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   27-MAR-2024, entry version 102.
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   GlyCosmos; P51609; 1 site, No reported glycans.
DR   GeneID; 373662; -.
DR   KEGG; xla:373662; -.
DR   AGR; Xenbase:XB-GENE-1013047; -.
DR   CTD; 373662; -.
DR   Xenbase; XB-GENE-1013047; ccn3.L.
DR   OrthoDB; 2970572at2759; -.
DR   Proteomes; UP000186698; Chromosome 6L.
DR   Bgee; 373662; Expressed in testis and 17 other cell types or 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; 2.10.70.10; Complement Module, domain 1; 1.
DR   Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 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   PANTHER; PTHR11348:SF8; CCN FAMILY MEMBER 3; 1.
DR   PANTHER; PTHR11348; CONNECTIVE TISSUE GROWTH FACTOR-RELATED; 1.
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; Growth factor receptor domain; 1.
DR   SUPFAM; SSF82895; TSP-1 type 1 repeat; 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        21..46
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DISULFID        25..48
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DISULFID        28..49
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DISULFID        35..52
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DISULFID        60..74
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DISULFID        66..87
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
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
//