GTR10_HUMAN
ID GTR10_HUMAN Reviewed; 541 AA.
AC O95528; A8K4J6; Q3MIX5; Q9H4I6;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Solute carrier family 2, facilitated glucose transporter member 10 {ECO:0000305};
DE AltName: Full=Glucose transporter type 10 {ECO:0000303|PubMed:11247674};
DE Short=GLUT-10 {ECO:0000303|PubMed:11247674};
GN Name=SLC2A10 {ECO:0000303|PubMed:11247674, ECO:0000312|HGNC:HGNC:13444};
GN Synonyms=GLUT10 {ECO:0000303|PubMed:11247674};
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].
RC TISSUE=Liver;
RX PubMed=11247674; DOI=10.1006/geno.2000.6457;
RA McVie-Wylie A.J., Lamson D.R., Chen Y.T.;
RT "Molecular cloning of a novel member of the GLUT family of transporters,
RT SLC2A10 (GLUT10), localized on chromosome 20q13.1: a candidate gene for
RT NIDDM susceptibility.";
RL Genomics 72:113-117(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TRANSPORTER ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RX PubMed=11592815; DOI=10.1006/mgme.2001.3212;
RA Dawson P.A., Mychaleckyj J.C., Fossey S.C., Mihic S.J., Craddock A.L.,
RA Bowden D.W.;
RT "Sequence and functional analysis of GLUT10: a glucose transporter in the
RT Type 2 diabetes-linked region of chromosome 20q12-13.1.";
RL Mol. Genet. Metab. 74:186-199(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Stavrides G.S., Hashim Y., Huckle E.J., Deloukas P.;
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
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].
RC TISSUE=Liver;
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 ASSOCIATION OF VARIANT THR-206 WITH LOWER SERUM INSULIN LEVEL.
RX PubMed=12941788; DOI=10.2337/diabetes.52.9.2445;
RA Andersen G., Rose C.S., Hamid Y.H., Drivsholm T., Borch-Johnsen K.,
RA Hansen T., Pedersen O.;
RT "Genetic variation of the GLUT10 glucose transporter (SLC2A10) and
RT relationships to type 2 diabetes and intermediary traits.";
RL Diabetes 52:2445-2448(2003).
RN [9]
RP VARIANT ATORS ARG-81, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=16550171; DOI=10.1038/ng1764;
RA Coucke P.J., Willaert A., Wessels M.W., Callewaert B., Zoppi N.,
RA De Backer J., Fox J.E., Mancini G.M.S., Kambouris M., Gardella R.,
RA Facchetti F., Willems P.J., Forsyth R., Dietz H.C., Barlati S., Colombi M.,
RA Loeys B., De Paepe A.;
RT "Mutations in the facilitative glucose transporter GLUT10 alter
RT angiogenesis and cause arterial tortuosity syndrome.";
RL Nat. Genet. 38:452-457(2006).
RN [10]
RP VARIANTS ATORS TRP-132; VAL-142; GLN-231; GLU-246; TRP-426 AND LYS-437.
RX PubMed=17935213; DOI=10.1002/humu.20623;
RA Callewaert B.L., Willaert A., Kerstjens-Frederikse W.S., De Backer J.,
RA Devriendt K., Albrecht B., Ramos-Arroyo M.A., Doco-Fenzy M.,
RA Hennekam R.C.M., Pyeritz R.E., Krogmann O.N., Gillessen-kaesbach G.,
RA Wakeling E.L., Nik-zainal S., Francannet C., Mauran P., Booth C.,
RA Barrow M., Dekens R., Loeys B.L., Coucke P.J., De Paepe A.M.;
RT "Arterial tortuosity syndrome: clinical and molecular findings in 12 newly
RT identified families.";
RL Hum. Mutat. 29:150-158(2008).
