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GTR11_HUMAN
ID   GTR11_HUMAN             Reviewed;         496 AA.
AC   Q9BYW1; E9PH55; Q542Y4; Q6ICJ5; Q8WXF9; Q8WYM4;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 174.
DE   RecName: Full=Solute carrier family 2, facilitated glucose transporter member 11 {ECO:0000305};
DE   AltName: Full=Glucose transporter type 11 {ECO:0000303|PubMed:11741323};
DE            Short=GLUT-11 {ECO:0000303|PubMed:11741323};
GN   Name=SLC2A11 {ECO:0000303|PubMed:11741323, ECO:0000312|HGNC:HGNC:14239};
GN   Synonyms=GLUT11 {ECO:0000303|PubMed:11741323};
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] (ISOFORM 1).
RC   TISSUE=Heart;
RA   Doege H., Bocianski A., Scheepers A., Axer H., Eckel J., Joost H.-G.;
RT   "Two novel members of the family of sugar transport facilitators: genomic
RT   organization and predominant expression in lymphocytes (GLUT9) and muscle
RT   (GLUT10).";
RL   Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 2 AND 4), AND VARIANT GLN-232.
RX   PubMed=11741323; DOI=10.1006/bbrc.2001.6101;
RA   Sasaki T., Minoshima S., Shiohama A., Shintani A., Shimizu A., Asakawa S.,
RA   Kawasaki K., Shimizu N.;
RT   "Molecular cloning of a member of the facilitative glucose transporter gene
RT   family GLUT11 (SLC2A11) and identification of transcription variants.";
RL   Biochem. Biophys. Res. Commun. 289:1218-1224(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), ALTERNATIVE SPLICING, FUNCTION,
RP   TRANSPORTER ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=12175779; DOI=10.1016/s1096-7192(02)00018-5;
RA   Wu X., Li W., Sharma V., Godzik A., Freeze H.H.;
RT   "Cloning and characterization of glucose transporter 11, a novel sugar
RT   transporter that is alternatively spliced in various tissues.";
RL   Mol. Genet. Metab. 76:37-45(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RX   PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA   Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA   Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA   Beare D.M., Dunham I.;
RT   "A genome annotation-driven approach to cloning the human ORFeome.";
RL   Genome Biol. 5:R84.1-R84.11(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANT GLN-232.
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Placenta;
RX   PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA   Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA   Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA   Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA   Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA   Isogai T.;
RT   "Signal sequence and keyword trap in silico for selection of full-length
RT   human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT   libraries.";
RL   DNA Res. 12:117-126(2005).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10591208; DOI=10.1038/990031;
RA   Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA   Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA   Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA   Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA   Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA   Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA   Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA   Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA   Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA   Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA   Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA   Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA   Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA   Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA   Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA   Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA   Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA   Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA   Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA   Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA   Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA   Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA   Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA   Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA   Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA   Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA   Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA   Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA   Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA   Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA   Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA   Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA   Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA   McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA   Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA   Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA   Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA   Wright H.;
RT   "The DNA sequence of human chromosome 22.";
RL   Nature 402:489-495(1999).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
CC   -!- FUNCTION: Facilitative glucose transporter.
CC       {ECO:0000269|PubMed:12175779}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glucose(out) = D-glucose(in); Xref=Rhea:RHEA:60376,
CC         ChEBI:CHEBI:4167; Evidence={ECO:0000269|PubMed:12175779};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12175779};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q9BYW1-1; Sequence=Displayed;
CC       Name=2; Synonyms=GLUT11-s {ECO:0000303|PubMed:12175779};
CC         IsoId=Q9BYW1-2; Sequence=VSP_006293, VSP_006294, VSP_006295;
CC       Name=3;
CC         IsoId=Q9BYW1-3; Sequence=VSP_006293;
CC       Name=4; Synonyms=GLUT11-L {ECO:0000303|PubMed:12175779};
CC         IsoId=Q9BYW1-4; Sequence=VSP_045650;
CC   -!- TISSUE SPECIFICITY: Expressed in heart and skeletal muscle.
CC       {ECO:0000269|PubMed:12175779}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC       transporter (TC 2.A.1.1) family. Glucose transporter subfamily.
CC       {ECO:0000305}.
CC   -!- CAUTION: Has been described as GLUT10 in literature, but this gene name
CC       has already been used for SLC2A10. {ECO:0000305|Ref.1}.
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DR   EMBL; AJ271290; CAC29020.1; -; mRNA.
DR   EMBL; AB049214; BAB68410.1; -; Genomic_DNA.
DR   EMBL; AB067443; BAB83505.1; -; Genomic_DNA.
DR   EMBL; AF443201; AAL39061.1; -; mRNA.
DR   EMBL; CR456373; CAG30259.1; -; mRNA.
DR   EMBL; AK075467; BAC11637.1; -; mRNA.
DR   EMBL; AK314502; BAG37102.1; -; mRNA.
