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G6PT2_HUMAN
ID   G6PT2_HUMAN             Reviewed;         533 AA.
AC   P57057; D3DSJ7; Q9HAQ1;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 2.
DT   03-AUG-2022, entry version 155.
DE   RecName: Full=Glucose-6-phosphate exchanger SLC37A1 {ECO:0000305|PubMed:21949678};
DE   AltName: Full=Glycerol-3-phosphate permease {ECO:0000303|PubMed:11112347};
DE            Short=G-3-P permease {ECO:0000303|PubMed:11112347};
DE   AltName: Full=Solute carrier family 37 member 1 {ECO:0000312|HGNC:HGNC:11024};
GN   Name=SLC37A1 {ECO:0000312|HGNC:HGNC:11024};
GN   Synonyms=G3PP {ECO:0000303|PubMed:11112347};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], VARIANT ASN-247, AND TISSUE SPECIFICITY.
RX   PubMed=11112347; DOI=10.1006/geno.2000.6395;
RA   Bartoloni L., Wattenhofer M., Kudoh J., Berry A., Shibuya K., Kawasaki K.,
RA   Wang J., Asakawa S., Talior I., Bonne-Tamir B., Rossier C., Michaud J.,
RA   McCabe E.R.B., Minoshima S., Shimizu N., Scott H.S., Antonarakis S.E.;
RT   "Cloning and characterization of a putative human glycerol 3-phosphate
RT   permease gene (SLC37A1 or G3PP) on 21q22.3: mutation analysis in two
RT   candidate phenotypes, DFNB10 and a glycerol kinase deficiency.";
RL   Genomics 70:190-200(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ILE-414.
RA   Solans A., Estivill X., de la Luna S.;
RT   "Cloning and characterization of human glycerol 3-phosphate permease gene
RT   (SLC37A1).";
RL   Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10830953; DOI=10.1038/35012518;
RA   Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA   Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA   Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA   Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA   Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA   Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA   Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA   Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA   Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA   Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA   Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT   "The DNA sequence of human chromosome 21.";
RL   Nature 405:311-319(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, ACTIVITY REGULATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=21949678; DOI=10.1371/journal.pone.0023157;
RA   Pan C.J., Chen S.Y., Jun H.S., Lin S.R., Mansfield B.C., Chou J.Y.;
RT   "SLC37A1 and SLC37A2 are phosphate-linked, glucose-6-phosphate
RT   antiporters.";
RL   PLoS ONE 6:E23157-E23157(2011).
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:0000269|PubMed:21949678}.
CC   -!- ACTIVITY REGULATION: Inhibited by vanadate but not by chlorogenic acid.
CC       {ECO:0000269|PubMed:21949678}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:21949678}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Expressed in numerous tissues, with highest
CC       expression in pancreas, kidney, bone marrow, spleen, liver, small
CC       intestine, as well as in fetal brain, liver and spleen.
CC       {ECO:0000269|PubMed:11112347, ECO:0000269|PubMed:21949678}.
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; AJ269529; CAB87248.1; -; mRNA.
DR   EMBL; AJ277912; CAB91985.1; -; mRNA.
DR   EMBL; AJ277913; CAB91986.1; -; mRNA.
DR   EMBL; AF311320; AAG29853.1; -; mRNA.
DR   EMBL; AP001625; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471079; EAX09552.1; -; Genomic_DNA.
DR   EMBL; CH471079; EAX09553.1; -; Genomic_DNA.
DR   CCDS; CCDS13689.1; -.
DR   RefSeq; NP_001307466.1; NM_001320537.1.
DR   RefSeq; NP_061837.3; NM_018964.3.
DR   RefSeq; XP_016883866.1; XM_017028377.1.
DR   RefSeq; XP_016883867.1; XM_017028378.1.
DR   RefSeq; XP_016883868.1; XM_017028379.1.
DR   RefSeq; XP_016883869.1; XM_017028380.1.
DR   AlphaFoldDB; P57057; -.
DR   BioGRID; 119832; 6.
DR   IntAct; P57057; 4.
DR   MINT; P57057; -.
DR   STRING; 9606.ENSP00000344648; -.
DR   TCDB; 2.A.1.4.7; the major facilitator superfamily (mfs).
DR   GlyGen; P57057; 2 sites.
DR   iPTMnet; P57057; -.
DR   PhosphoSitePlus; P57057; -.
DR   BioMuta; SLC37A1; -.
DR   DMDM; 317373359; -.
DR   EPD; P57057; -.
DR   MassIVE; P57057; -.
DR   MaxQB; P57057; -.
DR   PaxDb; P57057; -.
DR   PeptideAtlas; P57057; -.
DR   PRIDE; P57057; -.
DR   ProteomicsDB; 56976; -.
DR   Antibodypedia; 23842; 82 antibodies from 18 providers.
