TARG1_MOUSE
ID TARG1_MOUSE Reviewed; 173 AA.
AC Q8C838;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Trafficking regulator of GLUT4 1 {ECO:0000305};
DE AltName: Full=Dispanin subfamily B member 1;
DE Short=DSPB1;
DE AltName: Full=Tumor suppressor candidate 5 homolog;
GN Name=Trarg1; Synonyms=Tusc5 {ECO:0000312|MGI:MGI:3029307};
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=Head, and Inner ear;
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 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP GENE FAMILY.
RX PubMed=22363774; DOI=10.1371/journal.pone.0031961;
RA Sallman Almen M., Bringeland N., Fredriksson R., Schioth H.B.;
RT "The dispanins: a novel gene family of ancient origin that contains 14
RT human members.";
RL PLoS ONE 7:E31961-E31961(2012).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION BY TNF.
RX PubMed=26240143; DOI=10.1074/jbc.m115.657361;
RA Fazakerley D.J., Naghiloo S., Chaudhuri R., Koumanov F., Burchfield J.G.,
RA Thomas K.C., Krycer J.R., Prior M.J., Parker B.L., Murrow B.A.,
RA Stoeckli J., Meoli C.C., Holman G.D., James D.E.;
RT "Proteomic Analysis of GLUT4 Storage Vesicles Reveals Tumor Suppressor
RT Candidate 5 (TUSC5) as a Novel Regulator of Insulin Action in Adipocytes.";
RL J. Biol. Chem. 290:23528-23542(2015).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH
RP SLC2A4, DISRUPTION PHENOTYPE, AND INDUCTION BY PPARG.
RX PubMed=26629404; DOI=10.1016/j.molmet.2015.08.003;
RA Beaton N., Rudigier C., Moest H., Mueller S., Mrosek N., Roeder E.,
RA Rudofsky G., Ruelicke T., Ukropec J., Ukropcova B., Augustin R.,
RA Neubauer H., Wolfrum C.;
RT "TUSC5 regulates insulin-mediated adipose tissue glucose uptake by
RT modulation of GLUT4 recycling.";
RL Mol. Metab. 4:795-810(2015).
RN [8]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=29787242; DOI=10.1021/acs.biochem.8b00361;
RA Duan X., Krycer J.R., Cooke K.C., Yang G., James D.E., Fazakerley D.J.;
RT "Membrane Topology of Trafficking Regulator of GLUT4 1 (TRARG1).";
RL Biochemistry 57:3606-3615(2018).
CC -!- FUNCTION: Regulates insulin-mediated adipose tissue glucose uptake and
CC transport by modulation of SLC2A4 recycling. Not required for SLC2A4
CC membrane fusion upon an initial stimulus, but rather is necessary for
CC proper protein recycling during prolonged insulin stimulation.
CC {ECO:0000269|PubMed:26240143, ECO:0000269|PubMed:26629404}.
CC -!- SUBUNIT: Interacts with SLC2A4; the interaction is required for proper
CC SLC2A4 reacycling after insulin stimulation.
CC {ECO:0000269|PubMed:26629404}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26240143,
CC ECO:0000269|PubMed:26629404, ECO:0000269|PubMed:29787242}; Single-pass
CC membrane protein {ECO:0000305|PubMed:29787242}. Endomembrane system
CC {ECO:0000269|PubMed:26240143, ECO:0000269|PubMed:26629404}; Single-pass
CC membrane protein {ECO:0000305|PubMed:29787242}. Cytoplasm, perinuclear
CC region {ECO:0000269|PubMed:26240143}. Note=Shifts from low-density
CC microsome vesicles to the cell membrane upon insulin stimulation.
CC {ECO:0000269|PubMed:26240143, ECO:0000269|PubMed:26629404}.
CC -!- TISSUE SPECIFICITY: Expressed specifically in white and brown adipose
CC tissues. {ECO:0000269|PubMed:26240143, ECO:0000269|PubMed:26629404}.
CC -!- INDUCTION: Target gene of PPARG, expression is induced upon PPARG
CC activation (PubMed:26629404, PubMed:26240143). Expression is inhibited
CC by TNF (PubMed:26240143). {ECO:0000269|PubMed:26240143,
CC ECO:0000269|PubMed:26629404}.
