CCN2_BOVIN
ID CCN2_BOVIN Reviewed; 349 AA.
AC O18739; Q2HJ71; Q9GL71;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 11-FEB-2002, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=CCN family member 2 {ECO:0000305};
DE AltName: Full=Cellular communication network factor 2;
DE AltName: Full=Connective tissue growth factor;
DE Flags: Precursor;
GN Name=CCN2; Synonyms=CTGF;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Aorta;
RA Liliensiek B., Lin Z., Fotsis T., Schimanski M., Bierhaus A., Kanitz M.,
RA Kauffmann G., Schweigerer L., Ziegler R., Nawroth P.P.;
RT "Bos taurus connective tissue growth factor.";
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RA Mathahs M., Schwitters C., Hove M., Rupp S., Erondu N.E.;
RT "Bovine connective tissue growth factor, organization of the chromosomal
RT gene and demonstration of promoter activity.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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; AF000137; AAB66596.1; -; mRNA.
DR EMBL; AF309555; AAG30290.1; -; Genomic_DNA.
DR EMBL; BC113279; AAI13280.1; -; mRNA.
DR RefSeq; NP_776455.1; NM_174030.2.
DR AlphaFoldDB; O18739; -.
DR SMR; O18739; -.
DR STRING; 9913.ENSBTAP00000008357; -.
DR PaxDb; O18739; -.
DR PRIDE; O18739; -.
DR Ensembl; ENSBTAT00000008357; ENSBTAP00000008357; ENSBTAG00000006367.
DR GeneID; 281103; -.
DR KEGG; bta:281103; -.
DR CTD; 1490; -.
DR VEuPathDB; HostDB:ENSBTAG00000006367; -.
DR VGNC; VGNC:27794; CCN2.
DR eggNOG; ENOG502QQDX; Eukaryota.
DR GeneTree; ENSGT00940000155019; -.
DR HOGENOM; CLU_063247_1_0_1; -.
DR InParanoid; O18739; -.
DR OMA; QDCGGQC; -.
DR OrthoDB; 999958at2759; -.
DR TreeFam; TF326070; -.
DR Proteomes; UP000009136; Chromosome 9.
DR Bgee; ENSBTAG00000006367; Expressed in trachea and 103 other tissues.
DR ExpressionAtlas; O18739; baseline and differential.
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_0000014401"
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"
FT CONFLICT 28
FT /note="D -> DC (in Ref. 1; AAB66596)"
FT /evidence="ECO:0000305"
FT CONFLICT 58
FT /note="Missing (in Ref. 1; AAB66596)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="A -> T (in Ref. 1; AAB66596)"
FT /evidence="ECO:0000305"
FT CONFLICT 103..104
FT /note="CV -> YI (in Ref. 1; AAB66596)"
FT /evidence="ECO:0000305"
FT CONFLICT 166..169
FT /note="CDEP -> SRDE (in Ref. 1; AAB66596)"
FT /evidence="ECO:0000305"
FT CONFLICT 184
FT /note="P -> L (in Ref. 1; AAB66596)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="L -> Q (in Ref. 1; AAB66596)"
FT /evidence="ECO:0000305"
FT CONFLICT 209
FT /note="C -> Y (in Ref. 1; AAB66596)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="E -> Q (in Ref. 1; AAB66596)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="C -> F (in Ref. 1; AAB66596)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 349 AA; 37924 MW; 5FFC8EE83EFB4F99 CRC64;
MSATGLGPVR CAFVLLLALC SRPASSQDCS APCQCPAGPA PRCPAGVSLV LDGCGCCRVC
AKQLSELCTE RDPCDPHKGL FCDFGSPANR KIGVCTAKDG APCVFGGTVY QSGESFQSSC
KYQCTCLDGS VGCVPLCSVD VRLPSPDCPF PRRVKLPGKC CEEWVCDEPK EHTVVGPALA
AYRPEDTFGP DPTMIRANCL VQTTEWSACS KTCGMGISTR VTNDNAFCRL EKQSRLCMVR
PCEADLEENI KKGKKCIRTP KISKPIKFEL SGCTSMKTYR AKFCGVCTDG RCCTPHRTTT
LPVEFKCPDG EVMKKSMMFI KTCACHYNCP GDNDIFESLY YRKMYGDMA
