CCN2_HUMAN
ID CCN2_HUMAN Reviewed; 349 AA.
AC P29279; E1P578; Q6LCY0; Q96A79; Q96QX2; Q9UDL6;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=CCN family member 2 {ECO:0000305};
DE AltName: Full=Cellular communication network factor 2 {ECO:0000312|HGNC:HGNC:2500};
DE AltName: Full=Connective tissue growth factor {ECO:0000303|PubMed:1654338};
DE AltName: Full=Hypertrophic chondrocyte-specific protein 24 {ECO:0000303|PubMed:10614647};
DE AltName: Full=Insulin-like growth factor-binding protein 8;
DE Short=IBP-8;
DE Short=IGF-binding protein 8;
DE Short=IGFBP-8;
DE Flags: Precursor;
GN Name=CCN2 {ECO:0000312|HGNC:HGNC:2500};
GN Synonyms=CTGF {ECO:0000303|PubMed:1654338},
GN HCS24 {ECO:0000303|PubMed:10614647}, IGFBP8;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, AND VARIANT ASP-83.
RC TISSUE=Umbilical vein endothelial cell;
RX PubMed=1654338; DOI=10.1083/jcb.114.6.1285;
RA Bradham D.M., Igarashi A., Potter R.L., Grotendorst G.R.;
RT "Connective tissue growth factor: a cysteine-rich mitogen secreted by human
RT vascular endothelial cells is related to the SRC-induced immediate early
RT gene product CEF-10.";
RL J. Cell Biol. 114:1285-1294(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ASP-83.
RC TISSUE=Umbilical vein endothelial cell;
RX PubMed=1293144; DOI=10.1111/j.1346-8138.1992.tb03748.x;
RA Igarashi A., Bradham D.M., Okochi H., Grotendorst G.R.;
RT "Connective tissue growth factor.";
RL J. Dermatol. 19:642-643(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ASP-83.
RC TISSUE=Aorta;
RX PubMed=9054739; DOI=10.1161/01.cir.95.4.831;
RA Oemar B.S., Werner A., Garnier J.-M., Do D.D., Godoy N., Nauck M., Marz W.,
RA Rupp J., Pech M., Luescher T.F.;
RT "Human connective tissue growth factor is expressed in advanced
RT atherosclerotic lesions.";
RL Circulation 95:831-839(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ASP-83.
RA Li Q.-H., Wang L.-C., Liu L.-D., Dong S.-Z., Wang J.-J., Hu F., Wang J.,
RA He S.-Q., Dong C.-H., Zhao S.-D., Zhao H.-L.;
RT "Expression, purification and bio-activity of human connective tissue
RT growth factor.";
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ASP-83.
RC TISSUE=Liver;
RA Dai W.-J., Jiang H.-C., Fu S.-B.;
RT "Complete mRNA sequence of human connective tissue growth factor.";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ASP-83.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ASP-83.
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
RC TISSUE=Placenta;
RA Xin L.W., Martinerie C., Zumkeller W., Westphal M., Perbal B.;
RT "Differential expression of novH and CTGF in human glioma cell lines.";
RL Clin. Mol. Pathol. 49:91-97(1996).
RN [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
RA Blom I.E., van Dijk A.J., de Weger R.A., Tilanus M.G.J., Goldschmeding R.;
RT "Identification of human CCN2 (connective tissue growth factor) promoter
RT polymorphisms.";
RL J. Clin. Pathol. 54:192-196(2001).
RN [12]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 75-349, AND VARIANT ASP-83.
RA Cody C.W., Walker N.J., Greenlee W.F., Sutter T.R.;
RT "Connective tissue growth factor mRNA is expressed in human keratinocytes
RT as an immediate early gene that responds to serum, EGF, or wounding.";
RL Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN [13]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 99-176 AND 204-225 (ISOFORM 1), AND TISSUE
RP SPECIFICITY.
RX PubMed=1756408;
RA Martinerie C., Perbal B.;
RT "Expression of a gene encoding a novel potential IGF binding protein in
RT human tissues.";
RL C. R. Acad. Sci. III, Sci. Vie 313:345-351(1991).
