TPC1_YEAST
ID TPC1_YEAST Reviewed; 314 AA.
AC P53257; D6VUM8; Q6B1H1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Mitochondrial thiamine pyrophosphate carrier 1;
GN Name=TPC1; OrderedLocusNames=YGR096W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP FUNCTION.
RX PubMed=9178508;
RX DOI=10.1002/(sici)1097-0061(199705)13:6<573::aid-yea107>3.0.co;2-i;
RA el Moualij B., Duyckaerts C., Lamotte-Brasseur J., Sluse F.E.;
RT "Phylogenetic classification of the mitochondrial carrier family of
RT Saccharomyces cerevisiae.";
RL Yeast 13:573-581(1997).
RN [5]
RP FUNCTION.
RX PubMed=10930523; DOI=10.1016/s0005-2736(00)00222-4;
RA Belenkiy R., Haefele A., Eisen M.B., Wohlrab H.;
RT "The yeast mitochondrial transport proteins: new sequences and consensus
RT residues, lack of direct relation between consensus residues and
RT transmembrane helices, expression patterns of the transport protein genes,
RT and protein-protein interactions with other proteins.";
RL Biochim. Biophys. Acta 1467:207-218(2000).
RN [6]
RP FUNCTION, INDUCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=12411483; DOI=10.1093/emboj/cdf583;
RA Marobbio C.M.T., Vozza A., Harding M., Bisaccia F., Palmieri F.,
RA Walker J.E.;
RT "Identification and reconstitution of the yeast mitochondrial transporter
RT for thiamine pyrophosphate.";
RL EMBO J. 21:5653-5661(2002).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [8]
RP IDENTIFICATION BY MASS 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).
CC -!- FUNCTION: Mitochondrial transporter that mediates uptake of thiamine
CC pyrophosphate (ThPP) into mitochondria. {ECO:0000269|PubMed:10930523,
CC ECO:0000269|PubMed:12411483, ECO:0000269|PubMed:9178508}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.51 mM for dATP uptake by unloaded proteoliposomes
CC {ECO:0000269|PubMed:12411483};
CC Vmax=38 umol/min/g enzyme with dATP as substrate uptaken by unloaded
CC proteoliposomes {ECO:0000269|PubMed:12411483};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- INDUCTION: Expression is regulated by carbon source, with very low
CC expression with succinate, acetate, ethanol or pyruvate as carbon
CC source. {ECO:0000269|PubMed:12411483}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
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DR EMBL; Z72881; CAA97099.1; -; Genomic_DNA.
DR EMBL; AY693109; AAT93128.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08189.1; -; Genomic_DNA.
DR PIR; S64401; S64401.
DR RefSeq; NP_011610.3; NM_001181225.3.
DR AlphaFoldDB; P53257; -.
DR SMR; P53257; -.
DR BioGRID; 33339; 35.
DR IntAct; P53257; 1.
DR MINT; P53257; -.
DR STRING; 4932.YGR096W; -.
DR TCDB; 2.A.29.28.1; the mitochondrial carrier (mc) family.
DR PaxDb; P53257; -.
DR PRIDE; P53257; -.
DR EnsemblFungi; YGR096W_mRNA; YGR096W; YGR096W.
DR GeneID; 852988; -.
DR KEGG; sce:YGR096W; -.
DR SGD; S000003328; TPC1.
DR VEuPathDB; FungiDB:YGR096W; -.
DR eggNOG; KOG0752; Eukaryota.
DR GeneTree; ENSGT00550000074902; -.
DR HOGENOM; CLU_015166_10_3_1; -.
DR InParanoid; P53257; -.
DR OMA; MYVCYGA; -.
DR BioCyc; YEAST:G3O-30806-MON; -.
DR Reactome; R-SCE-196819; Vitamin B1 (thiamin) metabolism.
DR SABIO-RK; P53257; -.
DR PRO; PR:P53257; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53257; protein.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IDA:SGD.
DR GO; GO:0090422; F:thiamine pyrophosphate transmembrane transporter activity; IDA:SGD.
DR GO; GO:0015234; F:thiamine transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:1990545; P:mitochondrial thiamine pyrophosphate transmembrane transport; IDA:SGD.
DR GO; GO:0030974; P:thiamine pyrophosphate transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.50.40.10; -; 1.
DR InterPro; IPR002067; Mit_carrier.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR Pfam; PF00153; Mito_carr; 3.
DR PRINTS; PR00926; MITOCARRIER.
DR SUPFAM; SSF103506; SSF103506; 1.
DR PROSITE; PS50920; SOLCAR; 3.
PE 1: Evidence at protein level;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..314
FT /note="Mitochondrial thiamine pyrophosphate carrier 1"
FT /id="PRO_0000090696"
FT TRANSMEM 14..30
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..100
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..186
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..233
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..302
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT REPEAT 14..103
FT /note="Solcar 1"
FT REPEAT 110..195
FT /note="Solcar 2"
FT REPEAT 210..310
FT /note="Solcar 3"
FT CONFLICT 66
FT /note="M -> T (in Ref. 3; AAT93128)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 314 AA; 35137 MW; 1ED829A655ED03F4 CRC64;
MFKEEDSLRK GQNVAAWKTL LAGAVSGLLA RSITAPMDTI KIRLQLTPAN GLKPFGSQVM
EVARSMIKNE GIRSFWKGNI PGSLLYVTYG SAQFSSYSLF NRYLTPFGLE ARLHSLVVGA
FAGITSSIVS YPFDVLRTRL VANNQMHSMS ITREVRDIWK LEGLPGFFKG SIASMTTITL
TASIMFGTYE TIRIYCDENE KTTAAHKKWE LATLNHSAGT IGGVIAKIIT FPLETIRRRM
QFMNSKHLEK FSRHSSVYGS YKGYGFARIG LQILKQEGVS SLYRGILVAL SKTIPTTFVS
FWGYETAIHY LRMY
