ID   G6PT3_BOVIN             Reviewed;         491 AA.
AC   Q58CV5;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Glucose-6-phosphate exchanger SLC37A2 {ECO:0000305};
DE   AltName: Full=Solute carrier family 37 member 2 {ECO:0000250|UniProtKB:Q8TED4};
GN   Name=SLC37A2 {ECO:0000250|UniProtKB:Q8TED4};
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 [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
CC   -!- FUNCTION: Inorganic phosphate and glucose-6-phosphate antiporter. May
CC       transport cytoplasmic glucose-6-phosphate into the lumen of the
CC       endoplasmic reticulum and translocate inorganic phosphate into the
CC       opposite direction. Independent of a lumenal glucose-6-phosphatase. May
CC       not play a role in homeostatic regulation of blood glucose levels.
CC       {ECO:0000250|UniProtKB:Q8TED4}.
CC   -!- ACTIVITY REGULATION: Inhibited by vanadate but not by chlorogenic acid.
CC       {ECO:0000250|UniProtKB:Q8TED4}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q8TED4}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC       Organophosphate:Pi antiporter (OPA) (TC 2.A.1.4) family. {ECO:0000305}.
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DR   EMBL; BT021842; AAX46689.1; -; mRNA.
DR   RefSeq; NP_001019657.1; NM_001024486.1.
DR   AlphaFoldDB; Q58CV5; -.
DR   SMR; Q58CV5; -.
DR   STRING; 9913.ENSBTAP00000022208; -.
DR   PaxDb; Q58CV5; -.
DR   PRIDE; Q58CV5; -.
DR   GeneID; 506687; -.
DR   KEGG; bta:506687; -.
DR   CTD; 219855; -.
DR   eggNOG; KOG2533; Eukaryota.
DR   HOGENOM; CLU_001265_31_6_1; -.
DR   InParanoid; Q58CV5; -.
DR   OrthoDB; 964162at2759; -.
DR   TreeFam; TF314991; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0061513; F:glucose 6-phosphate:inorganic phosphate antiporter activity; ISS:UniProtKB.
DR   GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR   GO; GO:0015760; P:glucose-6-phosphate transport; ISS:UniProtKB.
DR   GO; GO:0035435; P:phosphate ion transmembrane transport; ISS:UniProtKB.
DR   CDD; cd17344; MFS_SLC37A1_2; 1.
DR   Gene3D; 1.20.1250.20; -; 2.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   InterPro; IPR044740; SLC37A1_2.
DR   InterPro; IPR000849; Sugar_P_transporter.
DR   Pfam; PF07690; MFS_1; 1.
DR   PIRSF; PIRSF002808; Hexose_phosphate_transp; 1.
DR   SUPFAM; SSF103473; SSF103473; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   2: Evidence at transcript level;
KW   Antiport; Endoplasmic reticulum; Glycoprotein; Membrane;
KW   Reference proteome; Sugar transport; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..491
FT                   /note="Glucose-6-phosphate exchanger SLC37A2"
FT                   /id="PRO_0000308321"
FT   TRANSMEM        5..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        78..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        108..130
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        132..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        169..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        200..220
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        292..312
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        328..348
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        352..372
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        377..397
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        424..444
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        452..472
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          229..257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        234..257
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        43
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        52
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        58
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   491 AA;  53454 MW;  05ECE7415FE56BF0 CRC64;
     MRSSLAPGIW YRAFILLITF LIYTCYHMSR KPISVVKSRL HHNCSEVIQP VNSTHSLNDT
     TWCNWAPFDK SNYKELLGAV DNAFLVAYAI GMFISGIFGE RLPLRYYLTA GMLLSGLFTS
     LFGLGYFWNI HVLWYFVLVQ IFNGLVQTTG WPAVVSCVGN WFGKGKRGLI MGIWNSHTSV
     GNILGSLLAG VWVDQQWGLS FVVPGVITAI MGIITFFFLI EYPEDVDCSP PQHHGNPEES
     QDQPEDPANG PSCNKESSLE SAVTCSKEAS AQPSAISFFG ALRIPGVVEF SLCLLFAKLV
     SYTFLYWLPL YISNVVHFTA KEAGDLSTLF DVGGIIGGIL AGLVSDYING RATTCCVMLI
     LAAPMMFLYN HVGQRGIGIS IVMLLICGAL VNGPYALITT AVSADLGTHK SLKGNAKALS
     TVTAIIDGTG SIGAALGPLL AGLISPTGWN NVFYMLIAAD VLACLLLCRL VYKEILAWKS
     SLSKDRGYRE M