GTR9_MOUSE
ID GTR9_MOUSE Reviewed; 538 AA.
AC Q3T9X0; A0A0J9YUW8; B7ZNE4; B9EHN5; D3Z1X2; D6REU9; Q5ERC7; Q7TSK9; Q7TSP0;
AC Q8BZR3; Q99JJ2;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Solute carrier family 2, facilitated glucose transporter member 9 {ECO:0000305};
DE AltName: Full=Glucose transporter type 9 {ECO:0000303|PubMed:16141072};
DE Short=GLUT-9 {ECO:0000303|PubMed:16141072};
DE AltName: Full=Urate transporter {ECO:0000305};
GN Name=Slc2a9 {ECO:0000312|MGI:MGI:2152844};
GN Synonyms=Glut9 {ECO:0000303|PubMed:16141072};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, GLYCOSYLATION, AND MUTAGENESIS OF ASN-71.
RX PubMed=16293642; DOI=10.1210/me.2005-0010;
RA Keembiyehetty C., Augustin R., Carayannopoulos M.O., Steer S.,
RA Manolescu A., Cheeseman C.I., Moley K.H.;
RT "Mouse glucose transporter 9 splice variants are expressed in adult liver
RT and kidney and are up-regulated in diabetes.";
RL Mol. Endocrinol. 20:686-697(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
RC STRAIN=FVB/N; TISSUE=Brain;
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 [6]
RP FUNCTION.
RX PubMed=18842065; DOI=10.1371/journal.pmed.0050197;
RA Caulfield M.J., Munroe P.B., O'Neill D., Witkowska K., Charchar F.J.,
RA Doblado M., Evans S., Eyheramendy S., Onipinla A., Howard P.,
RA Shaw-Hawkins S., Dobson R.J., Wallace C., Newhouse S.J., Brown M.,
RA Connell J.M., Dominiczak A., Farrall M., Lathrop G.M., Samani N.J.,
RA Kumari M., Marmot M., Brunner E., Chambers J., Elliott P., Kooner J.,
RA Laan M., Org E., Veldre G., Viigimaa M., Cappuccio F.P., Ji C., Iacone R.,
RA Strazzullo P., Moley K.H., Cheeseman C.;
RT "SLC2A9 is a high-capacity urate transporter in humans.";
RL PLoS Med. 5:e197-e197(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP FUNCTION, TRANSPORTER ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
RP SPECIFICITY.
RX PubMed=19587147; DOI=10.1152/ajprenal.00139.2009;
RA Bibert S., Hess S.K., Firsov D., Thorens B., Geering K., Horisberger J.D.,
RA Bonny O.;
RT "Mouse GLUT9: evidences for a urate uniporter.";
RL Am. J. Physiol. 297:F612-F619(2009).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=25100214; DOI=10.1038/ncomms5642;
RA DeBosch B.J., Kluth O., Fujiwara H., Schuermann A., Moley K.;
RT "Early-onset metabolic syndrome in mice lacking the intestinal uric acid
RT transporter SLC2A9.";
RL Nat. Commun. 5:4642-4642(2014).
CC -!- FUNCTION: High-capacity urate transporter, which may play a role in the
CC urate reabsorption by proximal tubules. May have a residual high-
CC affinity, low-capacity glucose and fructose transporter activity.
CC Transports urate at rates 45- to 60-fold faster than glucose. Does not
CC transport galactose. May mediate small uptake of adenine but not of
CC other nucleobases. {ECO:0000250|UniProtKB:Q9NRM0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=urate(out) = urate(in); Xref=Rhea:RHEA:60368,
CC ChEBI:CHEBI:17775; Evidence={ECO:0000269|PubMed:19587147};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=649 uM for urate {ECO:0000269|PubMed:19587147};
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC {ECO:0000269|PubMed:16293642, ECO:0000269|PubMed:25100214}; Multi-pass
CC membrane protein {ECO:0000255}. Apical cell membrane
CC {ECO:0000269|PubMed:25100214}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=GLUT9a {ECO:0000303|PubMed:16293642,
CC ECO:0000303|PubMed:18842065};
CC IsoId=Q3T9X0-1; Sequence=Displayed;
CC Name=2; Synonyms=GLUT9b {ECO:0000303|PubMed:16293642,
CC ECO:0000303|PubMed:18842065};
CC IsoId=Q3T9X0-2; Sequence=VSP_060215;
CC Name=3; Synonyms=GLUT9Sa {ECO:0000303|PubMed:16293642};
CC IsoId=Q3T9X0-3; Sequence=VSP_060216;
CC Name=4; Synonyms=GLUT9Sb {ECO:0000303|PubMed:16293642};
CC IsoId=Q3T9X0-4; Sequence=VSP_060215, VSP_060216;
CC -!- TISSUE SPECIFICITY: Highly expressed in the intestine, with high
CC expression in the jejunum and ileum, the segments of the intestine that
CC perform the majority of urate excretion (PubMed:25100214). Isoform 1:
CC Widely expressed (PubMed:16293642). Isoform 1: In kidney, expressed at
CC low levels in proximal tubules (PubMed:19587147). Isoform 2: Primarily
CC expressed in liver and kidney; with specific expression in distal
CC convoluted and connecting tubules of kidney (PubMed:16293642,
CC PubMed:19587147). {ECO:0000269|PubMed:16293642,
CC ECO:0000269|PubMed:19587147, ECO:0000269|PubMed:25100214}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:16293642}.
