CCN2_RAT
ID CCN2_RAT Reviewed; 347 AA.
AC Q9R1E9; Q53YJ0; Q9WVS1;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 150.
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 AltName: Full=Connective tissue growth-related protein;
DE Flags: Precursor;
GN Name=Ccn2 {ECO:0000312|RGD:621392}; Synonyms=Ctgf;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10679821;
RX DOI=10.1002/(sici)1097-4644(20000401)77:1<103::aid-jcb11>3.0.co;2-g;
RA Xu J., Smock S.L., Safadi F.F., Rosenzweig A.B., Odgren P.R.,
RA Marks S.C. Jr., Owen T.A., Popoff S.N.;
RT "Cloning the full-length cDNA for rat connective tissue growth factor:
RT implications for skeletal development.";
RL J. Cell. Biochem. 77:103-115(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10393331; DOI=10.1093/oxfordjournals.jbchem.a022414;
RA Shimo T., Nakanishi T., Nishida T., Asano M., Kanyama M., Kuboki T.,
RA Tamatani T., Tezuka K., Takemura M., Matsumura T., Takigawa M.;
RT "Connective tissue growth factor induces the proliferation, migration, and
RT tube formation of vascular endothelial cells in vitro, and angiogenesis in
RT vivo.";
RL J. Biochem. 126:137-145(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar;
RA Ma L.N., Zou Y.L.;
RT "Connective tissue growth related gene.";
RL Submitted (APR-2004) 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; AF120275; AAD39132.1; -; mRNA.
DR EMBL; AB023068; BAA82125.1; -; mRNA.
DR EMBL; AY596447; AAT08023.1; -; Transcribed_RNA.
DR RefSeq; NP_071602.1; NM_022266.2.
DR AlphaFoldDB; Q9R1E9; -.
DR SMR; Q9R1E9; -.
DR STRING; 10116.ENSRNOP00000020528; -.
DR jPOST; Q9R1E9; -.
DR PaxDb; Q9R1E9; -.
DR PRIDE; Q9R1E9; -.
DR GeneID; 64032; -.
DR KEGG; rno:64032; -.
DR CTD; 1490; -.
DR RGD; 621392; Ccn2.
DR VEuPathDB; HostDB:ENSRNOG00000015036; -.
DR eggNOG; ENOG502QQDX; Eukaryota.
DR HOGENOM; CLU_063247_1_0_1; -.
DR InParanoid; Q9R1E9; -.
DR OMA; QDCGGQC; -.
DR OrthoDB; 999958at2759; -.
DR PhylomeDB; Q9R1E9; -.
DR TreeFam; TF326070; -.
DR PRO; PR:Q9R1E9; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000015036; Expressed in lung and 20 other tissues.
DR ExpressionAtlas; Q9R1E9; baseline and differential.
DR Genevisible; Q9R1E9; RN.
DR GO; GO:0005938; C:cell cortex; IDA:RGD.
DR GO; GO:0005801; C:cis-Golgi network; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0031012; C:extracellular matrix; ISO:RGD.
DR GO; GO:0005576; C:extracellular region; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0001968; F:fibronectin binding; IDA:RGD.
DR GO; GO:0008083; F:growth factor activity; IDA:RGD.
DR GO; GO:0008201; F:heparin binding; ISO:RGD.
DR GO; GO:0005178; F:integrin binding; ISO:RGD.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0001525; P:angiogenesis; ISO:RGD.
DR GO; GO:0097553; P:calcium ion transmembrane import into cytosol; IMP:RGD.
DR GO; GO:0001502; P:cartilage condensation; ISO:RGD.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; ISO:RGD.
DR GO; GO:0016477; P:cell migration; ISO:RGD.
DR GO; GO:0007160; P:cell-matrix adhesion; ISO:RGD.
DR GO; GO:0035988; P:chondrocyte proliferation; ISO:RGD.
DR GO; GO:0061448; P:connective tissue development; ISO:RGD.
DR GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0070278; P:extracellular matrix constituent secretion; IMP:RGD.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; ISO:RGD.
DR GO; GO:0035556; P:intracellular signal transduction; IDA:RGD.
DR GO; GO:0030324; P:lung development; IEP:RGD.
DR GO; GO:0060548; P:negative regulation of cell death; IMP:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:0001503; P:ossification; ISO:RGD.
DR GO; GO:0060452; P:positive regulation of cardiac muscle contraction; IMP:RGD.
DR GO; GO:0050867; P:positive regulation of cell activation; IMP:RGD.
DR GO; GO:0010942; P:positive regulation of cell death; IMP:RGD.
DR GO; GO:0045597; P:positive regulation of cell differentiation; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:RGD.
DR GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IMP:RGD.
DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:RGD.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:RGD.
DR GO; GO:0070318; P:positive regulation of G0 to G1 transition; IMP:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:RGD.
DR GO; GO:0046330; P:positive regulation of JNK cascade; ISO:RGD.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:RGD.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; ISO:RGD.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; ISO:RGD.
DR GO; GO:0032330; P:regulation of chondrocyte differentiation; ISO:RGD.
DR GO; GO:0043200; P:response to amino acid; IEP:RGD.
DR GO; GO:0034059; P:response to anoxia; IEP:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0070542; P:response to fatty acid; IEP:RGD.
DR GO; GO:0009749; P:response to glucose; IEP:RGD.
DR GO; GO:0051385; P:response to mineralocorticoid; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0001894; P:tissue homeostasis; ISO:RGD.
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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..347
FT /note="CCN family member 2"
FT /id="PRO_0000014405"
FT DOMAIN 25..96
FT /note="IGFBP N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT DOMAIN 99..165
FT /note="VWFC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 196..241
FT /note="TSP type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 254..328
FT /note="CTCK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT REGION 245..347
FT /note="Heparin-binding"
FT /evidence="ECO:0000250|UniProtKB:P29279"
FT DISULFID 254..291
FT /evidence="ECO:0000250"
FT DISULFID 271..305
FT /evidence="ECO:0000250"
FT DISULFID 282..321
FT /evidence="ECO:0000250"
FT DISULFID 285..323
FT /evidence="ECO:0000250"
FT DISULFID 290..327
FT /evidence="ECO:0000250"
FT CONFLICT 35
FT /note="A -> R (in Ref. 2; BAA82125)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="T -> P (in Ref. 2; BAA82125)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 347 AA; 37756 MW; CFBE1A19766B7B16 CRC64;
MLASVAGPVS LALVLLLCTR PATGQDCSAQ CQCAAEAAPR CPAGVSLVLD GCGCCRVCAK
QLGELCTERD PCDPHKGLFC DFGSPANRKI GVCTAKDGAP CVFGGSVYRS GESFQSSCKY
QCTCLDGAVG CVPLCSMDVR LPSPDCPFPR RVKLPGKCCE EWVCDEPKDR TVVGPALAAY
RLEDTFGPDP TMMRANCLVQ TTEWSACSKT CGMGISTRVT NDNTFCRLEK QSRLCMVRPC
EADLEENIKK GKKCIRTPKI AKPVKFELSG CTSVKTYRAK FCGVCTDGRC CTPHRTTTLP
VEFKCPDGEI MKKNMMFIKT CACHYNCPGD NDIFESLYYR KMYGDMA