DR   DNASU; 54020; -.
DR   Ensembl; ENST00000352133.3; ENSP00000344648.2; ENSG00000160190.14.
DR   Ensembl; ENST00000398341.7; ENSP00000381383.3; ENSG00000160190.14.
DR   GeneID; 54020; -.
DR   KEGG; hsa:54020; -.
DR   MANE-Select; ENST00000352133.3; ENSP00000344648.2; NM_001320537.2; NP_001307466.1.
DR   UCSC; uc002zbi.3; human.
DR   CTD; 54020; -.
DR   DisGeNET; 54020; -.
DR   GeneCards; SLC37A1; -.
DR   HGNC; HGNC:11024; SLC37A1.
DR   HPA; ENSG00000160190; Tissue enhanced (intestine).
DR   MIM; 608094; gene.
DR   neXtProt; NX_P57057; -.
DR   OpenTargets; ENSG00000160190; -.
DR   PharmGKB; PA35892; -.
DR   VEuPathDB; HostDB:ENSG00000160190; -.
DR   eggNOG; KOG2533; Eukaryota.
DR   GeneTree; ENSGT00940000159245; -.
DR   HOGENOM; CLU_001265_31_6_1; -.
DR   InParanoid; P57057; -.
DR   OMA; WEPFDKS; -.
DR   OrthoDB; 964162at2759; -.
DR   PhylomeDB; P57057; -.
DR   TreeFam; TF314991; -.
DR   PathwayCommons; P57057; -.
DR   Reactome; R-HSA-70263; Gluconeogenesis.
DR   SignaLink; P57057; -.
DR   BioGRID-ORCS; 54020; 9 hits in 1074 CRISPR screens.
DR   ChiTaRS; SLC37A1; human.
DR   GenomeRNAi; 54020; -.
DR   Pharos; P57057; Tbio.
DR   PRO; PR:P57057; -.
DR   Proteomes; UP000005640; Chromosome 21.
DR   RNAct; P57057; protein.
DR   Bgee; ENSG00000160190; Expressed in olfactory segment of nasal mucosa and 121 other tissues.
DR   ExpressionAtlas; P57057; baseline and differential.
DR   Genevisible; P57057; HS.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR   GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0061513; F:glucose 6-phosphate:inorganic phosphate antiporter activity; IDA:UniProtKB.
DR   GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR   GO; GO:0015760; P:glucose-6-phosphate transport; IDA:UniProtKB.
DR   GO; GO:0035435; P:phosphate ion transmembrane transport; IDA: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..533
FT                   /note="Glucose-6-phosphate exchanger SLC37A1"
FT                   /id="PRO_0000199890"
FT   TRANSMEM        18..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        100..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        129..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        157..177
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        222..242
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        304..324
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        334..354
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        366..386
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        394..414
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        423..443
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        466..486
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        490..510
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        81
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        263
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VARIANT         247
FT                   /note="D -> N (in dbSNP:rs768541152)"
FT                   /evidence="ECO:0000269|PubMed:11112347"
FT                   /id="VAR_017110"
FT   VARIANT         414
FT                   /note="V -> I (in dbSNP:rs228104)"
FT                   /evidence="ECO:0000269|Ref.2"
FT                   /id="VAR_017111"
FT   CONFLICT        223
FT                   /note="F -> L (in Ref. 2; AAG29853)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        303
FT                   /note="H -> Q (in Ref. 2; AAG29853)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   533 AA;  57648 MW;  FA978FE2943C80AA CRC64;
     MARLPAGIRF IISFSRDQWY RAFIFILTFL LYASFHLSRK PISIVKGELH KYCTAWDEAD
     VRFSSQNRKS GSAAPHQLPD NETDCGWAPF DKNNYQQLLG ALDYSFLCAY AVGMYLSGII
     GERLPIRYYL TFGMLASGAF TALFGLGYFY NIHSFGFYVV TQVINGLVQT TGWPSVVTCL
     GNWFGKGRRG LIMGVWNSHT SVGNILGSLI AGYWVSTCWG LSFVVPGAIV AAMGIVCFLF
     LIEHPNDVRC SSTLVTHSKG YENGTNRLRL QKQILKSEKN KPLDPEMQCL LLSDGKGSIH
     PNHVVILPGD GGSGTAAISF TGALKIPGVI EFSLCLLFAK LVSYTFLFWL PLYITNVDHL
     DAKKAGELST LFDVGGIFGG ILAGVISDRL EKRASTCGLM LLLAAPTLYI FSTVSKMGLE
     ATIAMLLLSG ALVSGPYTLI TTAVSADLGT HKSLKGNAHA LSTVTAIIDG TGSVGAALGP
     LLAGLLSPSG WSNVFYMLMF ADACALLFLI RLIHKELSCP GSATGDQVPF KEQ
 
 
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