CC -!- DISRUPTION PHENOTYPE: Mutant adipocytes show reduced glucose uptake in
CC response to an insulin stimulus (PubMed:26629404). Knockout animals
CC placed on high-fat diet along with wild-type littermates exhibit an
CC increased weight gain, significant elevated blood insulin and glucose
CC levelswith insulin resistance (PubMed:26629404).
CC {ECO:0000269|PubMed:26629404}.
CC -!- SIMILARITY: Belongs to the CD225/Dispanin family. {ECO:0000305}.
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DR EMBL; AK048522; BAC33359.1; -; mRNA.
DR EMBL; AK158395; BAE34485.1; -; mRNA.
DR EMBL; BX000359; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC119801; AAI19802.1; -; mRNA.
DR EMBL; BC122875; AAI22876.1; -; mRNA.
DR CCDS; CCDS25069.1; -.
DR RefSeq; NP_808377.1; NM_177709.3.
DR AlphaFoldDB; Q8C838; -.
DR STRING; 10090.ENSMUSP00000061634; -.
DR iPTMnet; Q8C838; -.
DR PhosphoSitePlus; Q8C838; -.
DR SwissPalm; Q8C838; -.
DR jPOST; Q8C838; -.
DR MaxQB; Q8C838; -.
DR PaxDb; Q8C838; -.
DR PeptideAtlas; Q8C838; -.
DR PRIDE; Q8C838; -.
DR ProteomicsDB; 298338; -.
DR Antibodypedia; 58595; 157 antibodies from 27 providers.
DR DNASU; 237858; -.
DR Ensembl; ENSMUST00000062024; ENSMUSP00000061634; ENSMUSG00000046275.
DR GeneID; 237858; -.
DR KEGG; mmu:237858; -.
DR UCSC; uc007kfy.2; mouse.
DR CTD; 286753; -.
DR MGI; MGI:3029307; Trarg1.
DR VEuPathDB; HostDB:ENSMUSG00000046275; -.
DR eggNOG; ENOG502RY44; Eukaryota.
DR GeneTree; ENSGT00940000160337; -.
DR HOGENOM; CLU_103195_0_0_1; -.
DR InParanoid; Q8C838; -.
DR OMA; MQQGNVD; -.
DR OrthoDB; 1467259at2759; -.
DR PhylomeDB; Q8C838; -.
DR TreeFam; TF333012; -.
DR BioGRID-ORCS; 237858; 3 hits in 71 CRISPR screens.
DR PRO; PR:Q8C838; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8C838; protein.
DR Bgee; ENSMUSG00000046275; Expressed in lumbar dorsal root ganglion and 70 other tissues.
DR Genevisible; Q8C838; MM.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IDA:UniProtKB.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IDA:UniProtKB.
DR GO; GO:0099638; P:endosome to plasma membrane protein transport; IDA:UniProtKB.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0044381; P:glucose import in response to insulin stimulus; IDA:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; IDA:UniProtKB.
DR GO; GO:0099500; P:vesicle fusion to plasma membrane; IMP:MGI.
DR InterPro; IPR007593; CD225/Dispanin_fam.
DR Pfam; PF04505; CD225; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..173
FT /note="Trafficking regulator of GLUT4 1"
FT /id="PRO_0000263640"
FT TOPO_DOM 1..102
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:29787242"
FT INTRAMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 124..150
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:29787242"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 172..173
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:29787242"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2MHH0"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2MHH0"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2MHH0"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2MHH0"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2MHH0"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2MHH0"
SQ SEQUENCE 173 AA; 18719 MW; A57DA2E8C27BBE53 CRC64;
MANPAQPPLQ DPGSTSPLEL PEMEKLLTKV ENKDDQALNL SKSLSGALDL EQNGHSLPFK
VISEGHRQPS LSGSPSRVSS RRASSVITTS YAQDQEAPKD YLVLAIASCF CPVWPLNLIP
LIFSIMSRSS VQQGDLDGAR RLGRLARLLS ITFIILGIVI IIVAVTVNFT VPK