RN [14]
RP FUNCTION.
RC TISSUE=Chondrocyte;
RX PubMed=10614647; DOI=10.1210/endo.141.1.7267;
RA Nakanishi T., Nishida T., Shimo T., Kobayashi K., Kubo T., Tamatani T.,
RA Tezuka K., Takigawa M.;
RT "Effects of CTGF/Hcs24, a product of a hypertrophic chondrocyte-specific
RT gene, on the proliferation and differentiation of chondrocytes in
RT culture.";
RL Endocrinology 141:264-273(2000).
RN [15]
RP HEPARIN-BINDING, AND FUNCTION IN CELL ADHESION.
RX PubMed=12553878; DOI=10.1677/joe.0.176r001;
RA Ball D.K., Rachfal A.W., Kemper S.A., Brigstock D.R.;
RT "The heparin-binding 10 kDa fragment of connective tissue growth factor
RT (CTGF) containing module 4 alone stimulates cell adhesion.";
RL J. Endocrinol. 176:R1-R7(2003).
RN [16]
RP INTERACTION WITH TSKU.
RX PubMed=30232710; DOI=10.1007/s12079-018-0487-x;
RA Ohta K., Aoyama E., Ahmad S.A.I., Ito N., Anam M.B., Kubota S.,
RA Takigawa M.;
RT "CCN2/CTGF binds the small leucine rich proteoglycan protein Tsukushi.";
RL J. Cell Commun. Signal. 13:113-118(2019).
CC -!- FUNCTION: Major connective tissue mitoattractant secreted by vascular
CC endothelial cells. Promotes proliferation and differentiation of
CC chondrocytes. Mediates heparin- and divalent cation-dependent cell
CC adhesion in many cell types including fibroblasts, myofibroblasts,
CC endothelial and epithelial cells. Enhances fibroblast growth factor-
CC induced DNA synthesis. {ECO:0000269|PubMed:10614647,
CC ECO:0000269|PubMed:12553878}.
CC -!- SUBUNIT: Monomer (PubMed:1654338). Interacts with TSKU
CC (PubMed:30232710). {ECO:0000269|PubMed:1654338,
CC ECO:0000269|PubMed:30232710}.
CC -!- INTERACTION:
CC P29279; P03372: ESR1; NbExp=7; IntAct=EBI-2835375, EBI-78473;
CC P29279; Q92731: ESR2; NbExp=5; IntAct=EBI-2835375, EBI-78505;
CC P29279; P02751: FN1; NbExp=5; IntAct=EBI-2835375, EBI-1220319;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250|UniProtKB:P29268}. Secreted
CC {ECO:0000250|UniProtKB:P29268}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Long;
CC IsoId=P29279-1; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=P29279-2; Sequence=VSP_002460;
CC -!- TISSUE SPECIFICITY: Expressed in bone marrow and thymic cells. Also
CC expressed one of two Wilms tumors tested. {ECO:0000269|PubMed:1756408}.
CC -!- SIMILARITY: Belongs to the CCN family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/CTGFID40192ch6q23.html";
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DR EMBL; M92934; AAA91279.1; -; mRNA.
DR EMBL; X78947; CAA55544.1; -; mRNA.
DR EMBL; AY395801; AAQ95223.1; -; mRNA.
DR EMBL; AY550024; AAS55639.1; -; mRNA.
DR EMBL; BT019794; AAV38597.1; -; mRNA.
DR EMBL; BT019795; AAV38598.1; -; mRNA.
DR EMBL; CR541759; CAG46559.1; -; mRNA.
DR EMBL; AL354866; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X92511; CAA63267.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48038.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48039.1; -; Genomic_DNA.
DR EMBL; AF316366; AAK60505.1; -; Genomic_DNA.
DR EMBL; AF316367; AAK60506.1; -; Genomic_DNA.
DR EMBL; AF316368; AAK60507.1; -; Genomic_DNA.
DR EMBL; U14750; AAA75378.1; -; mRNA.