DR   EMBL; AP000350; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471095; EAW59618.1; -; Genomic_DNA.
DR   EMBL; BC100808; AAI00809.1; -; mRNA.
DR   CCDS; CCDS13818.1; -. [Q9BYW1-4]
DR   CCDS; CCDS33616.1; -. [Q9BYW1-3]
DR   CCDS; CCDS46673.1; -. [Q9BYW1-1]
DR   RefSeq; NP_001020109.1; NM_001024938.3. [Q9BYW1-1]
DR   RefSeq; NP_001020110.1; NM_001024939.3. [Q9BYW1-3]
DR   RefSeq; NP_110434.3; NM_030807.4. [Q9BYW1-4]
DR   AlphaFoldDB; Q9BYW1; -.
DR   SMR; Q9BYW1; -.
DR   BioGRID; 122454; 1.
DR   STRING; 9606.ENSP00000483038; -.
DR   DrugBank; DB01914; D-glucose.
DR   DrugBank; DB09341; Dextrose, unspecified form.
DR   DrugBank; DB09502; Fludeoxyglucose (18F).
DR   TCDB; 2.A.1.1.44; the major facilitator superfamily (mfs).
DR   GlyGen; Q9BYW1; 1 site.
DR   iPTMnet; Q9BYW1; -.
DR   PhosphoSitePlus; Q9BYW1; -.
DR   BioMuta; SLC2A11; -.
DR   DMDM; 17366685; -.
DR   MassIVE; Q9BYW1; -.
DR   PaxDb; Q9BYW1; -.
DR   PeptideAtlas; Q9BYW1; -.
DR   PRIDE; Q9BYW1; -.
DR   ProteomicsDB; 20459; -.
DR   ProteomicsDB; 79727; -. [Q9BYW1-1]
DR   ProteomicsDB; 79729; -. [Q9BYW1-3]
DR   Antibodypedia; 45145; 28 antibodies from 12 providers.
DR   DNASU; 66035; -.
DR   Ensembl; ENST00000316185.9; ENSP00000326748.8; ENSG00000133460.20. [Q9BYW1-3]
DR   Ensembl; ENST00000345044.10; ENSP00000342542.5; ENSG00000133460.20. [Q9BYW1-1]
DR   Ensembl; ENST00000398356.6; ENSP00000381399.2; ENSG00000133460.20. [Q9BYW1-4]
DR   Ensembl; ENST00000618502.4; ENSP00000482495.1; ENSG00000275744.4. [Q9BYW1-1]
DR   Ensembl; ENST00000619254.4; ENSP00000480839.1; ENSG00000275744.4. [Q9BYW1-4]
DR   Ensembl; ENST00000620942.4; ENSP00000483163.2; ENSG00000275744.4. [Q9BYW1-3]
DR   GeneID; 66035; -.
DR   KEGG; hsa:66035; -.
DR   MANE-Select; ENST00000316185.9; ENSP00000326748.8; NM_001024939.4; NP_001020110.1. [Q9BYW1-3]
DR   UCSC; uc002zym.6; human. [Q9BYW1-1]
DR   CTD; 66035; -.
DR   DisGeNET; 66035; -.
DR   GeneCards; SLC2A11; -.
DR   HGNC; HGNC:14239; SLC2A11.
DR   HPA; ENSG00000133460; Low tissue specificity.
DR   MIM; 610367; gene.
DR   neXtProt; NX_Q9BYW1; -.
DR   OpenTargets; ENSG00000133460; -.
DR   PharmGKB; PA37861; -.
DR   VEuPathDB; HostDB:ENSG00000133460; -.
DR   eggNOG; KOG0569; Eukaryota.
DR   GeneTree; ENSGT00940000161061; -.
DR   HOGENOM; CLU_001265_30_11_1; -.
DR   InParanoid; Q9BYW1; -.
DR   OMA; WAIEWGI; -.
DR   PhylomeDB; Q9BYW1; -.
DR   TreeFam; TF313762; -.
DR   PathwayCommons; Q9BYW1; -.
DR   Reactome; R-HSA-189200; Cellular hexose transport.
DR   SignaLink; Q9BYW1; -.
DR   BioGRID-ORCS; 66035; 12 hits in 1054 CRISPR screens.
DR   ChiTaRS; SLC2A11; human.
DR   GeneWiki; SLC2A11; -.
DR   GenomeRNAi; 66035; -.
DR   Pharos; Q9BYW1; Tbio.
DR   PRO; PR:Q9BYW1; -.
DR   Proteomes; UP000005640; Chromosome 22.
DR   RNAct; Q9BYW1; protein.
DR   Bgee; ENSG00000133460; Expressed in right hemisphere of cerebellum and 96 other tissues.
DR   ExpressionAtlas; Q9BYW1; baseline and differential.