CC -!- FUNCTION: Facilitative glucose transporter required for the development
CC of the cardiovascular system. {ECO:0000269|PubMed:11592815,
CC ECO:0000269|PubMed:16550171}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose(out) = D-glucose(in); Xref=Rhea:RHEA:60376,
CC ChEBI:CHEBI:4167; Evidence={ECO:0000269|PubMed:11592815};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.28 mM for 2-deoxy-D-glucose {ECO:0000269|PubMed:11592815};
CC -!- SUBCELLULAR LOCATION: Endomembrane system
CC {ECO:0000269|PubMed:16550171}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:16550171}.
CC -!- TISSUE SPECIFICITY: Widely expressed; highest levels in liver and
CC pancreas. {ECO:0000269|PubMed:11592815}.
CC -!- DISEASE: Arterial tortuosity syndrome (ATORS) [MIM:208050]: An
CC autosomal recessive disorder characterized by tortuosity and elongation
CC of major arteries, often resulting in death at young age. Other typical
CC features include aneurysms of large arteries and stenosis of the
CC pulmonary artery, in association with facial features and several
CC connective tissue manifestations such as soft skin and joint laxity.
CC Histopathological findings include fragmentation of elastic fibers in
CC the tunica media of large arteries. {ECO:0000269|PubMed:16550171,
CC ECO:0000269|PubMed:17935213}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
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; AF321240; AAK26294.1; -; mRNA.
DR EMBL; AF248053; AAK31911.1; -; mRNA.
DR EMBL; AL137188; CAB69822.2; -; mRNA.
DR EMBL; AK290961; BAF83650.1; -; mRNA.
DR EMBL; AL031055; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW75724.1; -; Genomic_DNA.
DR EMBL; BC101657; AAI01658.1; -; mRNA.
DR EMBL; BC113423; AAI13424.1; -; mRNA.
DR CCDS; CCDS13402.1; -.
DR RefSeq; NP_110404.1; NM_030777.3.
DR AlphaFoldDB; O95528; -.
DR SMR; O95528; -.
DR BioGRID; 123350; 7.
DR STRING; 9606.ENSP00000352216; -.
DR DrugBank; DB01914; D-glucose.
DR DrugBank; DB09341; Dextrose, unspecified form.
DR DrugBank; DB09502; Fludeoxyglucose (18F).
DR TCDB; 2.A.1.1.59; the major facilitator superfamily (mfs).
DR GlyGen; O95528; 1 site.
DR iPTMnet; O95528; -.
DR PhosphoSitePlus; O95528; -.
DR BioMuta; SLC2A10; -.
DR jPOST; O95528; -.
DR MassIVE; O95528; -.
DR MaxQB; O95528; -.
DR PaxDb; O95528; -.
DR PeptideAtlas; O95528; -.
DR PRIDE; O95528; -.
DR ProteomicsDB; 50935; -.
DR Antibodypedia; 13253; 162 antibodies from 27 providers.
DR DNASU; 81031; -.
DR Ensembl; ENST00000359271.4; ENSP00000352216.2; ENSG00000197496.6.
DR GeneID; 81031; -.
DR KEGG; hsa:81031; -.
DR MANE-Select; ENST00000359271.4; ENSP00000352216.2; NM_030777.4; NP_110404.1.
DR UCSC; uc002xsl.4; human.
DR CTD; 81031; -.
DR DisGeNET; 81031; -.
DR GeneCards; SLC2A10; -.
DR GeneReviews; SLC2A10; -.
DR HGNC; HGNC:13444; SLC2A10.
DR HPA; ENSG00000197496; Low tissue specificity.
DR MalaCards; SLC2A10; -.
DR MIM; 208050; phenotype.
DR MIM; 606145; gene.
DR neXtProt; NX_O95528; -.
DR OpenTargets; ENSG00000197496; -.
DR Orphanet; 3342; Arterial tortuosity syndrome.
DR PharmGKB; PA37769; -.
DR VEuPathDB; HostDB:ENSG00000197496; -.
