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CCN6_MOUSE
ID   CCN6_MOUSE              Reviewed;         354 AA.
AC   D3Z5L9;
DT   22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 2.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Cellular communication network factor 6;
DE   AltName: Full=CCN family member 6;
DE   AltName: Full=WNT1-inducible-signaling pathway protein 3 {ECO:0000303|PubMed:15601861};
DE            Short=WISP-3 {ECO:0000303|PubMed:15601861};
DE   Flags: Precursor;
GN   Name=Ccn6 {ECO:0000312|MGI:MGI:2685581};
GN   Synonyms=Wisp3 {ECO:0000303|PubMed:15601861};
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=15601861; DOI=10.1128/mcb.25.1.414-421.2005;
RA   Kutz W.E., Gong Y., Warman M.L.;
RT   "WISP3, the gene responsible for the human skeletal disease progressive
RT   pseudorheumatoid dysplasia, is not essential for skeletal function in
RT   mice.";
RL   Mol. Cell. Biol. 25:414-421(2005).
CC   -!- FUNCTION: Plays a role in mitochondrial electron transport and
CC       mitochondrial respiration. {ECO:0000250|UniProtKB:O95389}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O95389}.
CC       Mitochondrion {ECO:0000250|UniProtKB:O95389}. Note=Associated with
CC       membranes. {ECO:0000250|UniProtKB:O95389}.
CC   -!- DISRUPTION PHENOTYPE: Deficient mice are viable and fertile with no
CC       obvious abnormalities in size, weight, skeletal development,
CC       ossification, or the occurrence of joint disease.
CC       {ECO:0000269|PubMed:15601861}.
CC   -!- SIMILARITY: Belongs to the CCN family. {ECO:0000305}.
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DR   EMBL; AC153958; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS48537.1; -.
DR   RefSeq; NP_001120848.1; NM_001127376.1.
DR   AlphaFoldDB; D3Z5L9; -.
DR   SMR; D3Z5L9; -.
DR   STRING; 10090.ENSMUSP00000076003; -.
DR   GlyGen; D3Z5L9; 1 site.
DR   iPTMnet; D3Z5L9; -.
DR   PhosphoSitePlus; D3Z5L9; -.
DR   PaxDb; D3Z5L9; -.
DR   PeptideAtlas; D3Z5L9; -.
DR   PRIDE; D3Z5L9; -.
DR   ProteomicsDB; 297851; -.
DR   Antibodypedia; 32438; 192 antibodies from 25 providers.
DR   DNASU; 327743; -.
DR   Ensembl; ENSMUST00000076713; ENSMUSP00000076003; ENSMUSG00000062074.
DR   GeneID; 327743; -.
DR   KEGG; mmu:327743; -.
DR   UCSC; uc011xcu.1; mouse.
DR   CTD; 8838; -.
DR   MGI; MGI:2685581; Ccn6.
DR   VEuPathDB; HostDB:ENSMUSG00000062074; -.
DR   eggNOG; ENOG502QW30; Eukaryota.
DR   GeneTree; ENSGT00940000160119; -.
DR   HOGENOM; CLU_063247_2_0_1; -.
DR   InParanoid; D3Z5L9; -.
DR   OMA; LVQTTPW; -.
DR   OrthoDB; 601212at2759; -.
DR   PhylomeDB; D3Z5L9; -.
DR   TreeFam; TF326070; -.
DR   BioGRID-ORCS; 327743; 4 hits in 74 CRISPR screens.
DR   PRO; PR:D3Z5L9; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; D3Z5L9; protein.
DR   Bgee; ENSMUSG00000062074; Expressed in secondary oocyte and 39 other tissues.
DR   GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0008201; F:heparin binding; IBA:GO_Central.
DR   GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR   GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR   GO; GO:0016525; P:negative regulation of angiogenesis; ISO:MGI.
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:0051881; P:regulation of mitochondrial membrane potential; ISS:UniProtKB.
DR   GO; GO:1903426; P:regulation of reactive oxygen species biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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   Pfam; PF00007; Cys_knot; 1.
DR   Pfam; PF00219; IGFBP; 1.
DR   Pfam; PF19035; TSP1_CCN; 1.
DR   PIRSF; PIRSF036495; IGFBP_rP_CNN; 1.
DR   SMART; SM00041; CT; 1.
DR   SMART; SM00121; IB; 1.
DR   SMART; SM00209; TSP1; 1.
DR   SUPFAM; SSF57184; SSF57184; 1.
DR   SUPFAM; SSF82895; SSF82895; 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.
PE   3: Inferred from homology;
KW   Disulfide bond; Glycoprotein; Growth factor; Mitochondrion;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..354
FT                   /note="Cellular communication network factor 6"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000415855"
FT   DOMAIN          40..117
FT                   /note="IGFBP N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DOMAIN          208..253
FT                   /note="TSP type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          268..342
FT                   /note="CTCK"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT   CARBOHYD        308
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        209..238
FT                   /evidence="ECO:0000250"
FT   DISULFID        219..223
FT                   /evidence="ECO:0000250"
FT   DISULFID        247..252
FT                   /evidence="ECO:0000250"
FT   DISULFID        268..305
FT                   /evidence="ECO:0000250"
FT   DISULFID        285..319
FT                   /evidence="ECO:0000250"
FT   DISULFID        296..335
FT                   /evidence="ECO:0000250"
FT   DISULFID        299..337
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   354 AA;  39379 MW;  F45C5CD8896D1647 CRC64;
     MRRLLFCTLL MTGLTQLCCR TQGSAPQDST PGGRPGAALE VYQRTEVCRW PCRCPPQRPT
     CPPGVSLVRD GCGCCKVCAK QPGDTCNEAE ICDPHKGLYC DYSGDTPRYE TGVCAYLVAV
     GCEFNRVYYQ NGQVFQPHPL FSCLCVSGAI GCTPLFIPKL AGSNCSAAKG RRKTDPPNCG
     RGTLQQQNSA SYKTMSAYRN LPLTWRKKCL VQATKWTPCS RTCGMGISNR VTNDNANCEM
     RKERRLCYIQ PCSRNTSQAV KIPRGETCQP TFQLPKAEKF VFSGCSSTQS YRPTFCGICL
     DKRCCVPNKS KMITVRFDCP SEGSFKWQML WVTSCVCQRD CREPGDIFSE LRIL
 
 
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