S19A2_MOUSE
ID S19A2_MOUSE Reviewed; 498 AA.
AC Q9EQN9; Q8BRH5; Q8R4Y1;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Thiamine transporter 1 {ECO:0000303|PubMed:11481326};
DE Short=ThTr-1 {ECO:0000303|PubMed:11481326};
DE AltName: Full=Solute carrier family 19 member 2 {ECO:0000305};
GN Name=Slc19a2 {ECO:0000303|PubMed:11386850, ECO:0000312|MGI:MGI:1928761};
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 {ECO:0000312|Proteomes:UP000000589};
RN [1] {ECO:0000312|EMBL:AAG43424.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1),
RP FUNCTION, SUBCELLULAR LOCATION, TRANSPORTER ACTIVITY, AND INDUCTION.
RX PubMed=11481326; DOI=10.1074/jbc.m104701200;
RA Lo P.K., Chen J.Y., Tang P.P., Lin J., Lin C.H., Su L.T., Wu C.H.,
RA Chen T.L., Yang Y., Wang F.F.;
RT "Identification of a mouse thiamine transporter gene as a direct
RT transcriptional target for p53.";
RL J. Biol. Chem. 276:37186-37193(2001).
RN [2] {ECO:0000312|EMBL:AAL30451.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ {ECO:0000312|EMBL:AAL30451.1};
RX PubMed=11386850; DOI=10.1006/mgme.2001.3184;
RA Oishi K., Hirai T., Gelb B.D., Diaz G.A.;
RT "Slc19a2: cloning and characterization of the murine thiamin transporter
RT cDNA and genomic sequence, the orthologue of the human TRMA gene.";
RL Mol. Genet. Metab. 73:149-159(2001).
RN [3] {ECO:0000312|EMBL:AAK33067.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND TRANSPORTER
RP ACTIVITY.
RX PubMed=11592824; DOI=10.1006/mgme.2001.3241;
RA Fleming J.C., Steinkamp M.P., Kawatsuji R., Tartaglini E., Pinkus J.L.,
RA Pinkus G.S., Fleming M.D., Neufeld E.J.;
RT "Characterization of a murine high-affinity thiamine transporter,
RT Slc19a2.";
RL Mol. Genet. Metab. 74:273-280(2001).
RN [4] {ECO:0000312|EMBL:AAG43424.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION (ISOFORMS 1 AND 2),
RP TRANSPORTER ACTIVITY (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY (ISOFORMS 1
RP AND 2).
RX PubMed=12031504; DOI=10.1016/s0167-4781(02)00305-6;
RA Lo P.K., Wang F.F.;
RT "Identification of transcriptional start sites and splicing of mouse
RT thiamine transporter gene THTR-1 (Slc19a2).";
RL Biochim. Biophys. Acta 1576:209-213(2002).
RN [5] {ECO:0000312|EMBL:BAC32108.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC32108.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:BAC32108.1};
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 [6] {ECO:0000312|Proteomes:UP000000589}
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 [7] {ECO:0000312|EMBL:EDL39259.1}
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8] {ECO:0000312|EMBL:AAH34659.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH34659.1};
RC TISSUE=Eye {ECO:0000312|EMBL:AAH34659.1};
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).
RN [9] {ECO:0000305}
RP FUNCTION, DISRUPTION PHENOTYPE, AND TRANSPORTER ACTIVITY.
RX PubMed=12393806; DOI=10.1093/hmg/11.23.2951;
RA Oishi K., Hofmann S., Diaz G.A., Brown T., Manwani D., Ng L., Young R.,
RA Vlassara H., Ioannou Y.A., Forrest D., Gelb B.D.;
RT "Targeted disruption of Slc19a2, the gene encoding the high-affinity
RT thiamin transporter Thtr-1, causes diabetes mellitus, sensorineural
RT deafness and megaloblastosis in mice.";
RL Hum. Mol. Genet. 11:2951-2960(2002).
