YEA6_YEAST
ID YEA6_YEAST Reviewed; 335 AA.
AC P39953; D3DLP1;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Mitochondrial nicotinamide adenine dinucleotide transporter 2 {ECO:0000305};
DE AltName: Full=Mitochondrial NAD(+) transporter 2 {ECO:0000303|PubMed:16291748};
GN Name=YEA6; Synonyms=NDT2 {ECO:0000303|PubMed:16291748};
GN OrderedLocusNames=YEL006W;
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=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(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 IDENTIFICATION.
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 [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=16291748; DOI=10.1074/jbc.m510425200;
RA Todisco S., Agrimi G., Castegna A., Palmieri F.;
RT "Identification of the mitochondrial NAD+ transporter in Saccharomyces
RT cerevisiae.";
RL J. Biol. Chem. 281:1524-1531(2006).
RN [6]
RP FUNCTION.
RX PubMed=32906142; DOI=10.1038/s41586-020-2741-7;
RA Luongo T.S., Eller J.M., Lu M.J., Niere M., Raith F., Perry C.,
RA Bornstein M.R., Oliphint P., Wang L., McReynolds M.R., Migaud M.E.,
RA Rabinowitz J.D., Johnson F.B., Johnsson K., Ziegler M., Cambronne X.A.,
RA Baur J.A.;
RT "SLC25A51 is a mammalian mitochondrial NAD+ transporter.";
RL Nature 588:174-179(2020).
CC -!- FUNCTION: Mitochondrial inner membrane carrier protein that mediates
CC the import of NAD(+) into mitochondria (PubMed:16291748,
CC PubMed:32906142). Can transport NAD(+) by unidirectional transport or
CC by exchange with intramitochondrially generated dAMP and dGMP
CC (PubMed:16291748). Also able to transport NAD(+) by exchange with AMP,
CC GMP or deamido-NAD (+) in vitro (PubMed:16291748).
CC {ECO:0000269|PubMed:16291748, ECO:0000269|PubMed:32906142}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dAMP(in) + NAD(+)(out) = dAMP(out) + NAD(+)(in);
CC Xref=Rhea:RHEA:65412, ChEBI:CHEBI:57540, ChEBI:CHEBI:58245;
CC Evidence={ECO:0000269|PubMed:16291748};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65413;
CC Evidence={ECO:0000305|PubMed:16291748};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dGMP(in) + NAD(+)(out) = dGMP(out) + NAD(+)(in);
CC Xref=Rhea:RHEA:65416, ChEBI:CHEBI:57540, ChEBI:CHEBI:57673;
CC Evidence={ECO:0000269|PubMed:16291748};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65417;
CC Evidence={ECO:0000305|PubMed:16291748};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GMP(in) + NAD(+)(out) = GMP(out) + NAD(+)(in);
CC Xref=Rhea:RHEA:65420, ChEBI:CHEBI:57540, ChEBI:CHEBI:58115;
CC Evidence={ECO:0000269|PubMed:16291748};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65421;
CC Evidence={ECO:0000305|PubMed:16291748};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AMP(in) + NAD(+)(out) = AMP(out) + NAD(+)(in);
CC Xref=Rhea:RHEA:65424, ChEBI:CHEBI:57540, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:16291748};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65425;
CC Evidence={ECO:0000305|PubMed:16291748};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=deamido-NAD(+)(in) + NAD(+)(out) = deamido-NAD(+)(out) +
CC NAD(+)(in); Xref=Rhea:RHEA:65428, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:58437; Evidence={ECO:0000269|PubMed:16291748};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65429;
CC Evidence={ECO:0000305|PubMed:16291748};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 1630 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
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DR EMBL; U18530; AAB64483.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07645.1; -; Genomic_DNA.
DR PIR; S50453; S50453.
DR RefSeq; NP_010910.1; NM_001178821.1.
DR AlphaFoldDB; P39953; -.
DR SMR; P39953; -.
DR BioGRID; 36725; 32.
DR DIP; DIP-4659N; -.
DR STRING; 4932.YEL006W; -.
DR TCDB; 2.A.29.10.8; the mitochondrial carrier (mc) family.
DR iPTMnet; P39953; -.
DR MaxQB; P39953; -.
DR PaxDb; P39953; -.
DR PRIDE; P39953; -.
DR EnsemblFungi; YEL006W_mRNA; YEL006W; YEL006W.
DR GeneID; 856712; -.
DR KEGG; sce:YEL006W; -.
DR SGD; S000000732; YEA6.
DR VEuPathDB; FungiDB:YEL006W; -.
DR eggNOG; KOG0764; Eukaryota.
DR GeneTree; ENSGT00940000176809; -.
DR HOGENOM; CLU_015166_6_1_1; -.
DR InParanoid; P39953; -.
DR OMA; TYELIVC; -.
DR BioCyc; YEAST:G3O-30135-MON; -.
DR PRO; PR:P39953; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P39953; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0051724; F:NAD transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:1990549; P:mitochondrial NAD transmembrane transport; IDA:UniProtKB.
DR GO; GO:0035352; P:NAD transmembrane transport; IMP:SGD.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.50.40.10; -; 2.
DR InterPro; IPR002067; Mit_carrier.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR InterPro; IPR044712; SLC25A32-like.
DR PANTHER; PTHR45683; PTHR45683; 1.
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..335
FT /note="Mitochondrial nicotinamide adenine dinucleotide
FT transporter 2"
FT /id="PRO_0000090694"
FT TRANSMEM 42..62
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..218
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..267
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..318
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT REPEAT 36..128
FT /note="Solcar 1"
FT /evidence="ECO:0000255"
FT REPEAT 136..225
FT /note="Solcar 2"
FT /evidence="ECO:0000255"
FT REPEAT 241..329
FT /note="Solcar 3"
FT /evidence="ECO:0000255"
SQ SEQUENCE 335 AA; 36961 MW; 91555A2CE81286AC CRC64;
MNNGDNKTTL ENSKNASLAN GNYAIPTKLN RLKKNADPRV AAISGALSGA LSAMLVCPFD
VAKTRLQAQG LQNMTHQSQH YKGFFGTFAT IFKDEGAAGL YKGLQPTVLG YIPTLMIYFS
VYDFCRKYSV DIFPHSPFLS NASSAITAGA ISTVATNPIW VVKTRLMLQT GIGKYSTHYK
GTIDTFRKII QQEGAKALYA GLVPALLGML NVAIQFPLYE NLKIRFGYSE STDVSTDVTS
SNFQKLILAS MLSKMVASTV TYPHEILRTR MQLKSDLPNT VQRHLLPLIK ITYRQEGFAG
FYSGFATNLV RTVPAAVVTL VSFEYSKKYL TTFFQ