DR eggNOG; KOG0254; Eukaryota.
DR GeneTree; ENSGT00940000159430; -.
DR HOGENOM; CLU_001265_30_5_1; -.
DR InParanoid; O95528; -.
DR OMA; GCIWLPE; -.
DR OrthoDB; 326501at2759; -.
DR PhylomeDB; O95528; -.
DR TreeFam; TF332408; -.
DR PathwayCommons; O95528; -.
DR Reactome; R-HSA-189200; Cellular hexose transport.
DR Reactome; R-HSA-5619068; Defective SLC2A10 causes arterial tortuosity syndrome (ATS).
DR BioGRID-ORCS; 81031; 10 hits in 1063 CRISPR screens.
DR ChiTaRS; SLC2A10; human.
DR GeneWiki; SLC2A10; -.
DR GenomeRNAi; 81031; -.
DR Pharos; O95528; Tbio.
DR PRO; PR:O95528; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; O95528; protein.
DR Bgee; ENSG00000197496; Expressed in tibia and 158 other tissues.
DR ExpressionAtlas; O95528; baseline and differential.
DR Genevisible; O95528; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:ARUK-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0005351; F:carbohydrate:proton symporter activity; NAS:UniProtKB.
DR GO; GO:0055056; F:D-glucose transmembrane transporter activity; IDA:ARUK-UCL.
DR GO; GO:0033300; F:dehydroascorbic acid transmembrane transporter activity; IDA:ARUK-UCL.
DR GO; GO:0005355; F:glucose transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015293; F:symporter activity; IBA:GO_Central.
DR GO; GO:0060840; P:artery development; IMP:ARUK-UCL.
DR GO; GO:0045454; P:cell redox homeostasis; IMP:ARUK-UCL.
DR GO; GO:0072359; P:circulatory system development; IBA:GO_Central.
DR GO; GO:0070837; P:dehydroascorbic acid transport; IDA:ARUK-UCL.
DR GO; GO:0072498; P:embryonic skeletal joint development; IMP:ARUK-UCL.
DR GO; GO:0015757; P:galactose transmembrane transport; TAS:ARUK-UCL.
DR GO; GO:0098708; P:glucose import across plasma membrane; IDA:ARUK-UCL.
DR GO; GO:1904659; P:glucose transmembrane transport; IBA:GO_Central.
DR GO; GO:0008645; P:hexose transmembrane transport; TAS:Reactome.
DR GO; GO:0032683; P:negative regulation of connective tissue growth factor production; IMP:ARUK-UCL.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:ARUK-UCL.
DR GO; GO:2001045; P:negative regulation of integrin-mediated signaling pathway; IMP:ARUK-UCL.
DR GO; GO:1902729; P:negative regulation of proteoglycan biosynthetic process; IMP:ARUK-UCL.
DR GO; GO:0060392; P:negative regulation of SMAD protein signal transduction; IMP:ARUK-UCL.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IMP:ARUK-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:ARUK-UCL.
DR GO; GO:1902730; P:positive regulation of proteoglycan biosynthetic process; IMP:ARUK-UCL.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IMP:ARUK-UCL.
DR GO; GO:1903053; P:regulation of extracellular matrix organization; IMP:ARUK-UCL.
DR GO; GO:0043588; P:skin development; IMP:ARUK-UCL.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR GO; GO:0150104; P:transport across blood-brain barrier; NAS:ARUK-UCL.
DR Gene3D; 1.20.1250.20; -; 3.
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 PROSITE; PS50850; MFS; 1.
DR PROSITE; PS00216; SUGAR_TRANSPORT_1; 2.