RN [10] {ECO:0000305}
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=14567973; DOI=10.1016/s1096-7192(03)00141-0;
RA Fleming J.C., Tartaglini E., Kawatsuji R., Yao D., Fujiwara Y.,
RA Bednarski J.J., Fleming M.D., Neufeld E.J.;
RT "Male infertility and thiamine-dependent erythroid hypoplasia in mice
RT lacking thiamine transporter Slc19a2.";
RL Mol. Genet. Metab. 80:234-241(2003).
RN [11] {ECO:0000305}
RP DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=14738878; DOI=10.1016/j.ydbio.2003.10.026;
RA Oishi K., Barchi M., Au A.C., Gelb B.D., Diaz G.A.;
RT "Male infertility due to germ cell apoptosis in mice lacking the thiamin
RT carrier, Tht1. A new insight into the critical role of thiamin in
RT spermatogenesis.";
RL Dev. Biol. 266:299-309(2004).
RN [12] {ECO:0000305}
RP DISRUPTION PHENOTYPE.
RX PubMed=16642288; DOI=10.1007/s10162-006-0035-x;
RA Liberman M.C., Tartaglini E., Fleming J.C., Neufeld E.J.;
RT "Deletion of SLC19A2, the high affinity thiamine transporter, causes
RT selective inner hair cell loss and an auditory neuropathy phenotype.";
RL J. Assoc. Res. Otolaryngol. 7:211-217(2006).
RN [13] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND TRANSPORTER
RP ACTIVITY.
RX PubMed=22194418; DOI=10.1152/ajpgi.00484.2011;
RA Subramanian V.S., Subramanya S.B., Said H.M.;
RT "Relative contribution of THTR-1 and THTR-2 in thiamin uptake by pancreatic
RT acinar cells: studies utilizing Slc19a2 and Slc19a3 knockout mouse
RT models.";
RL Am. J. Physiol. 302:G572-G578(2012).
CC -!- FUNCTION: High-affinity transporter for the intake of thiamine
CC (PubMed:11481326, PubMed:11592824, PubMed:12393806, PubMed:22194418,
CC PubMed:12031504). Essential for spermatogenesis (PubMed:14567973,
CC PubMed:14738878). {ECO:0000269|PubMed:11481326,
CC ECO:0000269|PubMed:11592824, ECO:0000269|PubMed:12031504,
CC ECO:0000269|PubMed:12393806, ECO:0000269|PubMed:14567973,
CC ECO:0000269|PubMed:14738878, ECO:0000269|PubMed:22194418}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(in) + thiamine(out) = H(+)(out) + thiamine(in);
CC Xref=Rhea:RHEA:71271, ChEBI:CHEBI:15378, ChEBI:CHEBI:18385;
CC Evidence={ECO:0000269|PubMed:11481326, ECO:0000269|PubMed:11592824,
CC ECO:0000269|PubMed:12393806, ECO:0000269|PubMed:22194418};
CC -!- CATALYTIC ACTIVITY: [Isoform 1]:
CC Reaction=H(+)(in) + thiamine(out) = H(+)(out) + thiamine(in);
CC Xref=Rhea:RHEA:71271, ChEBI:CHEBI:15378, ChEBI:CHEBI:18385;
CC Evidence={ECO:0000269|PubMed:12031504};
CC -!- CATALYTIC ACTIVITY: [Isoform 2]:
CC Reaction=H(+)(in) + thiamine(out) = H(+)(out) + thiamine(in);
CC Xref=Rhea:RHEA:71271, ChEBI:CHEBI:15378, ChEBI:CHEBI:18385;
CC Evidence={ECO:0000269|PubMed:12031504};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11481326,
CC ECO:0000269|PubMed:11592824}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9EQN9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9EQN9-2; Sequence=VSP_059029;
CC -!- TISSUE SPECIFICITY: Expressed in cochlear hair cells and duodenum (at
CC protein level) (PubMed:11592824). Detected in pancreatic acinar cells
CC (at protein level) (PubMed:22194418). Also expressed strongly in
CC pancreatic islet cells (PubMed:22194418). Expressed in the testis
CC (PubMed:14738878). {ECO:0000269|PubMed:11592824,
CC ECO:0000269|PubMed:14738878, ECO:0000269|PubMed:22194418}.
