ID   CCN3_COTJA              Reviewed;         353 AA.
AC   P42642;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   27-MAR-2024, entry version 104.
DE   RecName: Full=CCN family member 3;
DE   AltName: Full=Cellular communication network factor 3 {ECO:0000250|UniProtKB:P48745};
DE   AltName: Full=Nephroblastoma-overexpressed gene protein;
DE   AltName: Full=Protein NOV;
DE   Flags: Precursor;
GN   Name=CCN3; Synonyms=NOV;
OS   Coturnix japonica (Japanese quail) (Coturnix coturnix japonica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Perdicinae; Coturnix.
OX   NCBI_TaxID=93934;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Weiskirchen R., Bister K.;
RL   Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Immediate-early protein likely to play a role in cell growth
CC       regulation. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9QZQ5}.
CC       Cytoplasm {ECO:0000250|UniProtKB:Q9QZQ5}. Cell junction, gap junction
CC       {ECO:0000250|UniProtKB:Q9QZQ5}.
CC   -!- SIMILARITY: Belongs to the CCN family. {ECO:0000305}.
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DR   EMBL; U13063; AAA21128.1; -; mRNA.
DR   RefSeq; NP_001310148.1; NM_001323219.1.
DR   AlphaFoldDB; P42642; -.
DR   SMR; P42642; -.
DR   GlyCosmos; P42642; 1 site, No reported glycans.
DR   Ensembl; ENSCJPT00005009151.1; ENSCJPP00005005682.1; ENSCJPG00005005391.1.
DR   GeneID; 107310512; -.
DR   KEGG; cjo:107310512; -.
DR   CTD; 4856; -.
DR   GeneTree; ENSGT00940000159963; -.
DR   OrthoDB; 2970572at2759; -.
DR   Proteomes; UP000694412; Chromosome 2.
DR   Proteomes; UP000694961; Chromosome 2.
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:0043231; C:intracellular membrane-bounded organelle; IEA:Ensembl.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0005178; F:integrin binding; IEA:Ensembl.
DR   GO; GO:0005112; F:Notch binding; IEA:Ensembl.
DR   GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR   GO; GO:1990523; P:bone regeneration; IEA:Ensembl.
DR   GO; GO:0033627; P:cell adhesion mediated by integrin; IEA:Ensembl.
DR   GO; GO:0002062; P:chondrocyte differentiation; IEA:Ensembl.
DR   GO; GO:0035767; P:endothelial cell chemotaxis; IEA:Ensembl.
DR   GO; GO:0071603; P:endothelial cell-cell adhesion; IEA:Ensembl.
DR   GO; GO:0010761; P:fibroblast migration; IEA:Ensembl.
DR   GO; GO:0061484; P:hematopoietic stem cell homeostasis; IEA:Ensembl.
DR   GO; GO:0030308; P:negative regulation of cell growth; IEA:Ensembl.
DR   GO; GO:1902731; P:negative regulation of chondrocyte proliferation; IEA:Ensembl.
DR   GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
DR   GO; GO:0046676; P:negative regulation of insulin secretion; IEA:Ensembl.
DR   GO; GO:0090027; P:negative regulation of monocyte chemotaxis; IEA:Ensembl.
DR   GO; GO:0010832; P:negative regulation of myotube differentiation; IEA:Ensembl.
DR   GO; GO:1901223; P:negative regulation of non-canonical NF-kappaB signal transduction; IEA:Ensembl.
DR   GO; GO:0060392; P:negative regulation of SMAD protein signal transduction; IEA:Ensembl.
DR   GO; GO:0045747; P:positive regulation of Notch signaling pathway; IEA:Ensembl.
DR   GO; GO:0014909; P:smooth muscle cell migration; IEA:Ensembl.
DR   GO; GO:0048659; P:smooth muscle cell proliferation; IEA:Ensembl.
DR   GO; GO:0044342; P:type B pancreatic cell proliferation; IEA:Ensembl.
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; 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   Cell junction; Cytoplasm; Disulfide bond; Gap junction; Glycoprotein;
KW   Growth factor; Proto-oncogene; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..353
FT                   /note="CCN family member 3"
FT                   /id="PRO_0000014414"
FT   DOMAIN          29..103
FT                   /note="IGFBP N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DOMAIN          106..172
FT                   /note="VWFC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT   DOMAIN          203..248
FT                   /note="TSP type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          260..334
FT                   /note="CTCK"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT   CARBOHYD        276
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        33..59
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DISULFID        37..61
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DISULFID        41..62
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DISULFID        48..65
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DISULFID        73..87
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DISULFID        79..100
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DISULFID        260..297
FT                   /evidence="ECO:0000250"
FT   DISULFID        277..311
FT                   /evidence="ECO:0000250"
FT   DISULFID        288..327
FT                   /evidence="ECO:0000250"
FT   DISULFID        291..329
FT                   /evidence="ECO:0000250"
FT   DISULFID        296..333
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   353 AA;  38667 MW;  717D9F8533882E89 CRC64;
     MEPGGGHSLP VLLLLLLLLL LRPSEVNGRE APCPRPCGGR CPAEPPRCAP GVPAVLDGCG
     CCLVCARQRG ESCSPLLPCD ESGGLYCDRG PEDGGGTGIC MVLEGDNCVF DGMIYRNGET
     FQPSCKYQCT CRDGQIGCLP RCNLGLLLPG PDCPFPRKIE VPGECCEKWV CEPRDEVLLG
     GFAMAAYRQE ATLGIDVSDS SANCIEQTTE WSACSRSCGM GFSTRVTNRN QQCEMVKQTR
     LCMMRPCENE EPSDKKGKKC IRTKKSMKAV RFEYKNCTSV QTYKPRYCGL CNDGRCCTPH
     NTKTIQVEFR CPQGKFLKKP MMLINTCVCH GNCPQSNNAF FQPLDPMSSE AKI
//