PE 1: Evidence at protein level;
KW Cytoplasm; Disease variant; Glycoprotein; Membrane; Reference proteome;
KW Sugar transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..541
FT /note="Solute carrier family 2, facilitated glucose
FT transporter member 10"
FT /id="PRO_0000050379"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..36
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..48
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 49..69
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..77
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..98
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 99..106
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..127
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 128..134
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..155
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 156..166
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 188..233
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 255..269
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 270..290
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 291..298
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 299..319
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 320..414
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 415..435
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 436..445
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 446..466
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 467..476
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 477..497
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 498..541
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 340..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..358
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..379
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 242..243
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 432
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 81
FT /note="S -> R (in ATORS; dbSNP:rs80358230)"
FT /evidence="ECO:0000269|PubMed:16550171"
FT /id="VAR_029535"
FT VARIANT 106
FT /note="A -> S (in dbSNP:rs6094438)"
FT /id="VAR_029536"
FT VARIANT 132
FT /note="R -> W (in ATORS; dbSNP:rs121908173)"
FT /evidence="ECO:0000269|PubMed:17935213"
FT /id="VAR_042417"
FT VARIANT 142
FT /note="G -> V (in ATORS; dbSNP:rs864309480)"
FT /evidence="ECO:0000269|PubMed:17935213"
FT /id="VAR_042418"
FT VARIANT 206
FT /note="A -> T (associated with lower insulin level;
FT dbSNP:rs2235491)"
FT /id="VAR_029335"
FT VARIANT 225
FT /note="R -> H (in dbSNP:rs34295241)"
FT /id="VAR_042419"
FT VARIANT 231
FT /note="R -> Q (in ATORS; dbSNP:rs771028960)"
FT /evidence="ECO:0000269|PubMed:17935213"
FT /id="VAR_042420"
FT VARIANT 246
FT /note="G -> E (in ATORS; dbSNP:rs564317065)"
FT /evidence="ECO:0000269|PubMed:17935213"
FT /id="VAR_042421"
FT VARIANT 426
FT /note="G -> W (in ATORS; dbSNP:rs121908172)"
FT /evidence="ECO:0000269|PubMed:17935213"
FT /id="VAR_042422"
FT VARIANT 437
FT /note="E -> K (in ATORS; dbSNP:rs763220502)"
FT /evidence="ECO:0000269|PubMed:17935213"
FT /id="VAR_042423"
FT VARIANT 445
FT /note="G -> E (in ATORS; dbSNP:rs753723351)"
FT /id="VAR_042424"
FT VARIANT 518
FT /note="T -> A (in dbSNP:rs6018008)"
FT /id="VAR_024652"
FT VARIANT 537
FT /note="I -> V (in dbSNP:rs7348121)"
FT /id="VAR_029537"
SQ SEQUENCE 541 AA; 56911 MW; 6D644525FA136908 CRC64;
MGHSPPVLPL CASVSLLGGL TFGYELAVIS GALLPLQLDF GLSCLEQEFL VGSLLLGALL
ASLVGGFLID CYGRKQAILG SNLVLLAGSL TLGLAGSLAW LVLGRAVVGF AISLSSMACC
IYVSELVGPR QRGVLVSLYE AGITVGILLS YALNYALAGT PWGWRHMFGW ATAPAVLQSL
SLLFLPAGTD ETATHKDLIP LQGGEAPKLG PGRPRYSFLD LFRARDNMRG RTTVGLGLVL
FQQLTGQPNV LCYASTIFSS VGFHGGSSAV LASVGLGAVK VAATLTAMGL VDRAGRRALL
LAGCALMALS VSGIGLVSFA VPMDSGPSCL AVPNATGQTG LPGDSGLLQD SSLPPIPRTN
EDQREPILST AKKTKPHPRS GDPSAPPRLA LSSALPGPPL PARGHALLRW TALLCLMVFV
SAFSFGFGPV TWLVLSEIYP VEIRGRAFAF CNSFNWAANL FISLSFLDLI GTIGLSWTFL
LYGLTAVLGL GFIYLFVPET KGQSLAEIDQ QFQKRRFTLS FGHRQNSTGI PYSRIEISAA
S
