCG SCVDGRCCTP QQTRTVKIRF RCDDGETFTK SVMMIQSCRC NYNCPHANEA
     YPFYRLVNDI HKFRD
 
 
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