GTR14_HUMAN
ID GTR14_HUMAN Reviewed; 520 AA.
AC Q8TDB8; B3KVB5; B3KWW7; B7Z844; B7ZAC3; Q6UY84; Q8TDB9;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Solute carrier family 2, facilitated glucose transporter member 14 {ECO:0000305};
DE AltName: Full=Glucose transporter type 14 {ECO:0000303|PubMed:12504846};
DE Short=GLUT-14 {ECO:0000303|PubMed:12504846};
GN Name=SLC2A14 {ECO:0000303|PubMed:27460888, ECO:0000312|HGNC:HGNC:18301};
GN Synonyms=GLUT14 {ECO:0000303|PubMed:12504846};
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] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=12504846; DOI=10.1006/geno.2002.7010;
RA Wu X., Freeze H.H.;
RT "GLUT14, a duplicon of GLUT3, is specifically expressed in testis as
RT alternative splice forms.";
RL Genomics 80:553-557(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RA Fang X., Wang H., Huo R., Lu L., Xu M., Xu Y.Z., Yin L.L., Li M.J.,
RA Zhou M.Z., Sha H.J.;
RT "Cloning of an isoform of SCL2A14 gene related to spermatogenesis.";
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 4 AND 5).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Fetal brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=27460888; DOI=10.1139/bcb-2015-0089;
RA Amir Shaghaghi M., Murphy B., Eck P.;
RT "The SLC2A14 gene: genomic locus, tissue expression, splice variants, and
RT subcellular localization of the protein.";
RL Biochem. Cell Biol. 94:331-335(2016).
RN [9]
RP FUNCTION, AND TRANSPORTER ACTIVITY.
RX PubMed=28971850; DOI=10.3945/ajcn.116.147603;
RA Amir Shaghaghi M., Zhouyao H., Tu H., El-Gabalawy H., Crow G.H., Levine M.,
RA Bernstein C.N., Eck P.;
RT "The SLC2A14 gene, encoding the novel glucose/dehydroascorbate transporter
RT GLUT14, is associated with inflammatory bowel disease.";
RL Am. J. Clin. Nutr. 106:1508-1513(2017).
CC -!- FUNCTION: Hexose transporter that can mediate the transport of glucose
CC and dehydroascorbate across the cell membrane.
CC {ECO:0000269|PubMed:28971850}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose(out) = D-glucose(in); Xref=Rhea:RHEA:60376,
CC ChEBI:CHEBI:4167; Evidence={ECO:0000269|PubMed:28971850};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-dehydroascorbate(out) = L-dehydroascorbate(in);
CC Xref=Rhea:RHEA:60380, ChEBI:CHEBI:58539;
CC Evidence={ECO:0000269|PubMed:28971850};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27460888};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=GLUT14-L {ECO:0000303|PubMed:12504846};
CC IsoId=Q8TDB8-1; Sequence=Displayed;
CC Name=2; Synonyms=GLUT14-S {ECO:0000303|PubMed:12504846};
CC IsoId=Q8TDB8-2; Sequence=VSP_014450;
CC Name=3;
CC IsoId=Q8TDB8-3; Sequence=VSP_014449;
CC Name=4;
CC IsoId=Q8TDB8-4; Sequence=VSP_055253;
CC Name=5;
CC IsoId=Q8TDB8-5; Sequence=VSP_055254;
CC -!- TISSUE SPECIFICITY: Mainly expressed in testis (PubMed:12504846,
CC PubMed:27460888). Also expressed in small intestine, liver and kidney
CC (PubMed:27460888). {ECO:0000269|PubMed:12504846,
CC ECO:0000269|PubMed:27460888}.
CC -!- MISCELLANEOUS: GLUT14 is a recent (less than 5 M year old) duplication
CC of GLUT3. {ECO:0000305|PubMed:12504846}.
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; AF481878; AAL89709.1; -; mRNA.
DR EMBL; AF481879; AAL89710.1; -; mRNA.
DR EMBL; AY357941; AAQ63763.1; -; mRNA.
DR EMBL; AK122783; BAG53727.1; -; mRNA.
DR EMBL; AK126026; BAG54279.1; -; mRNA.
DR EMBL; AK302881; BAH13830.1; -; mRNA.
DR EMBL; AK316238; BAH14609.1; -; mRNA.
DR EMBL; AL110298; CAB53739.2; -; mRNA.
DR EMBL; AC006517; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC007536; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC124891; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471116; EAW88652.1; -; Genomic_DNA.
DR EMBL; CH471116; EAW88653.1; -; Genomic_DNA.
DR EMBL; BC060766; AAH60766.1; -; mRNA.
