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 27-MAR-2024, entry version 212. 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}, HCS24 GN {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="https://atlasgeneticsoncology.org/gene/40192/CTGF"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 23. DR CORUM; P29279; -. DR IntAct; P29279; 26. DR MINT; P29279; -. DR STRING; 9606.ENSP00000356954; -. DR ChEMBL; CHEMBL3712901; -. DR GlyCosmos; P29279; 2 sites, No reported glycans. DR GlyGen; P29279; 6 sites, 2 O-linked glycans (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; 9606-ENSP00000356954; -. DR PeptideAtlas; P29279; -. DR ProteomicsDB; 54533; -. [P29279-1] DR ProteomicsDB; 54534; -. [P29279-2] DR Pumba; P29279; -. DR ABCD; P29279; 3 sequenced antibodies. DR Antibodypedia; 3916; 1076 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 AGR; HGNC:2500; -. 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; ERDPCDH; -. DR OrthoDB; 2970572at2759; -. 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 1152 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 191 other cell types or tissues. DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0005886; C:plasma membrane; TAS:ProtInc. 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:0001525; P:angiogenesis; 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:0008543; P:fibroblast growth factor receptor signaling pathway; IEA:Ensembl. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:Ensembl. DR GO; GO:0030324; P:lung development; IEA:Ensembl. DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl. DR GO; GO:0001503; P:ossification; IEA:Ensembl. DR GO; GO:0045597; P:positive regulation of cell differentiation; IDA:BHF-UCL. DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:BHF-UCL. DR GO; GO:0046330; P:positive regulation of JNK cascade; IDA:BHF-UCL. 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: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; Thrombospondin type-1 (TSP1) repeat; 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 PANTHER; PTHR11348:SF7; CCN FAMILY MEMBER 2; 1. DR PANTHER; PTHR11348; CONNECTIVE TISSUE GROWTH FACTOR-RELATED; 1. 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; SSF57603; FnI-like domain; 1. DR SUPFAM; SSF57184; Growth factor receptor domain; 1. DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 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. DR Genevisible; P29279; HS. 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 29..54 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653" FT DISULFID 33..56 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653" FT DISULFID 35..57 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653" FT DISULFID 43..60 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653" FT DISULFID 68..82 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653" FT DISULFID 74..95 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653" 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 //