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CCDC3_MOUSE
ID   CCDC3_MOUSE             Reviewed;         273 AA.
AC   Q9D6Y1;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Coiled-coil domain-containing protein 3;
DE   AltName: Full=Fat/vessel-derived secretory protein;
DE            Short=Favine {ECO:0000303|PubMed:25605713};
DE   Flags: Precursor;
GN   Name=Ccdc3;
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 MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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).
RN   [3]
RP   PROTEIN SEQUENCE OF N-TERMINUS, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP   SUBUNIT, AND GLYCOSYLATION.
RX   PubMed=20043878; DOI=10.1016/j.bbrc.2009.12.142;
RA   Kobayashi S., Fukuhara A., Taguchi T., Matsuda M., Tochino Y., Otsuki M.,
RA   Shimomura I.;
RT   "Identification of a new secretory factor, CCDC3/Favine, in adipocytes and
RT   endothelial cells.";
RL   Biochem. Biophys. Res. Commun. 392:29-35(2010).
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=25605713; DOI=10.1074/jbc.m114.592493;
RA   Kobayashi S., Fukuhara A., Otsuki M., Suganami T., Ogawa Y., Morii E.,
RA   Shimomura I.;
RT   "Fat/vessel-derived secretory protein (Favine)/CCDC3 is involved in lipid
RT   accumulation.";
RL   J. Biol. Chem. 290:7443-7451(2015).
CC   -!- FUNCTION: Negatively regulates TNF-alpha-induced pro-inflammatory
CC       response in endothelial cells (ECs) via inhibition of TNF-alpha-induced
CC       NF-kappaB activation in ECs (By similarity). Positively regulates lipid
CC       accumulation in adipose cells (PubMed:25605713).
CC       {ECO:0000250|UniProtKB:Q9BQI4, ECO:0000269|PubMed:25605713}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20043878}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20043878}.
CC   -!- TISSUE SPECIFICITY: Expressed in aorta and adipose tissue. Enriched in
CC       mature adipocytes. Over-expressed in adipose tissue from either
CC       hormonally-induced or nutritionally-regulated obese mice models.
CC       {ECO:0000269|PubMed:20043878}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:20043878}.
CC   -!- DISRUPTION PHENOTYPE: Mice exhibit a lean phenotype with reduced fat
CC       mass and smaller adipocyte size compared to wild type mice. Adipose
CC       tissue exhibit decreased levels of lipogenic genes, such as fatty-acid
CC       synthase (FASN), acetyl-CoA carboxylase (ACACA) and diacylglycerol O-
CC       acyltransferase-2 (DGAT2). Mice exhibit strongly inhibited age-related
CC       hepatic steatosis and decreased number of inflammatory cells in
CC       epididymal adipose tissue. {ECO:0000269|PubMed:25605713}.
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DR   EMBL; AK009833; BAB26531.1; -; mRNA.
DR   EMBL; BC058616; AAH58616.1; -; mRNA.
DR   CCDS; CCDS15664.1; -.
DR   RefSeq; NP_083080.1; NM_028804.1.
DR   AlphaFoldDB; Q9D6Y1; -.
DR   SMR; Q9D6Y1; -.
DR   STRING; 10090.ENSMUSP00000027988; -.
DR   GlyGen; Q9D6Y1; 1 site.
DR   iPTMnet; Q9D6Y1; -.
DR   PhosphoSitePlus; Q9D6Y1; -.
DR   MaxQB; Q9D6Y1; -.
DR   PaxDb; Q9D6Y1; -.
DR   PRIDE; Q9D6Y1; -.
DR   ProteomicsDB; 265368; -.
DR   Antibodypedia; 55471; 95 antibodies from 23 providers.
DR   Ensembl; ENSMUST00000027988; ENSMUSP00000027988; ENSMUSG00000026676.
DR   GeneID; 74186; -.
DR   KEGG; mmu:74186; -.
DR   UCSC; uc008ifo.1; mouse.
DR   CTD; 83643; -.
DR   MGI; MGI:1921436; Ccdc3.
DR   VEuPathDB; HostDB:ENSMUSG00000026676; -.
DR   eggNOG; ENOG502QPN3; Eukaryota.
DR   GeneTree; ENSGT00390000014429; -.
DR   HOGENOM; CLU_085750_1_0_1; -.
DR   InParanoid; Q9D6Y1; -.
DR   OMA; QDYAYFF; -.
DR   OrthoDB; 1381750at2759; -.
DR   PhylomeDB; Q9D6Y1; -.
DR   TreeFam; TF331410; -.
DR   BioGRID-ORCS; 74186; 4 hits in 70 CRISPR screens.
DR   PRO; PR:Q9D6Y1; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q9D6Y1; protein.
DR   Bgee; ENSMUSG00000026676; Expressed in tarsal region and 173 other tissues.
DR   Genevisible; Q9D6Y1; MM.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR   GO; GO:0005576; C:extracellular region; IDA:MGI.
DR   GO; GO:0008610; P:lipid biosynthetic process; IDA:MGI.
DR   GO; GO:0010629; P:negative regulation of gene expression; IMP:MGI.
DR   GO; GO:0051055; P:negative regulation of lipid biosynthetic process; IMP:MGI.
DR   GO; GO:0045833; P:negative regulation of lipid metabolic process; ISO:MGI.
DR   GO; GO:0010804; P:negative regulation of tumor necrosis factor-mediated signaling pathway; ISS:UniProtKB.
DR   GO; GO:0045600; P:positive regulation of fat cell differentiation; IDA:MGI.
DR   GO; GO:0046889; P:positive regulation of lipid biosynthetic process; IDA:MGI.
DR   InterPro; IPR040311; CCDC3.
DR   PANTHER; PTHR31663; PTHR31663; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Direct protein sequencing; Glycoprotein; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|PubMed:20043878"
FT   CHAIN           22..273
FT                   /note="Coiled-coil domain-containing protein 3"
FT                   /id="PRO_0000020863"
FT   COILED          188..250
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        100
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305|PubMed:20043878"
SQ   SEQUENCE   273 AA;  31093 MW;  C6F94A2CAD606E79 CRC64;
     MPLPLLLAAL CLAASPAPAR ACQLPSEWRP LSEGCRAELA ETIVYAKVLA LHPEVPGLYN
     YLPWQYQAGE GGLFYSAEVE MLCDQAWGSM LEVPAGSRLN LTGLGYFSCH SHTVVQDYSY
     FFFVRMDENY NLLPHGVNFQ DAIFPDTQEN RRMFSSLFQF ANCSQGQQLT TFSSDWEVQE
     DNRLMCSSVQ KALFEEEDHV KKLQQKVATL EKRNRQLRER VKKVKRSLRQ ARKNSRHLEL
     VNQKLNEKLG ASSAQQHINA LGREPVRAPY LHG
 
 
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