DR CCDS; CCDS66300.1; -. [Q8TDB8-4]
DR CCDS; CCDS66301.1; -. [Q8TDB8-2]
DR CCDS; CCDS66302.1; -. [Q8TDB8-5]
DR CCDS; CCDS8585.1; -. [Q8TDB8-1]
DR RefSeq; NP_001273162.1; NM_001286233.1. [Q8TDB8-1]
DR RefSeq; NP_001273163.1; NM_001286234.1. [Q8TDB8-2]
DR RefSeq; NP_001273164.1; NM_001286235.1. [Q8TDB8-2]
DR RefSeq; NP_001273165.1; NM_001286236.1. [Q8TDB8-4]
DR RefSeq; NP_001273166.1; NM_001286237.1. [Q8TDB8-5]
DR RefSeq; NP_703150.1; NM_153449.3. [Q8TDB8-1]
DR RefSeq; XP_005253372.1; XM_005253315.3. [Q8TDB8-2]
DR RefSeq; XP_005253374.1; XM_005253317.4. [Q8TDB8-2]
DR RefSeq; XP_011518864.1; XM_011520562.1. [Q8TDB8-2]
DR RefSeq; XP_011518865.1; XM_011520563.2. [Q8TDB8-2]
DR RefSeq; XP_011518866.1; XM_011520564.2. [Q8TDB8-4]
DR RefSeq; XP_011518867.1; XM_011520565.2. [Q8TDB8-4]
DR RefSeq; XP_016874335.1; XM_017018846.1. [Q8TDB8-2]
DR RefSeq; XP_016874336.1; XM_017018847.1. [Q8TDB8-2]
DR AlphaFoldDB; Q8TDB8; -.
DR SMR; Q8TDB8; -.
DR BioGRID; 126837; 26.
DR IntAct; Q8TDB8; 9.
DR STRING; 9606.ENSP00000445929; -.
DR BindingDB; Q8TDB8; -.
DR ChEMBL; CHEMBL4295906; -.
DR TCDB; 2.A.1.1.90; the major facilitator superfamily (mfs).
DR GlyGen; Q8TDB8; 1 site.
DR iPTMnet; Q8TDB8; -.
DR PhosphoSitePlus; Q8TDB8; -.
DR BioMuta; SLC2A14; -.
DR DMDM; 68565598; -.
DR EPD; Q8TDB8; -.
DR jPOST; Q8TDB8; -.
DR MassIVE; Q8TDB8; -.
DR MaxQB; Q8TDB8; -.
DR PaxDb; Q8TDB8; -.
DR PeptideAtlas; Q8TDB8; -.
DR PRIDE; Q8TDB8; -.
DR ProteomicsDB; 6924; -.
DR ProteomicsDB; 7059; -.
DR ProteomicsDB; 74258; -. [Q8TDB8-1]
DR ProteomicsDB; 74259; -. [Q8TDB8-2]
DR ProteomicsDB; 74260; -. [Q8TDB8-3]
DR Antibodypedia; 53025; 50 antibodies from 4 providers.
DR DNASU; 144195; -.
DR Ensembl; ENST00000340749.9; ENSP00000340450.5; ENSG00000173262.12. [Q8TDB8-2]
DR Ensembl; ENST00000396589.6; ENSP00000379834.2; ENSG00000173262.12. [Q8TDB8-1]
DR Ensembl; ENST00000431042.7; ENSP00000407287.2; ENSG00000173262.12. [Q8TDB8-2]
DR Ensembl; ENST00000535295.5; ENSP00000440492.1; ENSG00000173262.12. [Q8TDB8-4]
DR Ensembl; ENST00000539924.5; ENSP00000445929.1; ENSG00000173262.12. [Q8TDB8-5]
DR Ensembl; ENST00000542505.5; ENSP00000438484.1; ENSG00000173262.12. [Q8TDB8-3]
DR Ensembl; ENST00000542546.5; ENSP00000443903.1; ENSG00000173262.12. [Q8TDB8-4]
DR Ensembl; ENST00000543909.5; ENSP00000440480.1; ENSG00000173262.12. [Q8TDB8-1]
DR Ensembl; ENST00000616981.4; ENSP00000482927.1; ENSG00000173262.12. [Q8TDB8-1]
DR GeneID; 144195; -.
DR KEGG; hsa:144195; -.
DR MANE-Select; ENST00000431042.7; ENSP00000407287.2; NM_001286234.2; NP_001273163.1. [Q8TDB8-2]
DR UCSC; uc001qtk.5; human. [Q8TDB8-1]
DR CTD; 144195; -.
DR DisGeNET; 144195; -.
DR GeneCards; SLC2A14; -.
DR HGNC; HGNC:18301; SLC2A14.
DR HPA; ENSG00000173262; Tissue enriched (testis).
DR MIM; 611039; gene.
DR neXtProt; NX_Q8TDB8; -.
DR OpenTargets; ENSG00000173262; -.
DR PharmGKB; PA134885058; -.
DR VEuPathDB; HostDB:ENSG00000173262; -.
DR eggNOG; KOG0569; Eukaryota.
DR GeneTree; ENSGT00940000162491; -.
DR HOGENOM; CLU_001265_30_5_1; -.
DR InParanoid; Q8TDB8; -.
DR OMA; DENRHFH; -.
DR OrthoDB; 326501at2759; -.
