ID   CCN2_PIG                Reviewed;         349 AA.
AC   O19113;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=CCN family member 2;
DE   AltName: Full=Cellular communication network factor 2;
DE   AltName: Full=Connective tissue growth factor;
DE   Flags: Precursor;
GN   Name=CCN2; Synonyms=CTGF, HBGF-0.8 {ECO:0000303|PubMed:9242708};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Uterus;
RX   PubMed=9242708; DOI=10.1074/jbc.272.32.20275;
RA   Brigstock D.R., Steffen C.L., Kim G.Y., Vegunta R.K., Diehl J.R.,
RA   Harding P.A.;
RT   "Purification and characterization of novel heparin-binding growth factors
RT   in uterine secretory fluids. Identification as heparin-regulated Mr 10,000
RT   forms of connective tissue growth factor.";
RL   J. Biol. Chem. 272:20275-20282(1997).
CC   -!- FUNCTION: Major connective tissue mitoattractant secreted by vascular
CC       endothelial cells. Promotes proliferation and differentiation of
CC       chondrocytes (By similarity). Mediates heparin- and divalent cation-
CC       dependent cell adhesion in many cell types including fibroblasts,
CC       myofibroblasts, endothelial and epithelial cells (By similarity).
CC       Enhances fibroblast growth factor-induced DNA synthesis (By
CC       similarity). {ECO:0000250|UniProtKB:P29279}.
CC   -!- SUBUNIT: Monomer. Interacts with TSKU. {ECO:0000250|UniProtKB:P29279}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250|UniProtKB:P29268}. Secreted
CC       {ECO:0000250|UniProtKB:P29268}.
CC   -!- SIMILARITY: Belongs to the CCN family. {ECO:0000305}.
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DR   EMBL; U83916; AAC48756.1; -; mRNA.
DR   AlphaFoldDB; O19113; -.
DR   SMR; O19113; -.
DR   STRING; 9823.ENSSSCP00000004525; -.
DR   PaxDb; O19113; -.
DR   PRIDE; O19113; -.
DR   eggNOG; ENOG502QQDX; Eukaryota.
DR   InParanoid; O19113; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
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 adhesion; Disulfide bond; DNA synthesis; Extracellular matrix;
KW   Heparin-binding; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..349
FT                   /note="CCN family member 2"
FT                   /id="PRO_0000014404"
FT   DOMAIN          27..98
FT                   /note="IGFBP N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DOMAIN          101..167
FT                   /note="VWFC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT   DOMAIN          198..243
FT                   /note="TSP type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          256..330
FT                   /note="CTCK"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT   REGION          247..349
FT                   /note="Heparin-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P29279"
FT   DISULFID        256..293
FT                   /evidence="ECO:0000250"
FT   DISULFID        273..307
FT                   /evidence="ECO:0000250"
FT   DISULFID        284..323
FT                   /evidence="ECO:0000250"
FT   DISULFID        287..325
FT                   /evidence="ECO:0000250"
FT   DISULFID        292..329
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   349 AA;  38007 MW;  BB510E2B2B52D4A0 CRC64;
     MSATGLSPVR CAFVLLLALC SRPASGQDCS GQCQCAAGKR RACPAGVSLV LDGCGCCRLC
     AKQLGELCTE RDPCDPHKGL FCDFGSPANR KIGVCTAKDG APCVFGGTVY RSGESFQSSC
     KYQCTCLDGA VGCVPLCSMD VRLPSPDCPF PRRVKLPGKC CEEWVCDEPK DHTVVGPALA
     AYRLEDTFGP DPTMMRANCL VQTTEWSACS KTCGMGISTR VTNDNAFCRL EKQSRLCMVR
     PCEADLEENI KKGKKCIRTP KISKPVKFEL SGCTSVKTYR AKFCGVCTDG RCCTPHRTTT
     LPVEFKCPDG EVMKKSMMFI KTCACHYNCP GDNDIFESLY YRKMYGDMA