CCN5_MOUSE
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 25-MAY-2022, entry version 138.
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}.
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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 GlyGen; Q9Z0G4; 1 site.
DR MaxQB; Q9Z0G4; -.
DR PaxDb; Q9Z0G4; -.
DR PRIDE; Q9Z0G4; -.
DR ProteomicsDB; 297850; -.
DR DNASU; 22403; -.
DR GeneID; 22403; -.
DR KEGG; mmu:22403; -.
DR CTD; 8839; -.
DR MGI; MGI:1328326; Ccn5.
DR eggNOG; ENOG502RXIT; Eukaryota.
DR InParanoid; Q9Z0G4; -.
DR OrthoDB; 999958at2759; -.
DR PhylomeDB; Q9Z0G4; -.
DR BioGRID-ORCS; 22403; 2 hits in 73 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:0005737; C:cytoplasm; 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:0060548; P:negative regulation of cell death; 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; 2.20.100.10; -; 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 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; SSF57184; SSF57184; 1.
DR SUPFAM; SSF82895; SSF82895; 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; Glycoprotein; Reference proteome; Secreted; 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..94
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 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
