ID   GTR12_BOVIN             Reviewed;         621 AA.
AC   Q5J316;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Solute carrier family 2, facilitated glucose transporter member 12 {ECO:0000305};
DE   AltName: Full=Glucose transporter type 12 {ECO:0000303|PubMed:16284803};
DE            Short=GLUT-12 {ECO:0000303|PubMed:16284803};
GN   Name=SLC2A12 {ECO:0000250|UniProtKB:Q8TD20};
GN   Synonyms=GLUT12 {ECO:0000303|PubMed:16284803};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   GLYCOSYLATION.
RC   TISSUE=Mammary gland;
RX   PubMed=16284803; DOI=10.1007/s00335-005-0080-5;
RA   Miller P.J., Finucane K.A., Hughes M., Zhao F.-Q.;
RT   "Cloning and expression of bovine glucose transporter GLUT12.";
RL   Mamm. Genome 16:873-883(2005).
CC   -!- FUNCTION: Insulin-independent facilitative glucose transporter.
CC       {ECO:0000250|UniProtKB:Q8BFW9}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glucose(out) = D-glucose(in); Xref=Rhea:RHEA:60376,
CC         ChEBI:CHEBI:4167; Evidence={ECO:0000250|UniProtKB:Q8BFW9};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8BFW9};
CC       Multi-pass membrane protein {ECO:0000255}. Endomembrane system
CC       {ECO:0000269|PubMed:16284803}; 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   -!- TISSUE SPECIFICITY: Detected at high level in spleen and skeletal
CC       muscle, intermediate levels in kidney, testis and mammary gland, and at
CC       lower levels in liver, lung and intestine.
CC       {ECO:0000269|PubMed:16284803}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:16284803}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC       transporter (TC 2.A.1.1) family. Glucose transporter subfamily.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY514443; AAS07046.1; -; mRNA.
DR   RefSeq; NP_001011683.1; NM_001011683.2.
DR   AlphaFoldDB; Q5J316; -.
DR   SMR; Q5J316; -.
DR   STRING; 9913.ENSBTAP00000025291; -.
DR   PaxDb; Q5J316; -.
DR   PRIDE; Q5J316; -.
DR   GeneID; 497031; -.
DR   KEGG; bta:497031; -.
DR   CTD; 154091; -.
DR   eggNOG; KOG0254; Eukaryota.
DR   InParanoid; Q5J316; -.
DR   OrthoDB; 430696at2759; -.
DR   Proteomes; UP000009136; Unplaced.
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   1: Evidence at protein level;
KW   Cell membrane; Cytoplasm; Glycoprotein; Membrane; Reference proteome;
KW   Sugar transport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..621
FT                   /note="Solute carrier family 2, facilitated glucose
FT                   transporter member 12"
FT                   /id="PRO_0000292013"
FT   TOPO_DOM        1..48
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        49..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        70..84
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        85..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        106..111
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        112..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        133..141
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        142..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        163..168
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        169..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        190..201
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        202..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        223..282
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        283..303
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        304..321
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        322..342
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        343..349
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        350..370
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        371..470
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        471..491
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        492..502
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        503..523
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        524..532
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        533..553
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        554..621
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        195
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        375
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        387
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        400
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        405
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   621 AA;  67468 MW;  8D5A5A13A2925AC2 CRC64;
     MVPVENAEGP SLLKPKGRAA ETDGSDRASG GPHPPWARGC GMYTLLSSVT AAVSGFLVGY
     ELGIISGALL QIRTLLVLTC HEQEMVVSSL LIGALLASLI GGVLIDRYGR RAAIILSSCL
     LGLGSLVLII SLSYTTLIGG RIAIGVFISL SSTATCVYIA EIAPQHRRGL LVSLNELMIV
     IGILFAYISN YAFANISHGW KYMFGLVIPL GVLQAIAMYF LPPSPRFLVM KGHEEAASKV
     LGKLRAVLDT TEELTVIKSS LKDEYQYSFW DLFRSKDNMR TRIMIGLTLV FFVQITGQPN
     ILFYASTVLK SVGFQSNEAA SLASTGVGVV KVISTIPATL LVDQVGSKTF LCIGSSVMAA
     SLVTMGIVNL NIHMNFTSIC RNHSPINQSL DESVFYGPGN LSASNDTLRE SFKGMTFHSR
     SSLRPTRNDI NGRGETTLAS LPNAGLSQTE YQIVTDSADV PTFLKWLSLA SLLVYVAAFS
     IGLGPMPWLV LSEIFPGGIR GRAMALTSSM NWGINLLISL TFLTVTDLIG LPWVCFIYTV
     MSLASLVFVI VFIPETKGCS LEQISVELAK ENYVKNNICF MSHHREELVP KQLQKRKPQE
     QFLESKKLRG KGQPRQLSSE V