S19A2_HUMAN
ID S19A2_HUMAN Reviewed; 497 AA.
AC O60779; B2R9H0; B4E1X4; Q8WV87; Q9UBL7; Q9UKJ2; Q9UN31; Q9UN43;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Thiamine transporter 1;
DE Short=ThTr-1;
DE Short=ThTr1;
DE AltName: Full=Solute carrier family 19 member 2;
DE AltName: Full=Thiamine carrier 1;
DE Short=TC1;
GN Name=SLC19A2; Synonyms=THT1, TRMA;
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), FUNCTION, TISSUE SPECIFICITY,
RP TRANSPORTER ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Placenta;
RX PubMed=10542220; DOI=10.1074/jbc.274.45.31925;
RA Dutta B., Huang W., Molero M., Kekuda R., Leibach F.H., Devoe L.D.,
RA Ganapathy V., Prasad P.D.;
RT "Cloning of the human thiamine transporter, a member of the folate
RT transporter family.";
RL J. Biol. Chem. 274:31925-31929(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND VARIANT TRMA
RP ASP-172.
RX PubMed=10391221; DOI=10.1038/10372;
RA Labay V., Raz T., Baron D., Mandel H., Williams H., Barrett T., Szargel R.,
RA McDonald L., Shalata A., Nosaka K., Gregory S., Cohen N.;
RT "Mutations in SLC19A2 cause thiamine-responsive megaloblastic anaemia
RT associated with diabetes mellitus and deafness.";
RL Nat. Genet. 22:300-304(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), FUNCTION, TISSUE
RP SPECIFICITY, TRANSPORTER ACTIVITY, AND INVOLVEMENT IN TRMA.
RC TISSUE=Skeletal muscle;
RX PubMed=10391222; DOI=10.1038/10379;
RA Fleming J.C., Tartaglini E., Steinkamp M.P., Schorderet D.F., Cohen N.,
RA Neufeld E.J.;
RT "The gene mutated in thiamine-responsive anaemia with diabetes and deafness
RT (TRMA) encodes a functional thiamine transporter.";
RL Nat. Genet. 22:305-308(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Fetal brain;
RX PubMed=10391223; DOI=10.1038/10385;
RA Diaz G.A., Banikazemi M., Oishi K., Desnick R.J., Gelb B.D.;
RT "Mutations in a new gene encoding a thiamine transporter cause thiamine-
RT responsive megaloblastic anaemia syndrome.";
RL Nat. Genet. 22:309-312(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Colon;
RA Subramanian V.S., Chatterjee N.S., Fleming J.C., Neufeld E.J., Said H.M.;
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon, Testis, and Trachea;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [8]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Eye;
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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-222, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP VARIANTS TRMA HIS-93 AND PHE-143.
RX PubMed=10874303;
RX DOI=10.1002/1098-1004(200007)16:1<37::aid-humu7>3.0.co;2-9;
RA Raz T., Labay V., Baron D., Szargel R., Anbinder Y., Barrett T., Rabl W.,
RA Viana M.B., Mandel H., Baruchel A., Cayuela J.-M., Cohen N.;
RT "The spectrum of mutations, including four novel ones, in the thiamine-
RT responsive megaloblastic anemia gene SLC19A2 of eight families.";
RL Hum. Mutat. 16:37-42(2000).
CC -!- FUNCTION: High-affinity transporter for the intake of thiamine.
CC {ECO:0000269|PubMed:10391222, ECO:0000269|PubMed:10542220}.
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:10391222, ECO:0000269|PubMed:10542220};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.5 uM for thiamine {ECO:0000269|PubMed:10542220};
CC pH dependence:
CC Optimum pH is 8-8.5. {ECO:0000269|PubMed:10542220};
CC -!- INTERACTION:
CC O60779; O60635: TSPAN1; NbExp=5; IntAct=EBI-3941998, EBI-3914312;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:10391222,
CC ECO:0000305|PubMed:10542220}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O60779-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O60779-2; Sequence=VSP_036467;
CC -!- TISSUE SPECIFICITY: Ubiquitous; most abundant in skeletal and cardiac
CC muscle. Medium expression in placenta, heart, liver and kidney, low in
CC lung. {ECO:0000269|PubMed:10391222, ECO:0000269|PubMed:10542220}.
