ID   YIA6_YEAST              Reviewed;         373 AA.
AC   P40556; D6VVS4;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   24-JAN-2024, entry version 181.
DE   RecName: Full=Mitochondrial nicotinamide adenine dinucleotide transporter 1 {ECO:0000305};
DE   AltName: Full=Mitochondrial NAD(+) transporter 1;
GN   Name=YIA6;
GN   Synonyms=NDT1 {ECO:0000303|PubMed:32906142,
GN   ECO:0000303|PubMed:33087354}; OrderedLocusNames=YIL006W;
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=9169870;
RA   Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA   Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA   Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA   Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA   Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL   Nature 387:84-87(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   CAUTION.
RX   PubMed=12887330; DOI=10.1042/bj20030995;
RA   Hildyard J.C., Halestrap A.P.;
RT   "Identification of the mitochondrial pyruvate carrier in Saccharomyces
RT   cerevisiae.";
RL   Biochem. J. 374:607-611(2003).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
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   TOPOLOGY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 208353 / W303-1A;
RX   PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA   Kim H., Melen K., Oesterberg M., von Heijne G.;
RT   "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN   [7]
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).
RN   [8]
RP   FUNCTION.
RX   PubMed=33087354; DOI=10.1126/sciadv.abe5310;
RA   Kory N., Uit de Bos J., van der Rijt S., Jankovic N., Guera M., Arp N.,
RA   Pena I.A., Prakash G., Chan S.H., Kunchok T., Lewis C.A., Sabatini D.M.;
RT   "MCART1/SLC25A51 is required for mitochondrial NAD transport.";
RL   Sci. Adv. 6:0-0(2020).
CC   -!- FUNCTION: Mitochondrial inner membrane carrier protein that mediates
CC       the import of NAD(+) into mitochondria (PubMed:16291748,
CC       PubMed:32906142, PubMed:33087354). Can transport NAD(+) by
CC       unidirectional transport or by exchange with intramitochondrially
CC       generated dAMP and dGMP (PubMed:16291748). Also able to transport
CC       NAD(+) by exchange with AMP, GMP or deamido-NAD (+) in vitro
CC       (PubMed:16291748). {ECO:0000269|PubMed:16291748,
CC       ECO:0000269|PubMed:32906142, ECO:0000269|PubMed:33087354}.
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.38 mM for NAD(+) {ECO:0000269|PubMed:16291748};
CC         Vmax=617 nmol/min/mg enzyme {ECO:0000269|PubMed:16291748};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:16291748}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:16291748}.
CC   -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Was first identified as the mitochondrial pyruvate transporter
CC       (PubMed:12887330). However, later experiments showed that was a NAD(+)
CC       transporter (PubMed:16291748). {ECO:0000305|PubMed:12887330,
CC       ECO:0000305|PubMed:16291748}.
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DR   EMBL; Z38113; CAA86245.1; -; Genomic_DNA.
DR   EMBL; BK006942; DAA08540.1; -; Genomic_DNA.
DR   PIR; S48451; S48451.
DR   RefSeq; NP_012260.1; NM_001179356.1.
DR   AlphaFoldDB; P40556; -.
DR   SMR; P40556; -.
DR   BioGRID; 34986; 141.
DR   DIP; DIP-4960N; -.
DR   IntAct; P40556; 1.
DR   STRING; 4932.YIL006W; -.
DR   TCDB; 2.A.29.10.5; the mitochondrial carrier (mc) family.
DR   PaxDb; 4932-YIL006W; -.
DR   PeptideAtlas; P40556; -.
DR   EnsemblFungi; YIL006W_mRNA; YIL006W; YIL006W.
DR   GeneID; 854811; -.
DR   KEGG; sce:YIL006W; -.
DR   AGR; SGD:S000001268; -.
DR   SGD; S000001268; YIA6.
DR   VEuPathDB; FungiDB:YIL006W; -.
DR   eggNOG; KOG0764; Eukaryota.
DR   GeneTree; ENSGT00940000176809; -.
DR   HOGENOM; CLU_015166_6_1_1; -.
DR   InParanoid; P40556; -.
DR   OMA; AFYNGMG; -.
DR   OrthoDB; 4772at2759; -.
DR   BioCyc; YEAST:G3O-31285-MONOMER; -.
DR   BioGRID-ORCS; 854811; 7 hits in 10 CRISPR screens.
DR   PRO; PR:P40556; -.
DR   Proteomes; UP000002311; Chromosome IX.
DR   RNAct; P40556; Protein.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR   GO; GO:0051724; F:NAD transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0005477; F:pyruvate secondary active transmembrane transporter activity; IMP:SGD.
DR   GO; GO:1990549; P:mitochondrial NAD transmembrane transport; IDA:UniProtKB.
DR   GO; GO:0006850; P:mitochondrial pyruvate transmembrane transport; IMP:SGD.
DR   GO; GO:0035352; P:NAD transmembrane transport; IDA:SGD.
DR   Gene3D; 1.50.40.10; Mitochondrial carrier domain; 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:SF2; MITOCHONDRIAL NICOTINAMIDE ADENINE DINUCLEOTIDE TRANSPORTER 1-RELATED; 1.
DR   PANTHER; PTHR45683; MITOCHONDRIAL NICOTINAMIDE ADENINE DINUCLEOTIDE TRANSPORTER 1-RELATED-RELATED; 1.
DR   Pfam; PF00153; Mito_carr; 3.
DR   PRINTS; PR00926; MITOCARRIER.
DR   SUPFAM; SSF103506; Mitochondrial carrier; 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..373
FT                   /note="Mitochondrial nicotinamide adenine dinucleotide
FT                   transporter 1"
FT                   /id="PRO_0000090698"
FT   TOPO_DOM        1..80
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        81..101
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        102..141
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        142..162
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        163..176
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        177..199
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        200..235
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        236..256
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        257..280
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        281..297
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        298..335
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        336..358
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        359..373
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   REPEAT          75..166
FT                   /note="Solcar 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          174..263
FT                   /note="Solcar 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          276..364
FT                   /note="Solcar 3"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   373 AA;  41954 MW;  976C767C1D40E8DF CRC64;
     MTQTDNPVPN CGLLPEQQYC SADHEEPLLL HEEQLIFPDH SSQLSSADII EPIKMNSSTE
     SIIGTTLRKK WVPLSSTQIT ALSGAFAGFL SGVAVCPLDV AKTRLQAQGL QTRFENPYYR
     GIMGTLSTIV RDEGPRGLYK GLVPIVLGYF PTWMIYFSVY EFSKKFFHGI FPQFDFVAQS
     CAAITAGAAS TTLTNPIWVV KTRLMLQSNL GEHPTHYKGT FDAFRKLFYQ EGFKALYAGL
     VPSLLGLFHV AIHFPIYEDL KVRFHCYSRE NNTNSINLQR LIMASSVSKM IASAVTYPHE
     ILRTRMQLKS DIPDSIQRRL FPLIKATYAQ EGLKGFYSGF TTNLVRTIPA SAITLVSFEY
     FRNRLENIST MVI
//