NDT2_ARATH
ID NDT2_ARATH Reviewed; 363 AA.
AC Q8RWA5; Q4A3J5; Q9C6K8; Q9FRI7;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Nicotinamide adenine dinucleotide transporter 2, mitochondrial;
DE Short=AtNDT2;
DE AltName: Full=NAD(+) transporter 2;
GN Name=NDT2; Synonyms=NADT2; OrderedLocusNames=At1g25380; ORFNames=F4F7.45;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=cv. Wassilewskija;
RX PubMed=16055441; DOI=10.1074/jbc.m506045200;
RA Bedhomme M., Hoffmann M., McCarthy E.A., Gambonnet B., Moran R.G.,
RA Rebeille F., Ravanel S.;
RT "Folate metabolism in plants: an Arabidopsis homolog of the mammalian
RT mitochondrial folate transporter mediates folate import into
RT chloroplasts.";
RL J. Biol. Chem. 280:34823-34831(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBSTRATE SPECIFICITY, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=19745225; DOI=10.1074/jbc.m109.041830;
RA Palmieri F., Rieder B., Ventrella A., Blanco E., Do P.T., Nunes-Nesi A.,
RA Trauth A.U., Fiermonte G., Tjaden J., Agrimi G., Kirchberger S.,
RA Paradies E., Fernie A.R., Neuhaus H.E.;
RT "Molecular identification and functional characterization of Arabidopsis
RT thaliana mitochondrial and chloroplastic NAD+ carrier proteins.";
RL J. Biol. Chem. 284:31249-31259(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
CC -!- FUNCTION: Mediates the NAD(+) import into chloroplast. Favors the
CC NAD(+)(in)/ADP or AMP(out) antiport exchange, but is also able to
CC catalyze a low unidirectional transport (uniport) of NAD(+). Transports
CC NAD(+), nicotinic acid adenine dinucleotide, nicotinamide
CC mononucleotide, nicotinic acid mononucleotide, FAD, FMN, TTP, TDP, TMP,
CC UTP, UDP, UMP, CTP, CDP, CMP, GTP, GDP, GMP, 3'-AMP, ATP, ADP, AND AMP,
CC has low transport activity with cAMP, NADH and alpha-NAD(+), and has no
CC activity with NADP(+), NADPH, nicotinamide, nicotinic acid, adenosine,
CC thiamine mono- or diphosphate, inorganic phosphate, CoA, folate, NaCl,
CC malate, malonate, citrate, fumarate, aspartate, glutamate, S-
CC adenosylmethionine, lysine, arginine, and ornithine.
CC {ECO:0000269|PubMed:16055441, ECO:0000269|PubMed:19745225}.
CC -!- ACTIVITY REGULATION: Inhibited by pyridoxal 5'-phosphate,
CC bathophenanthroline, tannic acid, mersalyl, mercuric chloride, p-
CC hydroxymercuribenzoate, p-hydroxymercuribenzoate sulfonate, bromocresol
CC purple and N-ethylmaleimide. {ECO:0000269|PubMed:19745225}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.15 mM for the NAD(+)/NAD(+) exchange
CC {ECO:0000269|PubMed:19745225};
CC Vmax=4.76 mmol/min/g enzyme for the NAD(+)/NAD(+) exchange
CC {ECO:0000269|PubMed:19745225};
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in young meristematic shoot area,
CC vascular bundles of leaves, developing siliques including the funiculi,
CC petal veins, developing pollen and central cylinder of roots.
CC {ECO:0000269|PubMed:19745225}.
CC -!- MISCELLANEOUS: Appears to be a mitochondrial envelope-located membrane
CC protein lacking an N-terminal-located transit peptide.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG28807.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG50815.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ871010; CAI38581.1; -; mRNA.
DR EMBL; FM211594; CAR70089.1; -; mRNA.
DR EMBL; AC079281; AAG50815.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC079374; AAG28807.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30615.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM58659.1; -; Genomic_DNA.
DR EMBL; AY093232; AAM13231.1; -; mRNA.
DR EMBL; BT008746; AAP42759.1; -; mRNA.
DR PIR; G86383; G86383.
DR RefSeq; NP_001321077.1; NM_001332677.1.
DR RefSeq; NP_564233.1; NM_102349.4.
DR AlphaFoldDB; Q8RWA5; -.
DR SMR; Q8RWA5; -.
DR BioGRID; 24361; 1.
DR IntAct; Q8RWA5; 1.
DR STRING; 3702.AT1G25380.1; -.
DR TCDB; 2.A.29.10.10; the mitochondrial carrier (mc) family.
DR PaxDb; Q8RWA5; -.
DR PRIDE; Q8RWA5; -.
DR ProteomicsDB; 251101; -.
DR EnsemblPlants; AT1G25380.1; AT1G25380.1; AT1G25380.
DR EnsemblPlants; AT1G25380.2; AT1G25380.2; AT1G25380.
DR GeneID; 839124; -.
DR Gramene; AT1G25380.1; AT1G25380.1; AT1G25380.
DR Gramene; AT1G25380.2; AT1G25380.2; AT1G25380.
DR KEGG; ath:AT1G25380; -.
DR Araport; AT1G25380; -.
DR TAIR; locus:2031240; AT1G25380.
DR eggNOG; KOG0757; Eukaryota.
DR HOGENOM; CLU_015166_6_4_1; -.
DR InParanoid; Q8RWA5; -.
DR OMA; WSHLIAG; -.
DR OrthoDB; 1080385at2759; -.
DR PhylomeDB; Q8RWA5; -.
DR PRO; PR:Q8RWA5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8RWA5; baseline and differential.
DR Genevisible; Q8RWA5; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR GO; GO:0051724; F:NAD transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0035352; P:NAD transmembrane transport; IBA:GO_Central.
DR GO; GO:0043132; P:NAD transport; IDA:TAIR.
DR GO; GO:0055085; P: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 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 Antiport; Membrane; Mitochondrion; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..363
FT /note="Nicotinamide adenine dinucleotide transporter 2,
FT mitochondrial"
FT /id="PRO_0000420696"
FT TRANSMEM 21..41
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 215..235
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..299
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT REPEAT 15..107
FT /note="Solcar 1"
FT REPEAT 115..203
FT /note="Solcar 2"
FT REPEAT 215..305
FT /note="Solcar 3"
FT REGION 313..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 84
FT /note="S -> L (in Ref. 1; CAI38581)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 363 AA; 39496 MW; 44FA388F224EE992 CRC64;
MIEHGNSTFD YRSIREVAAN AGAGATAGAI AATFVCPLDV IKTRLQVLGL PEAPASGQRG
GVIITSLKNI IKEEGYRGMY RGLSPTIIAL LPNWAVYFSV YGKLKDVLQS SDGKLSIGSN
MIAAAGAGAA TSIATNPLWV VKTRLMTQGI RPGVVPYKSV MSAFSRICHE EGVRGLYSGI
LPSLAGVSHV AIQFPAYEKI KQYMAKMDNT SVENLSPGNV AIASSIAKVI ASILTYPHEV
IRAKLQEQGQ IRNAETKYSG VIDCITKVFR SEGIPGLYRG CATNLLRTTP SAVITFTTYE
MMLRFFRQVV PPETNRSDDR RREEERKNLV SRRGEEEDKD LGLRESQTQS NKISTPHIPL
GSK