DR   Genevisible; Q9BYW1; HS.
DR   GO; GO:0030054; C:cell junction; IDA:HPA.
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:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005353; F:fructose 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:0051119; F:sugar transmembrane transporter activity; TAS:Reactome.
DR   GO; GO:0015755; P:fructose transmembrane transport; IDA:UniProtKB.
DR   GO; GO:1904659; P:glucose transmembrane transport; IDA:UniProtKB.
DR   GO; GO:0008645; P:hexose transmembrane transport; TAS:Reactome.
DR   GO; GO:0015749; P:monosaccharide transmembrane transport; IBA:GO_Central.
DR   Gene3D; 1.20.1250.20; -; 1.
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; PR00171; SUGRTRNSPORT.
DR   SUPFAM; SSF103473; SSF103473; 1.
DR   TIGRFAMs; TIGR00879; SP; 1.
DR   PROSITE; PS50850; MFS; 1.
DR   PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell membrane; Glycoprotein; Membrane;
KW   Reference proteome; Sugar transport; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..496
FT                   /note="Solute carrier family 2, facilitated glucose
FT                   transporter member 11"
FT                   /id="PRO_0000050380"
FT   TOPO_DOM        1..11
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        12..32
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        33..61
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        62..82
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        83..97
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        98..118
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        119..128
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        129..149
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        150..157
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        158..178
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        179..187
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        188..208
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        209..273
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        274..294
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        295..311
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        312..332
FT                   /note="Helical; Name=8"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        333..338
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        339..359
FT                   /note="Helical; Name=9"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        360..364
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        365..385
FT                   /note="Helical; Name=10"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        386..408
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        409..429
FT                   /note="Helical; Name=11"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        430..435
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        436..456
FT                   /note="Helical; Name=12"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        457..496
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        47
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1..7
FT                   /note="MRALRRL -> MLHALLRSRM (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15461802"
FT                   /id="VSP_006293"
FT   VAR_SEQ         1..7
FT                   /note="MRALRRL -> MEDELEPSLRPRTQ (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:12175779,
FT                   ECO:0000303|PubMed:14702039"
FT                   /id="VSP_045650"
FT   VAR_SEQ         179..245
FT                   /note="RELLGGPQAWPLLLASCLVPGALQLASLPLLPESPRYLLIDCGDTEACLAAL
FT                   RRLRGSGDLAGELEE -> STTAATGLRGLGRGAGGAGGGARCLPGLPCPAPMGAVPAS
FT                   GPEETGDKPRGSGQCHGALRE (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_006294"
FT   VAR_SEQ         246..496
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_006295"
FT   VARIANT         60
FT                   /note="D -> N (in dbSNP:rs7292659)"
FT                   /id="VAR_046704"
FT   VARIANT         232
FT                   /note="R -> Q (in dbSNP:rs9608213)"
FT                   /evidence="ECO:0000269|PubMed:11741323,
FT                   ECO:0000269|PubMed:14702039"
FT                   /id="VAR_046705"
FT   VARIANT         301
FT                   /note="R -> Q (in dbSNP:rs36015336)"
FT                   /id="VAR_061881"
FT   VARIANT         420
FT                   /note="I -> F (in dbSNP:rs34096096)"
FT                   /id="VAR_046706"
FT   VARIANT         469
FT                   /note="K -> E (in dbSNP:rs60882514)"
FT                   /id="VAR_061882"
FT   CONFLICT        229
FT                   /note="A -> E (in Ref. 3; AAL39061)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   496 AA;  53703 MW;  55FFEA82C7007D6D CRC64;
     MRALRRLIQG RILLLTICAA GIGGTFQFGY NLSIINAPTL HIQEFTNETW QARTGEPLPD
     HLVLLMWSLI VSLYPLGGLF GALLAGPLAI TLGRKKSLLV NNIFVVSAAI LFGFSRKAGS
     FEMIMLGRLL VGVNAGVSMN IQPMYLGESA PKELRGAVAM SSAIFTALGI VMGQVVGLRE
     LLGGPQAWPL LLASCLVPGA LQLASLPLLP ESPRYLLIDC GDTEACLAAL RRLRGSGDLA
     GELEELEEER AACQGCRARR PWELFQHRAL RRQVTSLVVL GSAMELCGND SVYAYASSVF
     RKAGVPEAKI QYAIIGTGSC ELLTAVVSCV VIERVGRRVL LIGGYSLMTC WGSIFTVALC
     LQSSFPWTLY LAMACIFAFI LSFGIGPAGV TGILATELFD QMARPAACMV CGALMWIMLI
     LVGLGFPFIM EALSHFLYVP FLGVCVCGAI YTGLFLPETK GKTFQEISKE LHRLNFPRRA
     QGPTWRSLEV IQSTEL
 
 
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