DR PhylomeDB; Q8TDB8; -.
DR TreeFam; TF313762; -.
DR PathwayCommons; Q8TDB8; -.
DR Reactome; R-HSA-189200; Cellular hexose transport.
DR SignaLink; Q8TDB8; -.
DR BioGRID-ORCS; 144195; 10 hits in 1009 CRISPR screens.
DR ChiTaRS; SLC2A14; human.
DR GeneWiki; SLC2A14; -.
DR GenomeRNAi; 144195; -.
DR Pharos; Q8TDB8; Tbio.
DR PRO; PR:Q8TDB8; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q8TDB8; protein.
DR Bgee; ENSG00000173262; Expressed in left testis and 98 other tissues.
DR ExpressionAtlas; Q8TDB8; baseline and differential.
DR Genevisible; Q8TDB8; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0055056; F:D-glucose transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0033300; F:dehydroascorbic acid transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0005355; F:glucose transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015149; F:hexose transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0070837; P:dehydroascorbic acid transport; IDA:UniProtKB.
DR GO; GO:0046323; P:glucose import; IBA:GO_Central.
DR GO; GO:1904659; P:glucose transmembrane transport; IDA:UniProtKB.
DR GO; GO:0015749; P:monosaccharide transmembrane transport; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR002945; Glc_transpt_3.
DR InterPro; IPR045263; GLUT.
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 PANTHER; PTHR23503; PTHR23503; 1.
DR Pfam; PF00083; Sugar_tr; 1.
DR PRINTS; PR01192; GLUCTRSPORT3.
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.
DR PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Developmental protein;
KW Differentiation; Glycoprotein; Membrane; Reference proteome;
KW Spermatogenesis; Sugar transport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..520
FT /note="Solute carrier family 2, facilitated glucose
FT transporter member 14"
FT /id="PRO_0000050381"
FT TOPO_DOM 1..29
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 30..50
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 51..88
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..109
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 110..117
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..138
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 139..148
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..177
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 199..207
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..228
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 229..293
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..314
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 315..328
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 329..349
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 350..358
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 359..379
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 380..392
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 393..413
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 414..423
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 424..444
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 445..451
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 452..472
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 473..520
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 493..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 183
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 304..305
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 310
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 339
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 402
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 410
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..359
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_014449"
FT VAR_SEQ 1..113
FT /note="MEFHNGGHVSGIGGFLVSLTSRMKPHTLAVTPALIFAITVATIGSFQFGYNT
FT GVINAPETIIKEFINKTLTDKANAPPSEVLLTNLWSLSVAIFSVGGMIGSFSVGLFVNR
FT FG -> MLLR (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055253"
FT VAR_SEQ 1..29
FT /note="MEFHNGGHVSGIGGFLVSLTSRMKPHTLA -> MDNRQN (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:12504846,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334,
FT ECO:0000303|Ref.2"
FT /id="VSP_014450"
FT VAR_SEQ 1..29
FT /note="MEFHNGGHVSGIGGFLVSLTSRMKPHTLA -> MQRLQLLRVEVLLGVKQGD
FT EMRHFFFSSQTSTLEKSQNGGVGEE (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055254"
FT VARIANT 506
FT /note="G -> E (in dbSNP:rs10845981)"
FT /id="VAR_059852"
FT CONFLICT 369
FT /note="C -> G (in Ref. 2; AAQ63763)"
FT /evidence="ECO:0000305"
FT CONFLICT 376..377
FT /note="SL -> PC (in Ref. 2; AAQ63763)"
FT /evidence="ECO:0000305"
FT CONFLICT 456
FT /note="F -> L (in Ref. 4; CAB53739)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 520 AA; 56320 MW; EA304A5189087690 CRC64;
MEFHNGGHVS GIGGFLVSLT SRMKPHTLAV TPALIFAITV ATIGSFQFGY NTGVINAPET
IIKEFINKTL TDKANAPPSE VLLTNLWSLS VAIFSVGGMI GSFSVGLFVN RFGRRNSMLI
VNLLAATGGC LMGLCKIAES VEMLILGRLV IGLFCGLCTG FVPMYIGEIS PTALRGAFGT
LNQLGIVIGI LVAQIFGLEL ILGSEELWPV LLGFTILPAI LQSAALPCCP ESPRFLLINR
KKEENATRIL QRLWGTQDVS QDIQEMKDES ARMSQEKQVT VLELFRVSSY RQPIIISIVL
QLSQQLSGIN AVFYYSTGIF KDAGVQQPIY ATISAGVVNT IFTLLSLFLV ERAGRRTLHM
IGLGGMAFCS TLMTVSLLLK NHYNGMSFVC IGAILVFVAC FEIGPGPIPW FIVAELFSQG
PRPAAMAVAG CSNWTSNFLV GLLFPSAAYY LGAYVFIIFT GFLITFLAFT FFKVPETRGR
TFEDITRAFE GQAHGADRSG KDGVMGMNSI EPAKETTTNV