CC -!- DISEASE: Thiamine-responsive megaloblastic anemia syndrome (TRMA)
CC [MIM:249270]: An autosomal recessive disease characterized by
CC megaloblastic anemia, diabetes mellitus, and sensorineural deafness.
CC Onset is typically between infancy and adolescence, but all of the
CC cardinal findings are often not present initially. The anemia, and
CC sometimes the diabetes, improves with high doses of thiamine. Other
CC more variable features include optic atrophy, congenital heart defects,
CC short stature, and stroke. {ECO:0000269|PubMed:10391221,
CC ECO:0000269|PubMed:10391222, ECO:0000269|PubMed:10874303}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the reduced folate carrier (RFC) transporter (TC
CC 2.A.48) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD51280.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAD51283.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAG64936.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF160812; AAF15129.1; -; mRNA.
DR EMBL; AJ238413; CAB50771.1; -; Genomic_DNA.
DR EMBL; AJ237724; CAB50770.1; -; mRNA.
DR EMBL; AF135488; AAD45985.1; -; mRNA.
DR EMBL; AF158233; AAD51280.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AF160186; AAD51283.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AF160756; AAD54242.1; -; Genomic_DNA.
DR EMBL; AF153330; AAD43534.1; -; mRNA.
DR EMBL; AF272359; AAK54468.1; -; mRNA.
DR EMBL; AK304021; BAG64936.1; ALT_INIT; mRNA.
DR EMBL; AK313779; BAG36517.1; -; mRNA.
DR EMBL; AK316465; BAH14836.1; -; mRNA.
DR EMBL; AL021068; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471067; EAW90843.1; -; Genomic_DNA.
DR EMBL; CH471067; EAW90846.1; -; Genomic_DNA.
DR EMBL; BC018514; AAH18514.1; -; mRNA.
DR CCDS; CCDS1280.1; -. [O60779-1]
DR CCDS; CCDS81398.1; -. [O60779-2]
DR RefSeq; NP_001306596.1; NM_001319667.1. [O60779-2]
DR RefSeq; NP_008927.1; NM_006996.2. [O60779-1]
DR AlphaFoldDB; O60779; -.
DR BioGRID; 115811; 73.
DR IntAct; O60779; 33.
DR MINT; O60779; -.
DR STRING; 9606.ENSP00000236137; -.
DR BindingDB; O60779; -.
DR ChEMBL; CHEMBL3079; -.
DR DrugBank; DB00152; Thiamine.
DR DrugCentral; O60779; -.
DR TCDB; 2.A.48.1.2; the reduced folate carrier (rfc) family.
DR GlyGen; O60779; 2 sites.
DR iPTMnet; O60779; -.
DR PhosphoSitePlus; O60779; -.
DR BioMuta; SLC19A2; -.
DR EPD; O60779; -.
DR jPOST; O60779; -.
DR MassIVE; O60779; -.
DR MaxQB; O60779; -.
DR PaxDb; O60779; -.
DR PeptideAtlas; O60779; -.
DR PRIDE; O60779; -.
DR ProteomicsDB; 49594; -. [O60779-1]
DR ProteomicsDB; 49595; -. [O60779-2]
DR Antibodypedia; 1655; 100 antibodies from 20 providers.
DR DNASU; 10560; -.
DR Ensembl; ENST00000236137.10; ENSP00000236137.5; ENSG00000117479.15. [O60779-1]
DR Ensembl; ENST00000367804.4; ENSP00000356778.3; ENSG00000117479.15. [O60779-2]
DR GeneID; 10560; -.
DR KEGG; hsa:10560; -.
DR MANE-Select; ENST00000236137.10; ENSP00000236137.5; NM_006996.3; NP_008927.1.
DR UCSC; uc001gge.5; human. [O60779-1]
DR CTD; 10560; -.
DR DisGeNET; 10560; -.
DR GeneCards; SLC19A2; -.
DR GeneReviews; SLC19A2; -.
DR HGNC; HGNC:10938; SLC19A2.
DR HPA; ENSG00000117479; Tissue enhanced (skeletal muscle, tongue).
DR MalaCards; SLC19A2; -.
DR MIM; 249270; phenotype.
