YIA6_YEAST
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 03-AUG-2022, entry version 175.
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, ECO:0000303|PubMed:33087354};
GN 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; 137.
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; P40556; -.
DR PRIDE; P40556; -.
DR EnsemblFungi; YIL006W_mRNA; YIL006W; YIL006W.
DR GeneID; 854811; -.
DR KEGG; sce:YIL006W; -.
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; PTWAVYM; -.
DR BioCyc; YEAST:G3O-31285-MON; -.
DR PRO; PR:P40556; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40556; 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; 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:0022857; F:transmembrane transporter activity; IBA:GO_Central.
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 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..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
