S19A3_MACFA
ID S19A3_MACFA Reviewed; 496 AA.
AC Q4R877;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 50.
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; ORFNames=QtsA-13204;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Mediates high affinity thiamine uptake, probably via a proton
CC anti-port mechanism. Has no folate transport activity (By similarity).
CC {ECO:0000250|UniProtKB:Q9BZV2}.
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:0000250|UniProtKB:Q9BZV2};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the reduced folate carrier (RFC) transporter (TC
CC 2.A.48) family. {ECO:0000305}.
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DR EMBL; AB168581; BAE00695.1; -; mRNA.
DR AlphaFoldDB; Q4R877; -.
DR STRING; 9541.XP_005574555.1; -.
DR PRIDE; Q4R877; -.
DR eggNOG; KOG3810; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015234; F:thiamine transmembrane transporter activity; IEA:InterPro.
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 2: Evidence at transcript level;
KW Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..496
FT /note="Thiamine transporter 2"
FT /id="PRO_0000232657"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..53
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75..81
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103..110
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 132..144
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 166..169
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..282
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 304..316
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 317..337
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 338..342
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 343..363
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 364..375
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 376..396
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 397..405
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 427..434
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 435..455
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 456..496
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 210..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 496 AA; 55870 MW; A5EE5899F5065A1B CRC64;
MDCYRTSPSN SWIYTTVILC IFGFFSMMRP SEPFLIPYLS GPDKNLTSEE MTNEIFPVWT
YSYLVLLLPV LVLTDYVRYK PVIILQGISF IITWLLLLFG QGVKTMQVVE FFYGMVTATE
VAYYAYIYSV VSPEHYQRVS GYCRSVTLVA YTAGSVLAQL LVSLANLSYF YLNVISLASV
SVAFLFSLFL PMPKKSMFFH AKPSREIKKS SSVNPVLEET HEGEAPDCEK QKPTSEIPST
SGKLHKGQLN SLKPRNVTVE VFVQWFQDLK ECYSSKRLFY WSLWWAFATA GFNQILNYVQ
ILWDYKSPSQ DSSIYNGAVE ATATFGGAVA AFAVGYVKVN WDLLGELALA VFSVVNAGSL
FLMHYTANIW ACYAGYLIFK SSYMLLITIA VFQIAVNLSV ERYALVFGIN TFIALVIQTI
ITVIVVDQRG LNLPISIQFL VYGSYFAVIA GIFLMRSMYI IYSTKSQKDV QSPAPSENPD
MSHPEEESNA IMSTKL
