ID CCN5_MOUSE Reviewed; 251 AA. AC Q9Z0G4; Q8CIC8; DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 08-NOV-2023, entry version 143. DE RecName: Full=CCN family member 5 {ECO:0000305}; DE AltName: Full=Connective tissue growth factor-like protein; DE Short=CTGF-L; DE AltName: Full=WNT1-inducible-signaling pathway protein 2; DE Short=WISP-2; DE Flags: Precursor; GN Name=Ccn5; Synonyms=Ctgfl, Wisp2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Mammary gland; RX PubMed=9843955; DOI=10.1073/pnas.95.25.14717; RA Pennica D., Swanson T.A., Welsh J.W., Roy M.A., Lawrence D.A., Lee J., RA Brush J., Taneyhill L.A., Deuel B., Lew M., Watanabe C., Cohen R.L., RA Melham M.F., Finley G.G., Quirke P., Goddard A.D., Hillan K.J., RA Gurney A.L., Botstein D., Levine A.J.; RT "WISP genes are members of the connective tissue growth factor family that RT are up-regulated in wnt-1-transformed cells and aberrantly expressed in RT human colon tumors."; RL Proc. Natl. Acad. Sci. U.S.A. 95:14717-14722(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Lung; RX PubMed=10358067; DOI=10.1074/jbc.274.24.17123; RA Kumar S., Hand A.T., Connor J.R., Dodds R.A., Ryan P.J., Trill J.J., RA Fisher S.M., Nuttall M.E., Lipshutz D.B., Zou C., Hwang S.M., Votta B.J., RA James I.E., Rieman D.J., Gowen M., Lee J.C.; RT "Identification and cloning of a connective tissue growth factor-like cDNA RT from human osteoblasts encoding a novel regulator of osteoblast RT functions."; RL J. Biol. Chem. 274:17123-17131(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: May play an important role in modulating bone turnover. CC Promotes the adhesion of osteoblast cells and inhibits the binding of CC fibrinogen to integrin receptors. In addition, inhibits osteocalcin CC production (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. CC -!- SIMILARITY: Belongs to the CCN family. {ECO:0000305}. 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; AF100778; AAC96320.1; -; mRNA. DR EMBL; AF126063; AAD18058.1; -; mRNA. DR EMBL; BC032877; AAH32877.1; -; mRNA. DR CCDS; CCDS17016.1; -. DR RefSeq; NP_058569.2; NM_016873.2. DR AlphaFoldDB; Q9Z0G4; -. DR SMR; Q9Z0G4; -. DR STRING; 10090.ENSMUSP00000029188; -. DR GlyCosmos; Q9Z0G4; 1 site, No reported glycans. DR GlyGen; Q9Z0G4; 1 site. DR MaxQB; Q9Z0G4; -. DR PaxDb; 10090-ENSMUSP00000029188; -. DR ProteomicsDB; 297850; -. DR DNASU; 22403; -. DR GeneID; 22403; -. DR KEGG; mmu:22403; -. DR AGR; MGI:1328326; -. DR CTD; 8839; -. DR MGI; MGI:1328326; Ccn5. DR eggNOG; ENOG502RXIT; Eukaryota. DR InParanoid; Q9Z0G4; -. DR OrthoDB; 2970572at2759; -. DR PhylomeDB; Q9Z0G4; -. DR BioGRID-ORCS; 22403; 2 hits in 78 CRISPR screens. DR ChiTaRS; Ccn5; mouse. DR PRO; PR:Q9Z0G4; -. DR Proteomes; UP000000589; Unplaced. DR RNAct; Q9Z0G4; Protein. DR GO; GO:0009986; C:cell surface; ISO:MGI. DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central. DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:MGI. DR GO; GO:0002102; C:podosome; ISO:MGI. DR GO; GO:0008083; F:growth factor activity; ISA:MGI. DR GO; GO:0008201; F:heparin binding; IBA:GO_Central. DR GO; GO:0005178; F:integrin binding; ISO:MGI. DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central. DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI. DR GO; GO:0001558; P:regulation of cell growth; IDA:MGI. DR GO; GO:0007165; P:signal transduction; IBA:GO_Central. DR Gene3D; 2.10.70.10; Complement Module, domain 1; 1. DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 1. DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf. DR InterPro; IPR000867; IGFBP-like. 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:SF22; CCN FAMILY MEMBER 5; 1. DR PANTHER; PTHR11348; CONNECTIVE TISSUE GROWTH FACTOR-RELATED; 1. DR Pfam; PF00219; IGFBP; 1. DR Pfam; PF19035; TSP1_CCN; 1. DR Pfam; PF00093; VWC; 1. DR SMART; SM00121; IB; 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; 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; Glycoprotein; Reference proteome; Secreted; KW Signal. FT SIGNAL 1..23 FT /evidence="ECO:0000255" FT CHAIN 24..251 FT /note="CCN family member 5" FT /id="PRO_0000014410" FT DOMAIN 24..103 FT /note="IGFBP N-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653" FT DOMAIN 98..164 FT /note="VWFC" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220" FT DOMAIN 195..239 FT /note="TSP type-1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210" FT CARBOHYD 197 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 26..50 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653" FT DISULFID 30..52 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653" FT DISULFID 32..53 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653" FT DISULFID 39..56 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653" FT DISULFID 64..78 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653" FT DISULFID 70..100 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653" FT CONFLICT 23 FT /note="S -> A (in Ref. 3; AAH32877)" FT /evidence="ECO:0000305" FT CONFLICT 71 FT /note="D -> N (in Ref. 3; AAH32877)" FT /evidence="ECO:0000305" FT CONFLICT 89 FT /note="A -> V (in Ref. 3; AAH32877)" FT /evidence="ECO:0000305" SQ SEQUENCE 251 AA; 27095 MW; 893E1633F6E5C7FC CRC64; MRGNPLIHLL AISFLCILSM VYSQLCPAPC ACPWTPPQCP PGVPLVLDGC GCCRVCARRL GESCDHLHVC DPSQGLVCQP GAGPSGRGAV CLFEEDDGSC EVNGRRYLDG ETFKPNCRVL CRCDDGGFTC LPLCSEDVRL PSWDCPRPRR IQVPGRCCPE WVCDQAVMQP AIQPSSAQGH QLSALVTPAS ADGPCPNWST AWGPCSTTCG LGIATRVSNQ NRFCQLEIQR RLCLSRPCLA SRSHGSWNSA F //