TARG1_RAT
ID TARG1_RAT Reviewed; 173 AA.
AC Q2MHH0;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Trafficking regulator of GLUT4 1;
DE AltName: Full=Brain endothelial cell-derived protein 1;
DE Short=BEC-1;
DE AltName: Full=Dispanin subfamily B member 1;
DE Short=DSPB1;
DE AltName: Full=Tumor suppressor candidate 5 homolog;
GN Name=Trarg1 {ECO:0000312|RGD:1307639}; Synonyms=Tusc5;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=17007998; DOI=10.1016/j.mce.2006.08.007;
RA Shibata T., Koide H., Hayashi R., Nagata K., Takeo C., Yoshida T.,
RA Noguchi Y., Tanaka T., Saito Y., Tatsuno I.;
RT "Molecular cloning and characterization of rat brain endothelial cell
RT derived gene-1 (tumor suppressor candidate 5) expressing abundantly in
RT adipose tissues.";
RL Mol. Cell. Endocrinol. 263:38-45(2007).
RN [2]
RP INDUCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=17592729; DOI=10.1016/j.bbrc.2007.06.034;
RA Koide H., Shibata T., Yamada N., Asaki T., Nagao T., Yoshida T.,
RA Noguchi Y., Tanaka T., Saito Y., Tatsuno I.;
RT "Tumor suppressor candidate 5 (TUSC5) is expressed in brown adipocytes.";
RL Biochem. Biophys. Res. Commun. 360:139-145(2007).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-43; SER-45; SER-70;
RP SER-84 AND SER-85, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [4]
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 [5]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND FUNCTION.
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).
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:0000305|PubMed:17007998, ECO:0000305|PubMed:26240143}.
CC -!- SUBUNIT: Interacts with SLC2A4; the interaction is required for proper
CC SLC2A4 reacycling after insulin stimulation.
CC {ECO:0000250|UniProtKB:Q8C838}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8C838};
CC Single-pass membrane protein {ECO:0000305}. Endomembrane system
CC {ECO:0000269|PubMed:26240143}; Single-pass membrane protein
CC {ECO:0000305}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:26240143}. Note=Shifts from low-density microsome
CC vesicles to the cell membrane upon insulin stimulation.
CC {ECO:0000250|UniProtKB:Q8C838}.
CC -!- TISSUE SPECIFICITY: Present in adipose tissue and undetectable in other
CC tissues (at protein level). {ECO:0000269|PubMed:17007998,
CC ECO:0000269|PubMed:17592729, ECO:0000269|PubMed:26240143}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated during differentiation in primary
CC cultured rat brown preadipocytes. {ECO:0000269|PubMed:17592729}.
CC -!- INDUCTION: Down-regulated upon cold exposure in brown adipose tissue in
CC Zucker lean rats. Down-regulated by dexamethasone.
CC {ECO:0000269|PubMed:17592729}.
CC -!- SIMILARITY: Belongs to the CD225/Dispanin family. {ECO:0000305}.
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DR EMBL; AB218813; BAE75899.1; -; mRNA.
DR RefSeq; NP_001034252.1; NM_001039163.1.
DR AlphaFoldDB; Q2MHH0; -.
DR STRING; 10116.ENSRNOP00000063657; -.
DR iPTMnet; Q2MHH0; -.
DR PhosphoSitePlus; Q2MHH0; -.
DR PaxDb; Q2MHH0; -.
DR PRIDE; Q2MHH0; -.
DR Ensembl; ENSRNOT00000063941; ENSRNOP00000063657; ENSRNOG00000022239.
DR GeneID; 360576; -.
DR KEGG; rno:360576; -.
DR CTD; 286753; -.
DR RGD; 1307639; Trarg1.
DR eggNOG; ENOG502RY44; Eukaryota.
DR GeneTree; ENSGT00940000160337; -.
DR HOGENOM; CLU_103195_0_0_1; -.
DR InParanoid; Q2MHH0; -.
DR OMA; MQQGNVD; -.
DR OrthoDB; 1467259at2759; -.
DR PRO; PR:Q2MHH0; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000022239; Expressed in pancreas and 16 other tissues.
DR ExpressionAtlas; Q2MHH0; baseline and differential.
DR Genevisible; Q2MHH0; RN.
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; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
DR GO; GO:0099638; P:endosome to plasma membrane protein transport; ISS:UniProtKB.
DR GO; GO:0044381; P:glucose import in response to insulin stimulus; ISS:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
DR GO; GO:0099500; P:vesicle fusion to plasma membrane; ISO:RGD.
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_0000263641"
FT TOPO_DOM 1..102
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8C838"
FT INTRAMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 124..150
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8C838"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 172..173
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q8C838"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 173 AA; 18722 MW; D041DD49A25B55C3 CRC64;
MANPVQPQLQ DPGSTSPLDL PEMEKLLTKV ENKDDQALNL SKSLSGALDL EQNGHSLPFK
VISEGHRQPS LSGSPSRASS RRASSVVTTS YAQDQEAPKD YLVLAIASCF CPVWPLNLIP
LIFSIMSRSS VQQGDLDGAR RLGRLARLLS ITFIILGIVI IIVAVTVNFT VPK