CC -!- DISRUPTION PHENOTYPE: Conditional knockout mice lacking Slc2a9 in
CC enterocytes are born at the expected Mendelian rate; they show no
CC obvious phenotype and are fertile (PubMed:25100214). Mice however
CC develop impaired enterocyte uric acid transport kinetics,
CC hyperuricaemia, hyperuricosuria, spontaneous hypertension,
CC dyslipidaemia and elevated body fat (PubMed:25100214).
CC {ECO:0000269|PubMed:25100214}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. {ECO:0000305}.
CC -!- CAUTION: High-capacity urate transporter that was first described as a
CC fructose and glucose transporter. Also described in the literature as
CC high-affinity and low-capacity glucose and fructose transporter (By
CC similarity). However, another group could not confirm transporter
CC activity for glucose or fructose (By similarity).
CC {ECO:0000250|UniProtKB:Q9NRM0}.
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DR EMBL; AF490463; AAP44162.1; -; mRNA.
DR EMBL; AF469480; AAP47095.1; -; mRNA.
DR EMBL; AY776155; AAW78908.1; -; mRNA.
DR EMBL; AK033725; BAC28448.1; -; mRNA.
DR EMBL; AK156740; BAE33832.1; -; mRNA.
DR EMBL; AK172234; BAE42900.1; -; mRNA.
DR EMBL; AC084071; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC171271; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466524; EDL37556.1; -; Genomic_DNA.
DR EMBL; BC006076; AAH06076.1; -; mRNA.
DR EMBL; BC138213; AAI38214.1; -; mRNA.
DR EMBL; BC145198; AAI45199.1; -; mRNA.
DR CCDS; CCDS19256.1; -. [Q3T9X0-4]
DR CCDS; CCDS51482.1; -. [Q3T9X0-3]
DR CCDS; CCDS51483.1; -. [Q3T9X0-1]
DR CCDS; CCDS51484.1; -. [Q3T9X0-2]
DR RefSeq; NP_001012363.2; NM_001012363.2. [Q3T9X0-2]
DR RefSeq; NP_001095884.1; NM_001102414.1. [Q3T9X0-1]
DR RefSeq; NP_001095885.1; NM_001102415.1. [Q3T9X0-3]
DR RefSeq; NP_663534.1; NM_145559.2. [Q3T9X0-4]
DR RefSeq; XP_006503746.1; XM_006503683.3. [Q3T9X0-2]
DR RefSeq; XP_006503747.1; XM_006503684.3. [Q3T9X0-2]
DR RefSeq; XP_006503748.1; XM_006503685.3. [Q3T9X0-2]
DR RefSeq; XP_006503749.1; XM_006503686.3. [Q3T9X0-4]
DR RefSeq; XP_006503750.1; XM_006503687.3. [Q3T9X0-4]
DR RefSeq; XP_011238990.1; XM_011240688.2.
DR RefSeq; XP_011238991.1; XM_011240689.2. [Q3T9X0-2]
DR RefSeq; XP_011238992.1; XM_011240690.1. [Q3T9X0-2]
DR AlphaFoldDB; Q3T9X0; -.
DR SMR; Q3T9X0; -.
DR STRING; 10090.ENSMUSP00000063352; -.
DR TCDB; 2.A.1.1.47; the major facilitator superfamily (mfs).
DR GlyGen; Q3T9X0; 2 sites.
DR iPTMnet; Q3T9X0; -.
DR PhosphoSitePlus; Q3T9X0; -.
DR jPOST; Q3T9X0; -.
DR MaxQB; Q3T9X0; -.
DR PaxDb; Q3T9X0; -.
DR PRIDE; Q3T9X0; -.
DR ProteomicsDB; 308426; -.
DR ProteomicsDB; 312849; -.
DR ProteomicsDB; 320503; -.
DR ProteomicsDB; 326260; -.
DR ProteomicsDB; 330641; -. [Q3T9X0-1]
DR ProteomicsDB; 335133; -.
DR ProteomicsDB; 341277; -.
DR Antibodypedia; 22860; 308 antibodies from 25 providers.
DR DNASU; 117591; -.
DR Ensembl; ENSMUST00000005238; ENSMUSP00000005238; ENSMUSG00000005107. [Q3T9X0-4]
DR Ensembl; ENSMUST00000067872; ENSMUSP00000066872; ENSMUSG00000005107. [Q3T9X0-2]
DR Ensembl; ENSMUST00000067886; ENSMUSP00000063352; ENSMUSG00000005107. [Q3T9X0-1]
DR Ensembl; ENSMUST00000129099; ENSMUSP00000122723; ENSMUSG00000005107. [Q3T9X0-2]
DR Ensembl; ENSMUST00000143758; ENSMUSP00000118430; ENSMUSG00000005107. [Q3T9X0-3]
DR Ensembl; ENSMUST00000155634; ENSMUSP00000116354; ENSMUSG00000005107. [Q3T9X0-2]
DR GeneID; 117591; -.
