S19A3_MOUSE
ID S19A3_MOUSE Reviewed; 488 AA.
AC Q99PL8; Q32MF5;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Thiamine transporter 2;
DE Short=ThTr-2;
DE Short=ThTr2;
DE AltName: Full=Solute carrier family 19 member 3;
GN Name=Slc19a3;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=11136550; DOI=10.1006/mgme.2000.3112;
RA Eudy J.D., Spiegelstein O., Barber R.C., Wlodarczyk B.J., Talbot J.,
RA Finnell R.H.;
RT "Identification and characterization of the human and mouse SLC19A3 gene: a
RT novel member of the reduced folate family of micronutrient transporter
RT genes.";
RL Mol. Genet. Metab. 71:581-590(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP REVIEW.
RX PubMed=14770311; DOI=10.1007/s00424-003-1068-1;
RA Ganapathy V., Smith S.B., Prasad P.D.;
RT "SLC19: the folate/thiamine transporter family.";
RL Pflugers Arch. 447:641-646(2004).
RN [4]
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 {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:22194418};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: High expression in kidney, brain, lung and small
CC intestine (PubMed:11136550). Detected in pancreatic acinar cells (at
CC protein level) (PubMed:22194418). Also expressed strongly in pancreatic
CC islet cells (PubMed:22194418). {ECO:0000269|PubMed:11136550,
CC ECO:0000269|PubMed:22194418}.
CC -!- DISRUPTION PHENOTYPE: Thiamine uptake by pancreatic acinar cells from
CC knockout mice was found to be significantly lower than uptake by
CC pancreatic acinar cells of the wild-type littermates.
CC {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; AF271634; AAG53880.1; -; mRNA.
DR EMBL; BC109154; AAI09155.1; -; mRNA.
DR EMBL; BC109155; AAI09156.1; -; mRNA.
DR CCDS; CCDS15101.1; -.
DR RefSeq; NP_085033.2; NM_030556.2.
DR RefSeq; XP_006496642.1; XM_006496579.3.
DR RefSeq; XP_006496643.1; XM_006496580.3.
DR RefSeq; XP_011237017.1; XM_011238715.2.
DR RefSeq; XP_011237018.1; XM_011238716.2.
DR AlphaFoldDB; Q99PL8; -.
DR STRING; 10090.ENSMUSP00000126646; -.
DR GlyGen; Q99PL8; 2 sites.
DR iPTMnet; Q99PL8; -.
DR PhosphoSitePlus; Q99PL8; -.
DR PaxDb; Q99PL8; -.
DR PRIDE; Q99PL8; -.
DR ProteomicsDB; 256860; -.
DR Antibodypedia; 34387; 133 antibodies from 25 providers.
DR DNASU; 80721; -.
DR Ensembl; ENSMUST00000045560; ENSMUSP00000041683; ENSMUSG00000038496.
DR Ensembl; ENSMUST00000164473; ENSMUSP00000126646; ENSMUSG00000038496.
DR GeneID; 80721; -.
DR KEGG; mmu:80721; -.
DR UCSC; uc007bsi.2; mouse.
DR CTD; 80704; -.
DR MGI; MGI:1931307; Slc19a3.
DR VEuPathDB; HostDB:ENSMUSG00000038496; -.
DR eggNOG; KOG3810; Eukaryota.
DR GeneTree; ENSGT00950000183022; -.
DR HOGENOM; CLU_036909_0_0_1; -.
DR InParanoid; Q99PL8; -.
DR OMA; QDVYPFG; -.
DR OrthoDB; 795242at2759; -.
DR PhylomeDB; Q99PL8; -.
DR TreeFam; TF313684; -.
DR Reactome; R-MMU-196819; Vitamin B1 (thiamin) metabolism.
DR BioGRID-ORCS; 80721; 1 hit in 72 CRISPR screens.
DR PRO; PR:Q99PL8; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q99PL8; protein.
DR Bgee; ENSMUSG00000038496; Expressed in duodenum and 68 other tissues.
DR Genevisible; Q99PL8; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0015234; F:thiamine transmembrane transporter activity; IMP:BHF-UCL.
DR GO; GO:0071934; P:thiamine transmembrane transport; IMP:BHF-UCL.
DR GO; GO:0015888; P:thiamine transport; IMP: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; IPR028337; ThTr-2.
DR PANTHER; PTHR10686; PTHR10686; 1.
DR Pfam; PF01770; Folate_carrier; 1.
DR PIRSF; PIRSF028739; Folate_carrier; 1.
DR PIRSF; PIRSF500795; Thiamine_transporter_2; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00806; rfc; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..488
FT /note="Thiamine transporter 2"
FT /id="PRO_0000232658"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..54
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..82
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 104..111
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 133..145
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 167..172
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 194..276
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 298..310
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 311..331
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 332..335
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 357..369
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 391..399
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 400..420
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 421..428
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 429..449
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 450..488
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 469..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 358
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 129
FT /note="Y -> H (in Ref. 1; AAG53880)"
FT /evidence="ECO:0000305"
FT CONFLICT 183
FT /note="V -> G (in Ref. 1; AAG53880)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="V -> G (in Ref. 1; AAG53880)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="F -> V (in Ref. 1; AAG53880)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="M -> K (in Ref. 1; AAG53880)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 488 AA; 55073 MW; B078ECED31936B1F CRC64;
MDSSCRTPPS NSWVYPTVIL CLFGFFSMFR PSEAFLIPFL SEPSKNLTSP EMTNEILPVW
TYSYLATLPP VFVLTDYLRY KPVIMLHVVA FATSYLFLLF GQGVMLMQTA EFFFGVVSAT
EIAYFAYIYS MVSPEHYQKV SSYCRSITLV AYTAGSVLAQ LLVSLTNLPY SSLFYISLAC
VSVAFFFSLF LPMPKKSMFF HAKSDRDDCP KPLEQCTVPK EAQSNRTHSE LFANSKNLED
REMSNPDPEN SALRHFAHWF QDLKECYSSK HLVYWSLWWA FATAGYNQIL NYVQVLWEHK
APSQDSSIYN GAVEAIATFG GALASFSVGY LKVNWDLLGE LGLAVFSAVI AGSLFLMNYS
RSIWVCYAGY LLVKSSYSFL ITIAVFQIAV NLSLERYALV FGIDTFIALV IQTIMTMIVV
DQRGLQLPVT TQFLVYGSYF AVIAGVFLMR SIYILCSAKC RKEVQNLATT RSPNEPHPQE
PSNVSTKF
