PXN_ARATH
ID PXN_ARATH Reviewed; 331 AA.
AC O04200; Q8L9P5;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Peroxisomal nicotinamide adenine dinucleotide carrier;
DE AltName: Full=Peroxisomal NAD carrier;
DE AltName: Full=Peroxisomal membrane protein 38, (PMP36);
DE Short=AtPMP38;
DE AltName: Full=Protein ABERRANT PEROXISOME MORPHOLOGY 3;
DE AltName: Full=Solute carrier family 25 member 17;
GN Name=PXN; Synonyms=APEM3; OrderedLocusNames=At2g39970; ORFNames=T28M21.13;
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 SUBCELLULAR LOCATION.
RX PubMed=11522909; DOI=10.1093/pcp/pce108;
RA Fukao Y., Hayashi Y., Mano S., Hayashi M., Nishimura M.;
RT "Developmental analysis of a putative ATP/ADP carrier protein localized on
RT glyoxysomal membranes during the peroxisome transition in pumpkin
RT cotyledons.";
RL Plant Cell Physiol. 42:835-841(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
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 [4]
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).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP IDENTIFICATION, AND SUBCELLULAR LOCATION.
RX PubMed=19073763; DOI=10.1105/tpc.108.062042;
RA Linka N., Theodoulou F.L., Haslam R.P., Linka M., Napier J.A.,
RA Neuhaus H.E., Weber A.P.;
RT "Peroxisomal ATP import is essential for seedling development in
RT Arabidopsis thaliana.";
RL Plant Cell 20:3241-3257(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBUNIT, AND TISSUE SPECIFICITY.
RX PubMed=22034551; DOI=10.1093/pcp/pcr147;
RA Mano S., Nakamori C., Fukao Y., Araki M., Matsuda A., Kondo M.,
RA Nishimura M.;
RT "A defect of peroxisomal membrane protein 38 causes enlargement of
RT peroxisomes.";
RL Plant Cell Physiol. 52:2157-2172(2011).
RN [9]
RP FUNCTION, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=22555559; DOI=10.1007/s10863-012-9445-0;
RA Agrimi G., Russo A., Pierri C.L., Palmieri F.;
RT "The peroxisomal NAD+ carrier of Arabidopsis thaliana transports coenzyme A
RT and its derivatives.";
RL J. Bioenerg. Biomembr. 44:333-340(2012).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=21895810; DOI=10.1111/j.1365-313x.2011.04775.x;
RA Bernhardt K., Wilkinson S., Weber A.P., Linka N.;
RT "A peroxisomal carrier delivers NAD? and contributes to optimal fatty acid
RT degradation during storage oil mobilization.";
RL Plant J. 69:1-13(2012).
CC -!- FUNCTION: Mediates the NAD(+) import into peroxisomes. Favors the
CC NAD(+)(in)/AMP(out) antiport exchange, but is also able to catalyze a
CC low unidirectional transport that might be essential under special
CC conditions. Transports CoA, dephospho-CoA, acetyl-CoA, adenosine 3',5'-
CC diphosphate (PAP), NAD(+), AMP, ADP and NADH, but has no activity with
CC ATP, GTP, GDP, NADPH, NADP(+) or FAD. Required for peroxisomes
CC proliferation. {ECO:0000269|PubMed:21895810,
CC ECO:0000269|PubMed:22034551, ECO:0000269|PubMed:22555559}.
CC -!- ACTIVITY REGULATION: Inhibited by pyridoxal 5'-phosphate,
CC bathophenanthroline, tannic acid, mersalyl, mercuric chloride and
CC bromocresol purple. {ECO:0000269|PubMed:22555559}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=102 uM for the NAD(+)/NAD(+) exchange
CC {ECO:0000269|PubMed:21895810, ECO:0000269|PubMed:22555559};
CC KM=119 uM for the AMP/AMP exchange {ECO:0000269|PubMed:21895810,
CC ECO:0000269|PubMed:22555559};
CC Vmax=166 umol/min/g enzyme for the NAD(+)/NAD(+) exchange
CC {ECO:0000269|PubMed:21895810, ECO:0000269|PubMed:22555559};
CC Vmax=416 umol/min/g enzyme for the AMP/AMP exchange
CC {ECO:0000269|PubMed:21895810, ECO:0000269|PubMed:22555559};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:22034551}.
CC -!- SUBCELLULAR LOCATION: Glyoxysome membrane {ECO:0000269|PubMed:11522909,
CC ECO:0000269|PubMed:19073763, ECO:0000269|PubMed:21895810}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:11522909,
CC ECO:0000269|PubMed:19073763, ECO:0000269|PubMed:21895810}.