DR KEGG; mmu:117591; -.
DR UCSC; uc008xgo.1; mouse. [Q3T9X0-1]
DR UCSC; uc008xgp.1; mouse.
DR UCSC; uc008xgq.1; mouse.
DR UCSC; uc008xgr.1; mouse.
DR CTD; 56606; -.
DR MGI; MGI:2152844; Slc2a9.
DR VEuPathDB; HostDB:ENSMUSG00000005107; -.
DR eggNOG; KOG0569; Eukaryota.
DR GeneTree; ENSGT00940000159192; -.
DR HOGENOM; CLU_001265_28_0_1; -.
DR InParanoid; Q3T9X0; -.
DR OMA; MYQSEST; -.
DR OrthoDB; 326501at2759; -.
DR PhylomeDB; Q3T9X0; -.
DR TreeFam; TF313762; -.
DR Reactome; R-MMU-189200; Cellular hexose transport.
DR BioGRID-ORCS; 117591; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Slc2a9; mouse.
DR PRO; PR:Q3T9X0; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q3T9X0; protein.
DR Bgee; ENSMUSG00000005107; Expressed in small intestine Peyer's patch and 81 other tissues.
DR ExpressionAtlas; Q3T9X0; baseline and differential.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
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:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0005353; F:fructose transmembrane transporter activity; ISO:MGI.
DR GO; GO:0005355; F:glucose transmembrane transporter activity; IDA:MGI.
DR GO; GO:0015149; F:hexose transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015143; F:urate transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015755; P:fructose transmembrane transport; ISO:MGI.
DR GO; GO:1904659; P:glucose transmembrane transport; IDA:MGI.
DR GO; GO:0015749; P:monosaccharide transmembrane transport; IBA:GO_Central.
DR GO; GO:0046415; P:urate metabolic process; ISO:MGI.
DR GO; GO:0015747; P:urate transport; IDA:UniProtKB.
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; PS00216; SUGAR_TRANSPORT_1; 1.
DR PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Glycoprotein; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..538
FT /note="Solute carrier family 2, facilitated glucose
FT transporter member 9"
FT /id="PRO_0000447626"
FT TOPO_DOM 1..34
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 35..54
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..88
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 89..109
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 110..120
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 121..143
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 144..148
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 149..170
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 171..181
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 182..200
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 201..211
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 212..233
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 234..297
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 298..319
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 320..333
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 334..356
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 357..362
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 363..385
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 386..390
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 391..418
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 419..429
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 430..453
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 454..458
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 459..480
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 481..538
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 495..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRM0"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..31
FT /note="MDSRELALASLMCDTGGPGELSVGHQQRRTK -> MKLSEKNSAETKESQR
FT (in isoform 2 and isoform 4)"
FT /id="VSP_060215"
FT VAR_SEQ 208..315
FT /note="RESTWPYLFGVIIVPALVQLASLPFLPESPRYLLFEKHDEAGAMKAFQTFLG
FT KADVSQELEEALAESRVQRNLRLVSVLELLRAPFVRWQVITVIITMASYQLCGLNA ->
FT R (in isoform 3 and isoform 4)"
FT /id="VSP_060216"
FT MUTAGEN 71
FT /note="N->Q: Decreased N-glycosylation."
FT /evidence="ECO:0000269|PubMed:16293642"
FT CONFLICT 131
FT /note="S -> A (in Ref. 5; AAI45199)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="A -> T (in Ref. 5; AAI45199)"
FT /evidence="ECO:0000305"
FT CONFLICT 362
FT /note="R -> G (in Ref. 1; AAW78908/AAP47095)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 538 AA; 58621 MW; BC939DEFF6C79438 CRC64;
MDSRELALAS LMCDTGGPGE LSVGHQQRRT KKWSFSLVVA ALVGAFGSSF LYGYNLSVVN
APTPYIKAFY NGTWYRRHGQ PIDPDTLTLL WSVTVSIFAI GGLVGTLMVK MIGKFLGRKS
TLLVNNGFAI SAALLMACSL RAGTFEMLIV GRFIMGVDGG IALSALPMYL NEISPKEIRG
SLGQVTAIFI CIGVFSGQLL GLPELLGRES TWPYLFGVII VPALVQLASL PFLPESPRYL
LFEKHDEAGA MKAFQTFLGK ADVSQELEEA LAESRVQRNL RLVSVLELLR APFVRWQVIT
VIITMASYQL CGLNAIWFYT NSIFGKAGIP QDKIPYITLS TGGIETLAAI FSGLVIERLG
RRPLLIGGFG LMALFFGTLT ATLTLQDQAP WVPYLSIVCI LAIIASFCSG PGGIPFILTG
EFFQQSERPA AFMIAGTVNW LSNFAVGLLF PFIQKSLDSY CFLVFATICI AGATYFYFVL
PETKNRTHAE ISQAFAKRNK AQPPEVKADS AMTEEKANSQ TEPDSSSTLD SYGQNKIV