CC -!- TISSUE SPECIFICITY: [Isoform 1]: Very highly expressed in liver, and
CC also detected at lower levels in heart, testis, kidney, brain and
CC spleen. {ECO:0000269|PubMed:11386850, ECO:0000269|PubMed:12031504}.
CC -!- TISSUE SPECIFICITY: [Isoform 2]: Expressed at low levels in liver and
CC spleen. {ECO:0000269|PubMed:12031504}.
CC -!- DEVELOPMENTAL STAGE: At embryonic stage 16.5 dpc detected in intestinal
CC enterocytes, pancreatic acinar cells, and cochlear hair cells (at
CC protein level). In newborn mice, detected in brain, kidney, liver and
CC intestine (at protein level). {ECO:0000269|PubMed:11592824}.
CC -!- INDUCTION: Induced in a TP53/p53-dependent manner upon DNA damage.
CC {ECO:0000269|PubMed:11481326}.
CC -!- DISRUPTION PHENOTYPE: Males are infertile with reduced testis size and
CC aspermia (PubMed:14567973, PubMed:14738878). Spermatogenesis fails at
CC the pachytene spermatid stage with apoptosis of germ cells
CC (PubMed:14567973, PubMed:14738878). When fed on a thiamine-free diet,
CC animals develop additional phenotypes including diabetes mellitus,
CC profound hearing loss, and defective hematopoiesis (PubMed:12393806,
CC PubMed:14567973, PubMed:16642288). Pancreatic morphology appears to be
CC normal although insulin secretion is significantly impaired
CC (PubMed:12393806). Erythroid precursors in the bone marrow are almost
CC completely absent leading to loss of reticulocytes in the peripheral
CC blood (PubMed:14567973). The hearing loss phenotype is specifically
CC associated with loss of cochlear inner hair cells (PubMed:16642288).
CC These phenotypes can be reversed in many cases by re-introduction of a
CC high thiamine diet (PubMed:12393806, PubMed:14567973, PubMed:16642288).
CC Thiamine uptake by pancreatic acinar cells from knockout mice was found
CC to be significantly lower than uptake by pancreatic acinar cells of the
CC wild-type littermates (PubMed:22194418). {ECO:0000269|PubMed:12393806,
CC ECO:0000269|PubMed:14567973, ECO:0000269|PubMed:14738878,
CC ECO:0000269|PubMed:16642288, ECO:0000269|PubMed:22194418}.
CC -!- SIMILARITY: Belongs to the reduced folate carrier (RFC) transporter (TC
CC 2.A.48) family. {ECO:0000305}.
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DR EMBL; AF224341; AAL11497.1; -; Genomic_DNA.
DR EMBL; AF179403; AAG43424.1; -; mRNA.
DR EMBL; AF360396; AAL30451.1; -; mRNA.
DR EMBL; AF216204; AAK33067.1; -; mRNA.
DR EMBL; AF326916; AAL85635.1; -; mRNA.
DR EMBL; AF418986; AAM47550.1; -; mRNA.
DR EMBL; AK044825; BAC32108.1; -; mRNA.
DR EMBL; AC105161; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466520; EDL39259.1; -; Genomic_DNA.
DR EMBL; BC034659; AAH34659.1; -; mRNA.
DR CCDS; CCDS15433.1; -. [Q9EQN9-1]
DR CCDS; CCDS69968.1; -. [Q9EQN9-2]
DR RefSeq; NP_001263384.1; NM_001276455.1. [Q9EQN9-2]
DR RefSeq; NP_473428.1; NM_054087.3. [Q9EQN9-1]
DR AlphaFoldDB; Q9EQN9; -.
DR STRING; 10090.ENSMUSP00000037561; -.
DR GlyGen; Q9EQN9; 1 site.
DR PhosphoSitePlus; Q9EQN9; -.
DR EPD; Q9EQN9; -.
DR MaxQB; Q9EQN9; -.
DR PaxDb; Q9EQN9; -.
DR PRIDE; Q9EQN9; -.
