CCN3_XENLA
ID CCN3_XENLA Reviewed; 343 AA.
AC P51609;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=CCN family member 3;
DE AltName: Full=Cellular communication network factor 3 {ECO:0000250|UniProtKB:P48745};
DE AltName: Full=Protein NOV homolog;
DE Short=Xnov;
DE Flags: Precursor;
GN Name=ccn3; Synonyms=nov;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8666280; DOI=10.1016/0378-1119(95)00891-8;
RA Ying Z., King M.L.;
RT "Isolation and characterization of xnov, a Xenopus laevis ortholog of the
RT chicken nov gene.";
RL Gene 171:243-248(1996).
CC -!- FUNCTION: Immediate-early protein playing a role in various cellular
CC processes including proliferation, adhesion, migration, differentiation
CC and survival. Acts by binding to integrins or membrane receptors such
CC as NOTCH1. {ECO:0000250|UniProtKB:P48745, ECO:0000250|UniProtKB:Q64299,
CC ECO:0000250|UniProtKB:Q9QZQ5}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P48745}.
CC Cytoplasm {ECO:0000250|UniProtKB:P48745}. Cell junction, gap junction
CC {ECO:0000250|UniProtKB:P48745}.
CC -!- SIMILARITY: Belongs to the CCN family. {ECO:0000305}.
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DR EMBL; U37063; AAB17096.1; -; mRNA.
DR RefSeq; NP_001079127.1; NM_001085658.1.
DR AlphaFoldDB; P51609; -.
DR SMR; P51609; -.
DR PRIDE; P51609; -.
DR GeneID; 373662; -.
DR KEGG; xla:373662; -.
DR CTD; 373662; -.
DR Xenbase; XB-GENE-1013047; ccn3.L.
DR OrthoDB; 999958at2759; -.
DR Proteomes; UP000186698; Chromosome 6L.
DR Bgee; 373662; Expressed in testis and 17 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005921; C:gap junction; IEA:UniProtKB-SubCell.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
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; 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 Cell junction; Cytoplasm; Disulfide bond; Gap junction; Glycoprotein;
KW Growth factor; Reference proteome; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..343
FT /note="CCN family member 3"
FT /id="PRO_0000014418"
FT DOMAIN 19..90
FT /note="IGFBP N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT DOMAIN 93..159
FT /note="VWFC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 190..235
FT /note="TSP type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 249..323
FT /note="CTCK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 249..286
FT /evidence="ECO:0000250"
FT DISULFID 266..300
FT /evidence="ECO:0000250"
FT DISULFID 277..316
FT /evidence="ECO:0000250"
FT DISULFID 280..318
FT /evidence="ECO:0000250"
FT DISULFID 285..322
FT /evidence="ECO:0000250"
SQ SEQUENCE 343 AA; 38070 MW; 677D7078EB21365F CRC64;
MTPHLALCFI LLIQQVASQK CPSQCDQCPE EPPSCAPSVL LILDGCGCCP VCARQEGESC
SHLNPCQEDK GLYCEFNADP RMETGTCMAL EGNSCVFDGV VYRNRESFQP SCKYHCTCLN
GHIGCVPRCN LDLLLPGPDC PFPRRVKVPG ECCEKWVCDS KEEMAIGGFA MAAYRPEATL
GIDASDTSFA CIAQTTEWSA CSKTCGMGVS SRVTNRNARC EMQKQIRLCM VRSCEEEPGW
HVEKKGKKCV RVRKTTKPIH FHYKNCTSVQ PYKPKFCGQC SDGRCCTPHS TKTMHVEFVC
PQKRIVKKPV MVISTCVCHY NCPQDSSLLQ VENARFPGLK TNL