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 27-MAR-2024, entry version 187. 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, GN 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; LYS-437 AND RP GLU-445. 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}. 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; 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; 8. 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 GlyCosmos; O95528; 1 site, No reported glycans. DR GlyGen; O95528; 1 site. DR iPTMnet; O95528; -. DR PhosphoSitePlus; O95528; -. DR SwissPalm; O95528; -. DR BioMuta; SLC2A10; -. DR jPOST; O95528; -. DR MassIVE; O95528; -. DR MaxQB; O95528; -. DR PaxDb; 9606-ENSP00000352216; -. DR PeptideAtlas; O95528; -. DR ProteomicsDB; 50935; -. DR Antibodypedia; 13253; 169 antibodies from 28 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 AGR; HGNC:13444; -. 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; GCYRIPV; -. DR OrthoDB; 2013244at2759; -. 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; 12 hits in 1143 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 159 other cell types or tissues. DR ExpressionAtlas; O95528; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell. 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: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: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:0150104; P:transport across blood-brain barrier; NAS:ARUK-UCL. DR CDD; cd17436; MFS_GLUT10_Class3; 1. DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 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 PANTHER; PTHR48023; D-XYLOSE-PROTON SYMPORTER-LIKE 2; 1. DR PANTHER; PTHR48023:SF7; SOLUTE CARRIER FAMILY 2, FACILITATED GLUCOSE TRANSPORTER MEMBER 10; 1. DR Pfam; PF00083; Sugar_tr; 3. DR PRINTS; PR00171; SUGRTRNSPORT. DR SUPFAM; SSF103473; MFS general substrate transporter; 1. DR PROSITE; PS50850; MFS; 1. DR PROSITE; PS00216; SUGAR_TRANSPORT_1; 2. DR Genevisible; O95528; HS. 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 /evidence="ECO:0000269|PubMed:12941788" 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 /evidence="ECO:0000269|PubMed:17935213" 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 //