CCN3_CHICK
ID CCN3_CHICK Reviewed; 351 AA.
AC P28686;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=CCN family member 3 {ECO:0000305};
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 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].
RC STRAIN=Brown leghorn;
RX PubMed=1309586; DOI=10.1128/mcb.12.1.10-21.1992;
RA Joliot V., Martinerie C., Dambrine G., Plassiart G., Brisac M., Crochet J.,
RA Perbal B.;
RT "Proviral rearrangements and overexpression of a new cellular gene (nov) in
RT myeloblastosis-associated virus type 1-induced nephroblastomas.";
RL Mol. Cell. Biol. 12:10-21(1992).
CC -!- FUNCTION: Immediate-early protein likely to play a role in cell growth
CC regulation. Its overexpression is associated with tumorigenesis and
CC expression of a N-terminal-truncated version of CCN3 gene in chicken
CC embryonic fibroblasts (CEF) is sufficient to induce the transformation
CC of CEF in vitro.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9QZQ5}.
CC Cytoplasm {ECO:0000250|UniProtKB:Q9QZQ5}. Cell junction, gap junction
CC {ECO:0000250|UniProtKB:Q9QZQ5}.
CC -!- TISSUE SPECIFICITY: Brain and heart, and at a lower level in muscle and
CC intestine, in the embryo. Lung and less so in brain and spleen, in
CC adult chicken.
CC -!- DEVELOPMENTAL STAGE: MAV1-induced nephroblastomas express a high level
CC of NOV gene whose transcription is normally arrested in adult kidney.
CC -!- SIMILARITY: Belongs to the CCN family. {ECO:0000305}.
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DR EMBL; X59284; CAA41975.1; -; mRNA.
DR PIR; S20078; S20078.
DR RefSeq; NP_990599.1; NM_205268.1.
DR AlphaFoldDB; P28686; -.
DR SMR; P28686; -.
DR STRING; 9031.ENSGALP00000025912; -.
DR PaxDb; P28686; -.
DR GeneID; 396204; -.
DR KEGG; gga:396204; -.
DR CTD; 4856; -.
DR VEuPathDB; HostDB:geneid_396204; -.
DR eggNOG; ENOG502QR9V; Eukaryota.
DR InParanoid; P28686; -.
DR OrthoDB; 999958at2759; -.
DR PhylomeDB; P28686; -.
DR PRO; PR:P28686; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
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 GO; GO:0008201; F:heparin binding; IBA:GO_Central.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0060548; P:negative regulation of cell death; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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 Cell junction; Cytoplasm; Disulfide bond; Gap junction; Glycoprotein;
KW Growth factor; Proto-oncogene; Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..351
FT /note="CCN family member 3"
FT /id="PRO_0000014413"
FT DOMAIN 27..101
FT /note="IGFBP N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT DOMAIN 104..170
FT /note="VWFC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 201..246
FT /note="TSP type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 258..332
FT /note="CTCK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT CARBOHYD 274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 258..295
FT /evidence="ECO:0000250"
FT DISULFID 275..309
FT /evidence="ECO:0000250"
FT DISULFID 286..325
FT /evidence="ECO:0000250"
FT DISULFID 289..327
FT /evidence="ECO:0000250"
FT DISULFID 294..331
FT /evidence="ECO:0000250"
SQ SEQUENCE 351 AA; 38268 MW; 1ECB3FA3058C6797 CRC64;
METGGGQGLP VLLLLLLLLR PCEVSGREAA CPRPCGGRCP AEPPRCAPGV PAVLDGCGCC
LVCARQRGES CSPLLPCDES GGLYCDRGPE DGGGAGICMV LEGDNCVFDG MIYRNGETFQ
PSCKYQCTCR DGQIGCLPRC NLGLLLPGPD CPFPRKIEVP GECCEKWVCD PRDEVLLGGF
AMAAYRQEAT LGIDVSDSSA NCIEQTTEWS ACSKSCGMGF STRVTNRNQQ CEMVKQTRLC
MMRPCENEEP SDKKGKKCIQ TKKSMKAVRF EYKNCTSVQT YKPRYCGLCN DGRCCTPHNT
KTIQVEFRCP QGKFLKKPMM LINTCVCHGN CPQSNNAFFQ PLDPMSSEAK I
