ID A0A2K5L4B6_CERAT Unreviewed; 495 AA.
AC A0A2K5L4B6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Thiamine transporter 1 {ECO:0000256|PIRNR:PIRNR028739};
DE Short=ThTr-1 {ECO:0000256|PIRNR:PIRNR028739};
DE AltName: Full=Solute carrier family 19 member 2 {ECO:0000256|PIRNR:PIRNR028739};
GN Name=SLC19A2 {ECO:0000313|Ensembl:ENSCATP00000007788.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000007788.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000007788.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: High-affinity transporter for the intake of thiamine.
CC {ECO:0000256|PIRNR:PIRNR028739}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|PIRNR:PIRNR028739};
CC Multi-pass membrane protein {ECO:0000256|PIRNR:PIRNR028739}.
CC -!- SIMILARITY: Belongs to the reduced folate carrier (RFC) transporter (TC
CC 2.A.48) family. {ECO:0000256|ARBA:ARBA00005773,
CC ECO:0000256|PIRNR:PIRNR028739}.
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DR RefSeq; XP_011946426.1; XM_012091036.1.
DR AlphaFoldDB; A0A2K5L4B6; -.
DR STRING; 9531.ENSCATP00000007788; -.
DR Ensembl; ENSCATT00000026701.1; ENSCATP00000007788.1; ENSCATG00000023069.1.
DR GeneID; 105600165; -.
DR KEGG; caty:105600165; -.
DR CTD; 10560; -.
DR GeneTree; ENSGT00950000183022; -.
DR OMA; CYRCRPL; -.
DR OrthoDB; 51626at2759; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000023069; Expressed in skeletal muscle tissue and 12 other cell types or tissues.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015234; F:thiamine transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0031923; P:pyridoxine transport; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:Ensembl.
DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR InterPro; IPR002666; Folate_carrier.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR028338; ThTr-1.
DR PANTHER; PTHR10686; FOLATE TRANSPORTER; 1.
DR PANTHER; PTHR10686:SF19; THIAMINE TRANSPORTER 1; 1.
DR Pfam; PF01770; Folate_carrier; 1.
DR PIRSF; PIRSF028739; Folate_carrier; 1.
DR PIRSF; PIRSF500794; Thiamine_transporter_1; 1.
DR SUPFAM; SSF103473; MFS general substrate transporter; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|PIRNR:PIRNR028739};
KW Glycoprotein {ECO:0000256|PIRNR:PIRNR028739};
KW Membrane {ECO:0000256|PIRNR:PIRNR028739, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000233060};
KW Transmembrane {ECO:0000256|PIRNR:PIRNR028739, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|PIRNR:PIRNR028739,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|PIRNR:PIRNR028739}.
FT TRANSMEM 27..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 74..93
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 100..121
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 159..180
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 293..310
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 330..352
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 364..386
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 392..411
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 418..441
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 453..474
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 495 AA; 55199 MW; 27C8864D7762E215 CRC64;
MDVPGPVSRR AAAAAVLLRT ARVPRECWFL PTALLCAYGF FANLRPSEPF LTPYLLGPDK
NLTDREVFNE IYPVWTYSYL VLLFPVFLAT DYLRYKPVVL LQGLSLIVTW FMLLYAQGLL
AIQFLEFFYG IATATEIAYY SYIYSVVDLG MYQKVTSYCR SATLVGFTVG SVLGQILVSV
AGWSLFSLNV ISLTCVSVAF AVAWFLPMPQ KSLFFHHIPS TCQRVNGIKV QNGGIVTDTP
ASNHLPGWED IESKIPLNME EPPMEEPEPK PDRLLVLKVL WNDFLMCYSS RPLLCWSVWW
ALSTCGYFQV VNYTQGLWEK VMPSRYAAIY NGGVEAVSTL LGAVAVFAVG YIKISWSTWG
EMTLSLFSLL IAAAVYIMDT VGNIWVCYAS YVVFRIIYML LITIATFQIA ANLSMERYAL
VFGVNTFIAL ALQTLLTLIV VDASGLGLEI TTQFLIYAGY FALIAVVFLA SGAVSIMKKC
RKLEDPESSS QVTTS
//
