ADT_SCHPO
ID ADT_SCHPO Reviewed; 322 AA.
AC Q09188; P78754;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=ADP,ATP carrier protein;
DE AltName: Full=ADP/ATP translocase;
DE AltName: Full=Adenine nucleotide translocator;
DE Short=ANT;
GN Name=anc1; ORFNames=SPBC530.10c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=972 / ATCC 24843;
RX PubMed=8675018; DOI=10.1016/0378-1119(96)00095-9;
RA Couzin N., Trezeguet V., Saux A.L., Lauquin G.J.-M.;
RT "Cloning of the gene encoding the mitochondrial adenine nucleotide carrier
RT of Schizosaccharomyces pombe by functional complementation in Saccharomyces
RT cerevisiae.";
RL Gene 171:113-117(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-305.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
CC -!- FUNCTION: ADP:ATP antiporter that mediates import of ADP into the
CC mitochondrial matrix for ATP synthesis, and export of ATP out to fuel
CC the cell (PubMed:8675018). Cycles between the cytoplasmic-open state
CC (c-state) and the matrix-open state (m-state): operates by the
CC alternating access mechanism with a single substrate-binding site
CC intermittently exposed to either the cytosolic (c-state) or matrix (m-
CC state) side of the inner mitochondrial membrane (By similarity).
CC {ECO:0000250|UniProtKB:G2QNH0, ECO:0000269|PubMed:8675018}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ADP(in) + ATP(out) = ADP(out) + ATP(in); Xref=Rhea:RHEA:34999,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000305|PubMed:8675018};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35000;
CC Evidence={ECO:0000305|PubMed:8675018};
CC -!- ACTIVITY REGULATION: The matrix-open state (m-state) is inhibited by
CC the membrane-permeable bongkrekic acid (BKA). The cytoplasmic-open
CC state (c-state) is inhibited by the membrane-impermeable toxic
CC inhibitor carboxyatractyloside (CATR). {ECO:0000250|UniProtKB:G2QNH0}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:G2QNH0}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000305|PubMed:8675018}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DOMAIN: The transmembrane helices are not perpendicular to the plane of
CC the membrane, but cross the membrane at an angle. Odd-numbered
CC transmembrane helices exhibit a sharp kink, due to the presence of a
CC conserved proline residue. {ECO:0000250|UniProtKB:G2QNH0}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
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DR EMBL; Z49974; CAA90275.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA19176.1; -; Genomic_DNA.
DR EMBL; D89102; BAA13765.1; -; mRNA.
DR PIR; T40526; T40526.
DR PIR; T42011; T42011.
DR RefSeq; NP_595323.1; NM_001021230.2.
DR AlphaFoldDB; Q09188; -.
DR SMR; Q09188; -.
DR BioGRID; 277416; 5.
DR IntAct; Q09188; 1.
DR STRING; 4896.SPBC530.10c.1; -.
DR iPTMnet; Q09188; -.
DR MaxQB; Q09188; -.
DR PaxDb; Q09188; -.
DR PRIDE; Q09188; -.
DR EnsemblFungi; SPBC530.10c.1; SPBC530.10c.1:pep; SPBC530.10c.
DR GeneID; 2540900; -.
DR KEGG; spo:SPBC530.10c; -.
DR PomBase; SPBC530.10c; anc1.
DR VEuPathDB; FungiDB:SPBC530.10c; -.
DR eggNOG; KOG0749; Eukaryota.
DR HOGENOM; CLU_015166_12_0_1; -.
DR InParanoid; Q09188; -.
DR OMA; YDGIVEC; -.
DR PhylomeDB; Q09188; -.
DR Reactome; R-SPO-1268020; Mitochondrial protein import.
DR Reactome; R-SPO-83936; Transport of nucleosides and free purine and pyrimidine bases across the plasma membrane.
DR PRO; PR:Q09188; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IGI:PomBase.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0005471; F:ATP:ADP antiporter activity; IGI:PomBase.
DR GO; GO:0140021; P:mitochondrial ADP transmembrane transport; IGI:PomBase.
DR GO; GO:1990544; P:mitochondrial ATP transmembrane transport; IGI:PomBase.
DR Gene3D; 1.50.40.10; -; 1.
DR InterPro; IPR002113; ADT_euk_type.
DR InterPro; IPR002067; Mit_carrier.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR PANTHER; PTHR45635; PTHR45635; 1.
DR Pfam; PF00153; Mito_carr; 3.
DR PRINTS; PR00927; ADPTRNSLCASE.
DR PRINTS; PR00926; MITOCARRIER.
DR SUPFAM; SSF103506; SSF103506; 1.
DR PROSITE; PS50920; SOLCAR; 3.
PE 1: Evidence at protein level;
KW Antiport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..322
FT /note="ADP,ATP carrier protein"
FT /id="PRO_0000090592"
FT TRANSMEM 27..54
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P18239"
FT TRANSMEM 95..119
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P18239"
FT TRANSMEM 128..148
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P18239"
FT TRANSMEM 198..219
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P18239"
FT TRANSMEM 233..253
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P18239"
FT TRANSMEM 293..313
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P18239"
FT REPEAT 25..118
FT /note="Solcar 1"
FT REPEAT 130..222
FT /note="Solcar 2"
FT REPEAT 230..316
FT /note="Solcar 3"
FT REGION 257..262
FT /note="Important for transport activity"
FT /evidence="ECO:0000250|UniProtKB:P12235"
FT MOTIF 257..262
FT /note="Nucleotide carrier signature motif"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT BINDING 100
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT BINDING 112
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT BINDING 257
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P02722"
SQ SEQUENCE 322 AA; 35020 MW; 8AC3D16A40F41AFC CRC64;
MATSSAAAAA STPVNANTIT ETKNSTFFFD FMMGGVSAAV SKTAAAPIER VKLLIQNQDE
MIRAGRLSHR YKGIGECFKR TAAEEGVISL WRGNTANVLR YFPTQALNFA FKDKFKKMFG
YKKERDGYAK WFAGNLASGG AAGAASLLFV YSLDYARTRL ANDAKSAKKG GERQFNGLVD
VYRKTYRSDG LRGLYRGFGP SVVGIVVYRG LYFGMYDTLK PVVLVGPLEG NFLASFLLGW
AVTTGSGVAS YPLDTIRRRM MMTSGEAVKY SSSFECGRQI LAKEGARSFF KGAGANILRG
VAGAGVLSIY DQVQLLMFGK KF
