GTR12_XENLA
ID GTR12_XENLA Reviewed; 588 AA.
AC Q32NG5;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Solute carrier family 2, facilitated glucose transporter member 12 {ECO:0000305};
DE AltName: Full=Glucose transporter type 12 {ECO:0000250|UniProtKB:Q8TD20};
DE Short=GLUT-12 {ECO:0000250|UniProtKB:Q8TD20};
GN Name=slc2a12 {ECO:0000250|UniProtKB:Q8TD20};
GN Synonyms=glut12 {ECO:0000250|UniProtKB:Q8TD20};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Insulin-regulated facilitative glucose transporter.
CC {ECO:0000250|UniProtKB:Q6NWF1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose(out) = D-glucose(in); Xref=Rhea:RHEA:60376,
CC ChEBI:CHEBI:4167; Evidence={ECO:0000250|UniProtKB:Q6NWF1};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8BFW9};
CC Multi-pass membrane protein {ECO:0000255}. Endomembrane system
CC {ECO:0000250|UniProtKB:Q5J316}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q8TD20}. Note=Localizes primarily perinuclear
CC region in the absence of insulin. {ECO:0000250|UniProtKB:Q8TD20}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. Glucose transporter subfamily.
CC {ECO:0000305}.
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DR EMBL; BC108638; AAI08639.1; -; mRNA.
DR RefSeq; NP_001089895.1; NM_001096426.1.
DR AlphaFoldDB; Q32NG5; -.
DR SMR; Q32NG5; -.
DR GeneID; 734962; -.
DR KEGG; xla:734962; -.
DR CTD; 734962; -.
DR Xenbase; XB-GENE-1012139; slc2a12.L.
DR OrthoDB; 430696at2759; -.
DR Proteomes; UP000186698; Chromosome 5L.
DR Bgee; 734962; Expressed in zone of skin and 11 other tissues.
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:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
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; 1.
DR TIGRFAMs; TIGR00879; SP; 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cytoplasm; Glycoprotein; Membrane; Reference proteome;
KW Sugar transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..588
FT /note="Solute carrier family 2, facilitated glucose
FT transporter member 12"
FT /id="PRO_0000292018"
FT TOPO_DOM 1..28
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 50..74
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..103
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 125..131
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 153..158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..191
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 213..272
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..293
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 294..311
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 333..339
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 340..360
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 361..459
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 460..480
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 481..492
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 493..513
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 514..522
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 523..543
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 544..588
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 377
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 395
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 588 AA; 63891 MW; 4E5A2FC4150F92D7 CRC64;
MLAHSTAQDL ILQQRSSDDH PQTNPRQTGC GAFIILSSVI AAISGLLVGY ELGIISGALL
QLQSLLELTC QQQEIVVSAL LIGALVASLV GGCLIDLYGR RTTIIFTSIL LVFANLLPVV
VVSYGSLIAG RIFIGVSISL SAIATCVYIA ELSPQDKRGM LVSLNELMIV AGILLAYICN
YLFASVNNGW KYMFGLITPL AALQAVAMFF LPRSPRFLIM KGYDDAAGKV LQKLRATTDI
NEELTAIKSS IKAEYQYKFL DLFCSRDNMR ARLLIGLTLS FFVQITGQPN ILFYASTVLK
SVGFQSTEAA SLASTGIGVV KVVSTIPAIF LVDKIGSKTF LCIGSAVMAV SLVSVGLVSL
QLDVNYNNIC KVHTVQNHSL QDSFVYGPVA LAKHNESLFE ETGTWLESTK ASYHSTSQNG
TKLLHVSAPE DSSFGFTVKE PKVKSQSDEI PEYMKWLCLS SLLAFVAAFS IGLGPMAWLV
QSEIFPAGIK GRAFAITSSM NWGMNLLISL TFLTLTEMIG LPWMLFGYAL MSIASLVFVI
MFVPNTKGRP LEEISKELAN RSYMCNAVCH RRRSKKKLTP VALIQSPA
