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Database: UniProt
Entry: F7DSB8_MONDO
LinkDB: F7DSB8_MONDO
Original site: F7DSB8_MONDO 
ID   F7DSB8_MONDO            Unreviewed;       361 AA.
AC   F7DSB8;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 2.
DT   27-MAR-2024, entry version 74.
DE   RecName: Full=CCN family member 3 {ECO:0000256|ARBA:ARBA00039944};
DE   AltName: Full=Cellular communication network factor 3 {ECO:0000256|ARBA:ARBA00042352};
GN   Name=CCN3 {ECO:0000313|Ensembl:ENSMODP00000004913.3};
OS   Monodelphis domestica (Gray short-tailed opossum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Didelphimorphia; Didelphidae; Monodelphis.
OX   NCBI_TaxID=13616 {ECO:0000313|Ensembl:ENSMODP00000004913.3, ECO:0000313|Proteomes:UP000002280};
RN   [1] {ECO:0000313|Ensembl:ENSMODP00000004913.3, ECO:0000313|Proteomes:UP000002280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17495919; DOI=10.1038/nature05805;
RA   Mikkelsen T.S., Wakefield M.J., Aken B., Amemiya C.T., Chang J.L., Duke S.,
RA   Garber M., Gentles A.J., Goodstadt L., Heger A., Jurka J., Kamal M.,
RA   Mauceli E., Searle S.M., Sharpe T., Baker M.L., Batzer M.A., Benos P.V.,
RA   Belov K., Clamp M., Cook A., Cuff J., Das R., Davidow L., Deakin J.E.,
RA   Fazzari M.J., Glass J.L., Grabherr M., Greally J.M., Gu W., Hore T.A.,
RA   Huttley G.A., Kleber M., Jirtle R.L., Koina E., Lee J.T., Mahony S.,
RA   Marra M.A., Miller R.D., Nicholls R.D., Oda M., Papenfuss A.T., Parra Z.E.,
RA   Pollock D.D., Ray D.A., Schein J.E., Speed T.P., Thompson K.,
RA   VandeBerg J.L., Wade C.M., Walker J.A., Waters P.D., Webber C.,
RA   Weidman J.R., Xie X., Zody M.C., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA   Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA   Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA   Bayul T., Berlin A., Bessette D., Bloom T., Bloom T., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA   Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA   D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA   Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA   Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA   Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA   Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA   Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA   Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA   Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA   Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA   Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA   McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA   Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA   Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA   Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA   Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA   Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA   Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA   Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA   Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA   Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA   Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA   Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA   Chin C., Gnerre S., MacCallum I., Graves J.A., Ponting C.P., Breen M.,
RA   Samollow P.B., Lander E.S., Lindblad-Toh K.;
RT   "Genome of the marsupial Monodelphis domestica reveals innovation in non-
RT   coding sequences.";
RL   Nature 447:167-177(2007).
RN   [2] {ECO:0000313|Ensembl:ENSMODP00000004913.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell junction, gap junction
CC       {ECO:0000256|ARBA:ARBA00004610}. Secreted
CC       {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the CCN family. {ECO:0000256|ARBA:ARBA00008125}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00039}.
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DR   RefSeq; XP_001381016.3; XM_001380979.4.
DR   AlphaFoldDB; F7DSB8; -.
DR   STRING; 13616.ENSMODP00000004913; -.
DR   Ensembl; ENSMODT00000005017.4; ENSMODP00000004913.3; ENSMODG00000003994.4.
DR   GeneID; 100031859; -.
DR   KEGG; mdo:100031859; -.
DR   CTD; 4856; -.
DR   eggNOG; ENOG502QR9V; Eukaryota.
DR   GeneTree; ENSGT00940000159963; -.
DR   HOGENOM; CLU_063247_1_0_1; -.
DR   InParanoid; F7DSB8; -.
DR   OMA; CACHTNC; -.
DR   OrthoDB; 2970572at2759; -.
DR   TreeFam; TF326070; -.
DR   Proteomes; UP000002280; Chromosome 3.
DR   Bgee; ENSMODG00000003994; Expressed in skeletal muscle tissue and 13 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005921; C:gap junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:Ensembl.
