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ANT1_YEAST
ID   ANT1_YEAST              Reviewed;         328 AA.
AC   Q06497; D6W4C5;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 160.
DE   RecName: Full=Peroxisomal adenine nucleotide transporter 1;
GN   Name=ANT1; OrderedLocusNames=YPR128C;
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=9169875;
RA   Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA   Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA   Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA   Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA   DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA   Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA   Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA   Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA   Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA   Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA   Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA   Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA   Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA   Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA   Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA   Vo D.H., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL   Nature 387:103-105(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   FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=11566870; DOI=10.1093/emboj/20.18.5049;
RA   Palmieri L., Rottensteiner H., Girzalsky W., Scarcia P., Palmieri F.,
RA   Erdmann R.;
RT   "Identification and functional reconstitution of the yeast peroxisomal
RT   adenine nucleotide transporter.";
RL   EMBO J. 20:5049-5059(2001).
RN   [4]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=11390660; DOI=10.1128/mcb.21.13.4321-4329.2001;
RA   van Roermund C.W.T., Drissen R., van Den Berg M., Ijlst L., Hettema E.H.,
RA   Tabak H.F., Waterham H.R., Wanders R.J.A.;
RT   "Identification of a peroxisomal ATP carrier required for medium-chain
RT   fatty acid beta-oxidation and normal peroxisome proliferation in
RT   Saccharomyces cerevisiae.";
RL   Mol. Cell. Biol. 21:4321-4329(2001).
RN   [5]
RP   INDUCTION.
RX   PubMed=12071844; DOI=10.1042/bj20011495;
RA   Rottensteiner H., Palmieri L., Hartig A., Hamilton B., Ruis H., Erdmann R.,
RA   Gurvitz A.;
RT   "The peroxisomal transporter gene ANT1 is regulated by a deviant oleate
RT   response element (ORE): characterization of the signal for fatty acid
RT   induction.";
RL   Biochem. J. 365:109-117(2002).
RN   [6]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [7]
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   [8]
RP   FUNCTION.
RX   PubMed=15219179; DOI=10.1042/bj20040856;
RA   Lasorsa F.M., Scarcia P., Erdmann R., Palmieri F., Rottensteiner H.,
RA   Palmieri L.;
RT   "The yeast peroxisomal adenine nucleotide transporter: characterization of
RT   two transport modes and involvement in DeltapH formation across peroxisomal
RT   membranes.";
RL   Biochem. J. 381:581-585(2004).
RN   [9]
RP   FUNCTION.
RX   PubMed=15316083; DOI=10.1242/jcs.01305;
RA   van Roermund C.W.T., de Jong M., Ijlst L., van Marle J., Dansen T.B.,
RA   Wanders R.J.A., Waterham H.R.;
RT   "The peroxisomal lumen in Saccharomyces cerevisiae is alkaline.";
RL   J. Cell Sci. 117:4231-4237(2004).
CC   -!- FUNCTION: Adenine nucleotide transporter involved in the uniport of ATP
CC       and adenine nucleotide hetero-exchange transport between the cytosol
CC       and the peroxisomal lumen. This transport is accompanied by a proton
CC       transport from the peroxisomal lumen to the cytosol. Transport of ATP
CC       into the peroxisome is required for beta-oxidation of medium-chain
CC       fatty acids. Required for growth on medium-chain fatty acids, pH
CC       gradient formation in peroxisomes and for normal peroxisome
CC       proliferation. {ECO:0000269|PubMed:11390660,
CC       ECO:0000269|PubMed:11566870, ECO:0000269|PubMed:15219179,
CC       ECO:0000269|PubMed:15316083}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000269|PubMed:11390660,
CC       ECO:0000269|PubMed:11566870, ECO:0000269|PubMed:14562095}; Multi-pass
CC       membrane protein {ECO:0000269|PubMed:11390660,
CC       ECO:0000269|PubMed:11566870, ECO:0000269|PubMed:14562095}.
CC   -!- INDUCTION: Induced by oleic acid, through its ORE-like (oleate
CC       responsive element) promoter element and the PIP2-OAF1 transcription
CC       factors. {ECO:0000269|PubMed:12071844}.