DR CCDS; CCDS5151.1; -. [P29279-1]
DR PIR; A40551; A40551.
DR RefSeq; NP_001892.1; NM_001901.2. [P29279-1]
DR AlphaFoldDB; P29279; -.
DR SMR; P29279; -.
DR BioGRID; 107872; 19.
DR CORUM; P29279; -.
DR IntAct; P29279; 25.
DR MINT; P29279; -.
DR STRING; 9606.ENSP00000356954; -.
DR ChEMBL; CHEMBL3712901; -.
DR GlyGen; P29279; 3 sites.
DR iPTMnet; P29279; -.
DR PhosphoSitePlus; P29279; -.
DR BioMuta; CTGF; -.
DR DMDM; 116241320; -.
DR EPD; P29279; -.
DR jPOST; P29279; -.
DR MassIVE; P29279; -.
DR MaxQB; P29279; -.
DR PaxDb; P29279; -.
DR PeptideAtlas; P29279; -.
DR PRIDE; P29279; -.
DR ProteomicsDB; 54533; -. [P29279-1]
DR ProteomicsDB; 54534; -. [P29279-2]
DR ABCD; P29279; 3 sequenced antibodies.
DR Antibodypedia; 3916; 953 antibodies from 43 providers.
DR DNASU; 1490; -.
DR Ensembl; ENST00000367976.4; ENSP00000356954.3; ENSG00000118523.6. [P29279-1]
DR GeneID; 1490; -.
DR KEGG; hsa:1490; -.
DR MANE-Select; ENST00000367976.4; ENSP00000356954.3; NM_001901.4; NP_001892.2.
DR UCSC; uc003qcz.4; human. [P29279-1]
DR CTD; 1490; -.
DR DisGeNET; 1490; -.
DR GeneCards; CCN2; -.
DR HGNC; HGNC:2500; CCN2.
DR HPA; ENSG00000118523; Low tissue specificity.
DR MalaCards; CCN2; -.
DR MIM; 121009; gene.
DR neXtProt; NX_P29279; -.
DR OpenTargets; ENSG00000118523; -.
DR Orphanet; 220393; Diffuse cutaneous systemic sclerosis.
DR Orphanet; 220402; Limited cutaneous systemic sclerosis.
DR PharmGKB; PA27003; -.
DR VEuPathDB; HostDB:ENSG00000118523; -.
DR eggNOG; ENOG502QQDX; Eukaryota.
DR GeneTree; ENSGT00940000155019; -.
DR HOGENOM; CLU_063247_1_0_1; -.
DR InParanoid; P29279; -.
DR OMA; QDCGGQC; -.
DR OrthoDB; 999958at2759; -.
DR PhylomeDB; P29279; -.
DR TreeFam; TF326070; -.
DR PathwayCommons; P29279; -.
DR Reactome; R-HSA-2032785; YAP1- and WWTR1 (TAZ)-stimulated gene expression.
DR Reactome; R-HSA-8951671; RUNX3 regulates YAP1-mediated transcription.
DR SignaLink; P29279; -.
DR SIGNOR; P29279; -.
DR BioGRID-ORCS; 1490; 12 hits in 1074 CRISPR screens.
DR ChiTaRS; CTGF; human.
DR GeneWiki; CTGF; -.
DR GenomeRNAi; 1490; -.
DR Pharos; P29279; Tbio.
DR PRO; PR:P29279; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P29279; protein.
DR Bgee; ENSG00000118523; Expressed in tibia and 189 other tissues.
DR Genevisible; P29279; HS.
DR GO; GO:0005938; C:cell cortex; IEA:Ensembl.
DR GO; GO:0005801; C:cis-Golgi network; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; TAS:ProtInc.
DR GO; GO:0001968; F:fibronectin binding; IEA:Ensembl.
DR GO; GO:0008083; F:growth factor activity; IEA:Ensembl.
DR GO; GO:0008201; F:heparin binding; IBA:GO_Central.