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:0005112; F:Notch binding; IEA:Ensembl.
DR   GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR   GO; GO:1990523; P:bone regeneration; IEA:Ensembl.
DR   GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR   GO; GO:0033627; P:cell adhesion mediated by integrin; IEA:Ensembl.
DR   GO; GO:0002062; P:chondrocyte differentiation; IEA:Ensembl.
DR   GO; GO:0035767; P:endothelial cell chemotaxis; IEA:Ensembl.
DR   GO; GO:0071603; P:endothelial cell-cell adhesion; IEA:Ensembl.
DR   GO; GO:0010761; P:fibroblast migration; IEA:Ensembl.
DR   GO; GO:0061484; P:hematopoietic stem cell homeostasis; IEA:Ensembl.
DR   GO; GO:0030308; P:negative regulation of cell growth; IEA:Ensembl.
DR   GO; GO:1902731; P:negative regulation of chondrocyte proliferation; IEA:Ensembl.
DR   GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
DR   GO; GO:0046676; P:negative regulation of insulin secretion; IEA:Ensembl.
DR   GO; GO:0090027; P:negative regulation of monocyte chemotaxis; IEA:Ensembl.
DR   GO; GO:0010832; P:negative regulation of myotube differentiation; IEA:Ensembl.
DR   GO; GO:1901223; P:negative regulation of non-canonical NF-kappaB signal transduction; IEA:Ensembl.
DR   GO; GO:0060392; P:negative regulation of SMAD protein signal transduction; IEA:Ensembl.
DR   GO; GO:0045747; P:positive regulation of Notch signaling pathway; IEA:Ensembl.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   GO; GO:0014909; P:smooth muscle cell migration; IEA:Ensembl.
DR   GO; GO:0048659; P:smooth muscle cell proliferation; IEA:Ensembl.
DR   GO; GO:0044342; P:type B pancreatic cell proliferation; IEA:Ensembl.
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; 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; IPR043973; TSP1_CCN.
DR   InterPro; IPR000884; TSP1_rpt.
DR   InterPro; IPR036383; TSP1_rpt_sf.
DR   InterPro; IPR001007; VWF_dom.
DR   PANTHER; PTHR11348:SF8; CCN FAMILY MEMBER 3; 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; 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; PS51323; IGFBP_N_2; 1.
DR   PROSITE; PS50092; TSP1; 1.
DR   PROSITE; PS01208; VWFC_1; 1.
DR   PROSITE; PS50184; VWFC_2; 1.
PE   3: Inferred from homology;
KW   Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Gap junction {ECO:0000256|ARBA:ARBA00022868};
KW   Growth factor {ECO:0000256|ARBA:ARBA00023030};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002280};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           36..361
FT                   /note="CCN family member 3"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003356528"
FT   DOMAIN          35..109
FT                   /note="IGFBP N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51323"
FT   DOMAIN          112..178
FT                   /note="VWFC"
FT                   /evidence="ECO:0000259|PROSITE:PS50184"
FT   DOMAIN          268..342
FT                   /note="CTCK"
FT                   /evidence="ECO:0000259|PROSITE:PS01225"
SQ   SEQUENCE   361 AA;  39953 MW;  3FF914B6852C6B16 CRC64;
     MQCGLLPPPG MRLQLQKQCL CLSFLLLLLL HKVVPAQSCP TPCPGQCPAQ PPACAPGVPA
     VLDRCSCCLV CARQRGESCS ELLPCQESSG LYCDRSADPR AEVGICMVLE EDNCVFDGII
     YRSGETFQPS CKYQCTCRDG QIGCVPRCNH DLLLPRPDCP FPRKVEVPGE CCEQWVCDPK
     EEVALGGLAL AAYRQEATLG IGVSDSSLNC IEQTTEWSAC SKSCGMGFST RVTNRNRHCE
     MTKQTRLCIV RPCEQEIEHA TEKKGKRCLR TKKSLKAIHL QYKNCTSTQT YKPRYCGICT
     DGRCCTPHNT KTIQVAFQCP QGQTVKKPMM LINTCACHTN CPQSNDAFHQ ALESKPRRMK
     I
//
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