DR ProteomicsDB; 256815; -. [Q9EQN9-1]
DR ProteomicsDB; 256816; -. [Q9EQN9-2]
DR Antibodypedia; 1655; 100 antibodies from 20 providers.
DR DNASU; 116914; -.
DR Ensembl; ENSMUST00000044021; ENSMUSP00000037561; ENSMUSG00000040918. [Q9EQN9-1]
DR Ensembl; ENSMUST00000159230; ENSMUSP00000123870; ENSMUSG00000040918. [Q9EQN9-2]
DR GeneID; 116914; -.
DR KEGG; mmu:116914; -.
DR UCSC; uc007did.2; mouse. [Q9EQN9-1]
DR UCSC; uc007die.2; mouse.
DR CTD; 10560; -.
DR MGI; MGI:1928761; Slc19a2.
DR VEuPathDB; HostDB:ENSMUSG00000040918; -.
DR eggNOG; KOG3810; Eukaryota.
DR GeneTree; ENSGT00950000183022; -.
DR InParanoid; Q9EQN9; -.
DR OMA; CYRCRPL; -.
DR OrthoDB; 795242at2759; -.
DR PhylomeDB; Q9EQN9; -.
DR TreeFam; TF313684; -.
DR Reactome; R-MMU-196819; Vitamin B1 (thiamin) metabolism.
DR BioGRID-ORCS; 116914; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Slc19a2; mouse.
DR PRO; PR:Q9EQN9; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9EQN9; protein.
DR Bgee; ENSMUSG00000040918; Expressed in pigmented layer of retina and 227 other tissues.
DR ExpressionAtlas; Q9EQN9; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0015234; F:thiamine transmembrane transporter activity; IDA:MGI.
DR GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
DR GO; GO:0071934; P:thiamine transmembrane transport; IMP:BHF-UCL.
DR GO; GO:0015888; P:thiamine transport; IDA:UniProtKB.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR002666; Folate_carrier.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR028338; ThTr-1.
DR PANTHER; PTHR10686; PTHR10686; 1.
DR Pfam; PF01770; Folate_carrier; 1.
DR PIRSF; PIRSF028739; Folate_carrier; 1.
DR PIRSF; PIRSF500794; Thiamine_transporter_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell membrane; Differentiation;
KW Glycoprotein; Membrane; Phosphoprotein; Reference proteome;
KW Spermatogenesis; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..498
FT /note="Thiamine transporter 1"
FT /id="PRO_0000441105"
FT TOPO_DOM 1..28
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 29..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 47..71
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..105
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 127..128
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 150..164
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 208..295
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 317..334
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 356..360
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 361..381
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 382..386
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 387..407
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 408..423
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 424..444
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 445..456
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 457..477
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 478..498
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O60779"
FT MOD_RES 222
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60779"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 232..269
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_059029"
FT CONFLICT 394
FT /note="Y -> C (in Ref. 5; BAC32108)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 498 AA; 55676 MW; 4B892FE1636D0F34 CRC64;
MDVPARVSRR AAAAAARMLL RTARVPRECW FLPTALLCAY GFFANLRPSE PFLTPYLLGP
DKNLTERQVY NEIYPVWTYS YLLLLFPVFL ATDYLRYKPV ILLQGLSLIV TWFMLLYAQG
LLAIQFLEFF YGIATATEIA YYSYIYTVVD LGMYQKVTSY CRSATLVGFT VGSVLGQILV
SVVGWSLFSL NVISLTCVSV AFAVAWFLPM PQKSLFFHHI PSSCHGVNGL KVQNGGIVTD
TPAANHLPGW EDIESKIPLN LDEPPVEEPE EPKPDRLRVF RVLWNDFLMC YSSRPLLCWS
VWWALSTCGY FQVVNYAQGL WEKVMPSQNA DIYNGGVEAV STLLGASAVF AVGYIKLSWS
TWGEMTLFLC SLLIAAAVYV MDTVQSIWVC YASYVVFRII YMVLITIATF QIAANLSMER
YALVFGVNTF IALALQTLLT LIVVDARGLG LCITTQFLIY ASYFAAISVV FLANGIVSII
KKCRKQEDPS SSPQASTS
