MYCT_RAT
ID MYCT_RAT Reviewed; 637 AA.
AC Q921A2;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Proton myo-inositol cotransporter {ECO:0000305};
DE Short=H(+)-myo-inositol cotransporter {ECO:0000303|PubMed:11500374};
DE Short=Hmit {ECO:0000303|PubMed:11500374};
DE AltName: Full=H(+)-myo-inositol symporter {ECO:0000303|PubMed:11500374};
DE AltName: Full=Solute carrier family 2 member 13;
GN Name=Slc2a13 {ECO:0000312|RGD:621814};
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 SUBCELLULAR LOCATION.
RX PubMed=11500374; DOI=10.1093/emboj/20.16.4467;
RA Uldry M., Ibberson M., Horisberger J.-D., Chatton J.-Y., Riederer B.M.,
RA Thorens B.;
RT "Identification of a mammalian H(+)-myo-inositol symporter expressed
RT predominantly in the brain.";
RL EMBO J. 20:4467-4477(2001).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44; SER-47; SER-629 AND
RP SER-634, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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).
CC -!- FUNCTION: H(+)-myo-inositol cotransporter (PubMed:11500374). Can also
CC transport related stereoisomers (PubMed:11500374).
CC {ECO:0000269|PubMed:11500374}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(out) + myo-inositol(out) = H(+)(in) + myo-inositol(in);
CC Xref=Rhea:RHEA:60364, ChEBI:CHEBI:15378, ChEBI:CHEBI:17268;
CC Evidence={ECO:0000250|UniProtKB:Q96QE2};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11500374};
CC Multi-pass membrane protein {ECO:0000269|PubMed:11500374}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC51117.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ315643; CAC51117.1; ALT_INIT; mRNA.
DR RefSeq; NP_598295.2; NM_133611.2.
DR AlphaFoldDB; Q921A2; -.
DR SMR; Q921A2; -.
DR STRING; 10116.ENSRNOP00000021153; -.
DR GlyGen; Q921A2; 3 sites.
DR iPTMnet; Q921A2; -.
DR PhosphoSitePlus; Q921A2; -.
DR PaxDb; Q921A2; -.
DR PRIDE; Q921A2; -.
DR Ensembl; ENSRNOT00000021153; ENSRNOP00000021153; ENSRNOG00000015741.
DR GeneID; 171147; -.
DR KEGG; rno:171147; -.
DR CTD; 114134; -.
DR RGD; 621814; Slc2a13.
DR eggNOG; KOG0254; Eukaryota.
DR GeneTree; ENSGT00940000155870; -.
DR HOGENOM; CLU_001265_30_5_1; -.
DR InParanoid; Q921A2; -.
DR OMA; WAITASF; -.
DR OrthoDB; 326501at2759; -.
DR PhylomeDB; Q921A2; -.
DR TreeFam; TF314916; -.
DR Reactome; R-RNO-429593; Inositol transporters.
DR PRO; PR:Q921A2; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000015741; Expressed in Ammon's horn and 16 other tissues.
DR Genevisible; Q921A2; RN.
DR GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central.
DR GO; GO:0097450; C:astrocyte end-foot; IDA:ARUK-UCL.
DR GO; GO:0044297; C:cell body; IDA:ARUK-UCL.
DR GO; GO:0071944; C:cell periphery; IDA:ARUK-UCL.
DR GO; GO:0042995; C:cell projection; IDA:ARUK-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:ARUK-UCL.
DR GO; GO:0030426; C:growth cone; IDA:ARUK-UCL.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:RGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:ARUK-UCL.
DR GO; GO:0016020; C:membrane; IDA:ARUK-UCL.
DR GO; GO:0031090; C:organelle membrane; ISO:RGD.
DR GO; GO:0051117; F:ATPase binding; ISO:RGD.
DR GO; GO:0005365; F:myo-inositol transmembrane transporter activity; IDA:ARUK-UCL.
DR GO; GO:0005366; F:myo-inositol:proton symporter activity; ISO:RGD.
DR GO; GO:0002020; F:protease binding; ISO:RGD.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015798; P:myo-inositol transport; IDA:ARUK-UCL.
DR GO; GO:1902004; P:positive regulation of amyloid-beta formation; ISO:RGD.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR005828; MFS_sugar_transport-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR003663; Sugar/inositol_transpt.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR Pfam; PF00083; Sugar_tr; 2.
DR PRINTS; PR00171; SUGRTRNSPORT.
DR SUPFAM; SSF103473; SSF103473; 2.
DR TIGRFAMs; TIGR00879; SP; 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
DR PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..637
FT /note="Proton myo-inositol cotransporter"
FT /id="PRO_0000050457"
FT TOPO_DOM 1..65
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..86
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 87..114
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 136..137
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..167
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..201
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 223..228
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 250..313
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..334
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 335..352
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 353..373
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 374..382
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 383..403
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 404..497
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 498..518
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 519..538
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 539..559
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 560..562
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 563..583
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 584..637
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 16..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UHK1"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 629
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 634
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 422
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 447
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 474
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 637 AA; 69149 MW; E8539A372600FBD9 CRC64;
MSRKASEDVE YTLRSLSSLM GERRRRQPEP GAPGGERSLL AAESAASLQG AELERAARRQ
FQRDETPAFV YAAAAFSALG GFLFGYDTGV VSGAMLLLRR QMRLGAMWQE LLVSGAVGAA
AVAALAGGAL NGALGRRSAI LLASALCTVG SAVLAAAANK ETLLAGRLVV GLGIGIASMT
VPVYIAEVSP PNLRGRLVTI NTLFITGGQF FASVVDGAFS YLQKDGWRYM LGLAAIPAVI
QFLGFLFLPE SPRWLIQKGQ TQKARRILSQ MRGNQTIDEE YDSIRNSIEE EEKEASAAGP
IICRMLSYPP TRRALAVGCG LQMFQQLSGI NTIMYYSATI LQMSGVEDDR LAIWLASITA
FTNFIFTLVG VWLVEKVGRR KLTFGSLAGT TVALTILALG FLLSAQVSPR VTFRPTAPSG
QNATCTEYSY CNECMLDPDC GFCYKINSSA VIDSSCVPVN KASTNEAAWG RCENETKFKA
EDVHWAYSFC PTPYSWTALV GLVLYLVFFA PGMGPMPWTV NSEIYPLWAR STGNACSAGI
NWIFNVLVSL TFLHTAEYLT YYGAFFLYAG FAAVGLLFVY GCLPETKGKK LEEIESLFDH
RLCTCGTADS DEGRYIEYIR VKGSNYHLSD NDASDVE