CC   -!- MISCELLANEOUS: Present with 2250 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; U40829; AAB68270.1; -; Genomic_DNA.
DR   EMBL; BK006949; DAA11541.1; -; Genomic_DNA.
DR   PIR; S69019; S69019.
DR   RefSeq; NP_015453.1; NM_001184225.1.
DR   AlphaFoldDB; Q06497; -.
DR   SMR; Q06497; -.
DR   BioGRID; 36295; 98.
DR   DIP; DIP-8825N; -.
DR   IntAct; Q06497; 2.
DR   MINT; Q06497; -.
DR   STRING; 4932.YPR128C; -.
DR   TCDB; 2.A.29.17.1; the mitochondrial carrier (mc) family.
DR   iPTMnet; Q06497; -.
DR   MaxQB; Q06497; -.
DR   PaxDb; Q06497; -.
DR   PRIDE; Q06497; -.
DR   EnsemblFungi; YPR128C_mRNA; YPR128C; YPR128C.
DR   GeneID; 856246; -.
DR   KEGG; sce:YPR128C; -.
DR   SGD; S000006332; ANT1.
DR   VEuPathDB; FungiDB:YPR128C; -.
DR   eggNOG; KOG0769; Eukaryota.
DR   HOGENOM; CLU_015166_6_3_1; -.
DR   InParanoid; Q06497; -.
DR   OMA; PLEMINT; -.
DR   BioCyc; YEAST:G3O-34265-MON; -.
DR   PRO; PR:Q06497; -.
DR   Proteomes; UP000002311; Chromosome XVI.
DR   RNAct; Q06497; protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005779; C:integral component of peroxisomal membrane; IDA:SGD.
DR   GO; GO:0000295; F:adenine nucleotide transmembrane transporter activity; IDA:SGD.
DR   GO; GO:0015217; F:ADP transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0005347; F:ATP transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0015866; P:ADP transport; IBA:GO_Central.
DR   GO; GO:0015867; P:ATP transport; IDA:SGD.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IMP:SGD.
DR   GO; GO:0007031; P:peroxisome organization; IMP:SGD.
DR   Gene3D; 1.50.40.10; -; 1.
DR   InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR   InterPro; IPR023395; Mt_carrier_dom_sf.
DR   InterPro; IPR045900; Peroxisomal_Ade_carrier.
DR   PANTHER; PTHR46650; PTHR46650; 1.
DR   Pfam; PF00153; Mito_carr; 3.
DR   SUPFAM; SSF103506; SSF103506; 1.
DR   PROSITE; PS50920; SOLCAR; 3.
PE   1: Evidence at protein level;
KW   Hydrogen ion transport; Ion transport; Membrane; Peroxisome;
KW   Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..328
FT                   /note="Peroxisomal adenine nucleotide transporter 1"
FT                   /id="PRO_0000227603"
FT   TRANSMEM        1..21
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        78..98
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        128..148
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        185..202
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        226..246
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        277..297
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1..101
FT                   /note="Solcar 1"
FT   REPEAT          122..208
FT                   /note="Solcar 2"
FT   REPEAT          220..304
FT                   /note="Solcar 3"
SQ   SEQUENCE   328 AA;  36367 MW;  ED24312E5F57DBB2 CRC64;
     MLTLESALTG AVASAMANIA VYPLDLSKTI IQSQVSPSSS EDSNEGKVLP NRRYKNVVDC
     MINIFKEKGI LGLYQGMTVT TVATFVQNFV YFFWYTFIRK SYMKHKLLGL QSLKNRDGPI
     TPSTIEELVL GVAAASISQL FTSPMAVVAT RQQTVHSAES AKFTNVIKDI YRENNGDITA
     FWKGLRTGLA LTINPSITYA SFQRLKEVFF HDHSNDAGSL SAVQNFILGV LSKMISTLVT
     QPLIVAKAML QSAGSKFTTF QEALLYLYKN EGLKSLWKGV LPQLTKGVIV QGLLFAFRGE
     LTKSLKRLIF LYSSFFLKHN GQRKLAST
 
 
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