DR MIM; 603941; gene.
DR neXtProt; NX_O60779; -.
DR OpenTargets; ENSG00000117479; -.
DR Orphanet; 49827; Thiamine-responsive megaloblastic anemia syndrome.
DR PharmGKB; PA35825; -.
DR VEuPathDB; HostDB:ENSG00000117479; -.
DR eggNOG; KOG3810; Eukaryota.
DR GeneTree; ENSGT00950000183022; -.
DR HOGENOM; CLU_036909_0_1_1; -.
DR InParanoid; O60779; -.
DR OMA; CYRCRPL; -.
DR PhylomeDB; O60779; -.
DR TreeFam; TF313684; -.
DR PathwayCommons; O60779; -.
DR Reactome; R-HSA-196819; Vitamin B1 (thiamin) metabolism.
DR SABIO-RK; O60779; -.
DR SignaLink; O60779; -.
DR BioGRID-ORCS; 10560; 27 hits in 1082 CRISPR screens.
DR ChiTaRS; SLC19A2; human.
DR GeneWiki; SLC19A2; -.
DR GenomeRNAi; 10560; -.
DR Pharos; O60779; Tbio.
DR PRO; PR:O60779; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O60779; protein.
DR Bgee; ENSG00000117479; Expressed in secondary oocyte and 191 other tissues.
DR ExpressionAtlas; O60779; baseline and differential.
DR Genevisible; O60779; HS.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0008517; F:folic acid transmembrane transporter activity; NAS:UniProtKB.
DR GO; GO:0015234; F:thiamine transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0071934; P:thiamine transmembrane transport; ISS:BHF-UCL.
DR GO; GO:0015888; P:thiamine transport; IDA:UniProtKB.
DR GO; GO:0042723; P:thiamine-containing compound metabolic process; TAS:Reactome.
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; Deafness;
KW Diabetes mellitus; Disease variant; Glycoprotein; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..497
FT /note="Thiamine transporter 1"
FT /id="PRO_0000178663"
FT TOPO_DOM 1..28
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 29..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 47..72
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 92..99
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..128
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 150..165
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186..191
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 209..285
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 311..337
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..354
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 355..363
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 364..380
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 381..386
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 387..409
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 410..419
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 420..443
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 444..455
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 456..479
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 480..497
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 222
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 314
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 69..269
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_036467"
FT VARIANT 93
FT /note="D -> H (in TRMA)"
FT /evidence="ECO:0000269|PubMed:10874303"
FT /id="VAR_010249"
FT VARIANT 143
FT /note="S -> F (in TRMA; dbSNP:rs761957186)"
FT /evidence="ECO:0000269|PubMed:10874303"
FT /id="VAR_010250"
FT VARIANT 172
FT /note="G -> D (in TRMA; dbSNP:rs28937595)"
FT /evidence="ECO:0000269|PubMed:10391221"
FT /id="VAR_010248"
SQ SEQUENCE 497 AA; 55400 MW; 87A993E2B6FBFE96 CRC64;
MDVPGPVSRR AAAAAATVLL RTARVRRECW FLPTALLCAY GFFASLRPSE PFLTPYLLGP
DKNLTEREVF NEIYPVWTYS YLVLLFPVFL ATDYLRYKPV VLLQGLSLIV TWFMLLYAQG
LLAIQFLEFF YGIATATEIA YYSYIYSVVD LGMYQKVTSY CRSATLVGFT VGSVLGQILV
SVAGWSLFSL NVISLTCVSV AFAVAWFLPM PQKSLFFHHI PSTCQRVNGI KVQNGGIVTD
TPASNHLPGW EDIESKIPLN MEEPPVEEPE PKPDRLLVLK VLWNDFLMCY SSRPLLCWSV
WWALSTCGYF QVVNYTQGLW EKVMPSRYAA IYNGGVEAVS TLLGAVAVFA VGYIKISWST
WGEMTLSLFS LLIAAAVYIM DTVGNIWVCY ASYVVFRIIY MLLITIATFQ IAANLSMERY
ALVFGVNTFI ALALQTLLTL IVVDASGLGL EITTQFLIYA SYFALIAVVF LASGAVSVMK
KCRKLEDPQS SSQVTTS