CC -!- TISSUE SPECIFICITY: Expressed in cotyledons, hypocotyls, vascular
CC tissues, trichomes, hydathodes, seeds, pedicels, flowers and stigma.
CC {ECO:0000269|PubMed:21895810, ECO:0000269|PubMed:22034551}.
CC -!- DISRUPTION PHENOTYPE: No germination or growth inhibition, but delayed
CC storage oil mobilization. Decreased sensitivity to 4-(2,4-
CC dichlorophenoxy)butanoic acid (2,4-DB), a precursor converted in vivo
CC by beta-oxidation into the herbicide 2,4-dichlorophenoxyacetic acid
CC (2,4-D). Enlarged peroxisomes. {ECO:0000269|PubMed:21895810,
CC ECO:0000269|PubMed:22034551}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be an adenine nucleotide carrier.
CC {ECO:0000305|PubMed:11522909}.
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DR EMBL; AB047148; BAB62814.1; -; mRNA.
DR EMBL; AF002109; AAB95282.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09757.1; -; Genomic_DNA.
DR EMBL; AY039858; AAK63962.1; -; mRNA.
DR EMBL; BT003020; AAO23585.1; -; mRNA.
DR EMBL; AY088311; AAM65850.1; -; mRNA.
DR PIR; F84823; F84823.
DR RefSeq; NP_181526.1; NM_129555.4.
DR AlphaFoldDB; O04200; -.
DR SMR; O04200; -.
DR BioGRID; 3922; 1.
DR STRING; 3702.AT2G39970.1; -.
DR TCDB; 2.A.29.6.2; the mitochondrial carrier (mc) family.
DR iPTMnet; O04200; -.
DR PaxDb; O04200; -.
DR PRIDE; O04200; -.
DR ProMEX; O04200; -.
DR ProteomicsDB; 226132; -.
DR EnsemblPlants; AT2G39970.1; AT2G39970.1; AT2G39970.
DR GeneID; 818584; -.
DR Gramene; AT2G39970.1; AT2G39970.1; AT2G39970.
DR KEGG; ath:AT2G39970; -.
DR Araport; AT2G39970; -.
DR TAIR; locus:2061176; AT2G39970.
DR eggNOG; KOG0769; Eukaryota.
DR HOGENOM; CLU_015166_6_3_1; -.
DR InParanoid; O04200; -.
DR OMA; YEWTRSF; -.
DR OrthoDB; 1186395at2759; -.
DR PhylomeDB; O04200; -.
DR PRO; PR:O04200; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O04200; baseline and differential.
DR Genevisible; O04200; AT.
DR GO; GO:0046861; C:glyoxysomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0043132; P:NAD transport; IMP:TAIR.
DR GO; GO:0044375; P:regulation of peroxisome size; IMP:TAIR.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.50.40.10; -; 1.
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 SUPFAM; SSF103506; SSF103506; 1.
DR PROSITE; PS50920; SOLCAR; 3.
PE 1: Evidence at protein level;
KW Antiport; Glyoxysome; Membrane; Peroxisome; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..331
FT /note="Peroxisomal nicotinamide adenine dinucleotide
FT carrier"
FT /id="PRO_0000420694"
FT TRANSMEM 5..25
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..85
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..200
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..255
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT REPEAT 2..91
FT /note="Solcar 1"
FT REPEAT 109..216
FT /note="Solcar 2"
FT REPEAT 229..320
FT /note="Solcar 3"
FT CONFLICT 331
FT /note="S -> I (in Ref. 5; AAM65850)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 331 AA; 36213 MW; 28F6A06215E98EF2 CRC64;
MSDALINGLA GAGGGIIAQL LTYPLQTVNT RQQTERDLKR EKRKLGTIEH MCQVVKQEGW
ERLYGGLAPS LAGTAASQGV YYYFYQVFRN RAEATALARK KKGLGDGSVG MFASLLVAAF
AGSVNVLMTN PIWVIVTRMQ THRKMTKDQT AAPESPSSNA EALVAVEPRP YGTFNTIREV
YDEAGITGFW KGVIPTLIMV SNPSMQFMLY ETMLTKLKKK RALKGSNNVT ALETFLLGAV
AKLGATVTTY PLLVVKSRLQ AKQVTTGDKR QQYKGTLDAI LKMIRYEGLY GFYKGMSTKI
VQSVLAAAVL FMIKEELVKG AKLLLSNATS S