DR GO; GO:0005520; F:insulin-like growth factor binding; TAS:ProtInc.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR GO; GO:0097553; P:calcium ion transmembrane import into cytosol; IEA:Ensembl.
DR GO; GO:0001502; P:cartilage condensation; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IEA:Ensembl.
DR GO; GO:0007160; P:cell-matrix adhesion; IEA:Ensembl.
DR GO; GO:0002062; P:chondrocyte differentiation; IEA:Ensembl.
DR GO; GO:0035988; P:chondrocyte proliferation; IEA:Ensembl.
DR GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008544; P:epidermis development; TAS:ProtInc.
DR GO; GO:0070278; P:extracellular matrix constituent secretion; IEA:Ensembl.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:Ensembl.
DR GO; GO:0030324; P:lung development; IEA:Ensembl.
DR GO; GO:0060548; P:negative regulation of cell death; IBA:GO_Central.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:0001503; P:ossification; IEA:Ensembl.
DR GO; GO:0060452; P:positive regulation of cardiac muscle contraction; IEA:Ensembl.
DR GO; GO:0050867; P:positive regulation of cell activation; IEA:Ensembl.
DR GO; GO:0010942; P:positive regulation of cell death; IEA:Ensembl.
DR GO; GO:0045597; P:positive regulation of cell differentiation; IDA:BHF-UCL.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IEA:Ensembl.
DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:BHF-UCL.
DR GO; GO:0070318; P:positive regulation of G0 to G1 transition; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IDA:BHF-UCL.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IDA:BHF-UCL.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; IEA:Ensembl.
DR GO; GO:0032330; P:regulation of chondrocyte differentiation; IEA:Ensembl.
DR GO; GO:0043200; P:response to amino acid; IEA:Ensembl.
DR GO; GO:0034059; P:response to anoxia; IEA:Ensembl.
DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR GO; GO:0070542; P:response to fatty acid; IEA:Ensembl.
DR GO; GO:0009749; P:response to glucose; IEA:Ensembl.
DR GO; GO:0051385; P:response to mineralocorticoid; IEA:Ensembl.
DR GO; GO:0043434; P:response to peptide hormone; IEA:Ensembl.
DR GO; GO:0009611; P:response to wounding; TAS:ProtInc.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0001894; P:tissue homeostasis; IEA:Ensembl.
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 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Disulfide bond; DNA synthesis;
KW Extracellular matrix; Glycoprotein; Heparin-binding; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..349
FT /note="CCN family member 2"
FT /id="PRO_0000014402"
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:0000269|PubMed:12553878"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 VAR_SEQ 172..198
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_002460"
FT VARIANT 83
FT /note="H -> D (in dbSNP:rs7451102)"
FT /evidence="ECO:0000269|PubMed:1293144,
FT ECO:0000269|PubMed:1654338, ECO:0000269|PubMed:9054739,
FT ECO:0000269|Ref.12, ECO:0000269|Ref.4, ECO:0000269|Ref.5,
FT ECO:0000269|Ref.6, ECO:0000269|Ref.7"
FT /id="VAR_027925"
FT CONFLICT 175
FT /note="V -> L (in Ref. 13; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 349 AA; 38091 MW; 62CF878C7F57EC1F CRC64;
MTAASMGPVR VAFVVLLALC SRPAVGQNCS GPCRCPDEPA PRCPAGVSLV LDGCGCCRVC
AKQLGELCTE RDPCDPHKGL FCHFGSPANR KIGVCTAKDG APCIFGGTVY RSGESFQSSC
KYQCTCLDGA VGCMPLCSMD VRLPSPDCPF PRRVKLPGKC CEEWVCDEPK DQTVVGPALA
AYRLEDTFGP DPTMIRANCL VQTTEWSACS KTCGMGISTR VTNDNASCRL EKQSRLCMVR
PCEADLEENI KKGKKCIRTP KISKPIKFEL SGCTSMKTYR AKFCGVCTDG RCCTPHRTTT
LPVEFKCPDG EVMKKNMMFI KTCACHYNCP GDNDIFESLY YRKMYGDMA
