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ADP/ATP translocase 2 (ADP,ATP carrier protein 2) (ADP,ATP carrier protein, fibroblast isoform) (Adenine nucleotide translocator 2) (ANT 2) (Solute carrier family 25 member 5) [Cleaved into: ADP/ATP translocase 2, N-terminally processed]

 ADT2_HUMAN              Reviewed;         298 AA.
P05141; B2RCV1; O43350;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 7.
12-SEP-2018, entry version 209.
RecName: Full=ADP/ATP translocase 2;
AltName: Full=ADP,ATP carrier protein 2;
AltName: Full=ADP,ATP carrier protein, fibroblast isoform;
AltName: Full=Adenine nucleotide translocator 2;
Short=ANT 2;
AltName: Full=Solute carrier family 25 member 5;
Contains:
RecName: Full=ADP/ATP translocase 2, N-terminally processed;
Name=SLC25A5; Synonyms=ANT2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ARG-111.
TISSUE=Placenta;
PubMed=2168878;
Ku D.-H., Kagan J., Chen S.-T., Chang C.-D., Baserga R., Wurzel J.;
"The human fibroblast adenine nucleotide translocator gene. Molecular
cloning and sequence.";
J. Biol. Chem. 265:16060-16063(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ARG-111.
PubMed=3031073;
Battini R., Ferrari S., Kaczmarek L., Calabretta B., Chen S.T.,
Baserga R.;
"Molecular cloning of a cDNA for a human ADP/ATP carrier which is
growth-regulated.";
J. Biol. Chem. 262:4355-4358(1987).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ARG-111.
PubMed=8918809; DOI=10.1093/nar/24.20.4034;
Chen C.N., Su Y., Baybayan P., Siruno A., Nagaraja R., Mazzarella R.,
Schlessinger D., Chen E.;
"Ordered shotgun sequencing of a 135 kb Xq25 YAC containing ANT2 and
four possible genes, including three confirmed by EST matches.";
Nucleic Acids Res. 24:4034-4041(1996).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-111.
TISSUE=Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 2-31; 34-43; 64-92; 141-147; 189-199 AND 273-296,
CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT THR-2, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=B-cell lymphoma;
Bienvenut W.V.;
Submitted (OCT-2004) to UniProtKB.
[8]
PROTEIN SEQUENCE OF 2-23; 32-43; 50-60; 64-92; 81-92; 97-106; 112-138;
172-199; 207-235; 245-259 AND 281-295, CLEAVAGE OF INITIATOR
METHIONINE, ACETYLATION AT THR-2, METHYLATION AT LYS-52, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Embryonic kidney;
Bienvenut W.V., Waridel P., Quadroni M.;
Submitted (MAR-2009) to UniProtKB.
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 46-297.
TISSUE=Liver;
PubMed=2829183; DOI=10.1073/pnas.85.2.377;
Houldsworth J., Attardi G.;
"Two distinct genes for ADP/ATP translocase are expressed at the mRNA
level in adult human liver.";
Proc. Natl. Acad. Sci. U.S.A. 85:377-381(1988).
[10]
INTERACTION WITH HIV-1 VPR (MICROBIAL INFECTION).
PubMed=16120388; DOI=10.1016/j.mito.2004.06.012;
Deniaud A., Brenner C., Kroemer G.;
"Mitochondrial membrane permeabilization by HIV-1 Vpr.";
Mitochondrion 4:223-233(2004).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, CLEAVAGE OF
INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-105 AND LYS-163, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[13]
FUNCTION, AND IDENTIFICATION IN MMXD COMPLEX.
PubMed=20797633; DOI=10.1016/j.molcel.2010.07.029;
Ito S., Tan L.J., Andoh D., Narita T., Seki M., Hirano Y., Narita K.,
Kuraoka I., Hiraoka Y., Tanaka K.;
"MMXD, a TFIIH-independent XPD-MMS19 protein complex involved in
chromosome segregation.";
Mol. Cell 39:632-640(2010).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[15]
MALONYLATION AT LYS-23; LYS-92; LYS-96 AND LYS-147.
PubMed=21908771; DOI=10.1074/mcp.M111.012658;
Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y.,
He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C.,
Dai J., Verdin E., Ye Y., Zhao Y.;
"The first identification of lysine malonylation substrates and its
regulatory enzyme.";
Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[18]
METHYLATION [LARGE SCALE ANALYSIS] AT LYS-52 AND LYS-147, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[19]
ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: Catalyzes the exchange of cytoplasmic ADP with
mitochondrial ATP across the mitochondrial inner membrane. As part
of the mitotic spindle-associated MMXD complex it may play a role
in chromosome segregation. {ECO:0000269|PubMed:20797633}.
-!- SUBUNIT: Homodimer. Component of the MMXD complex, which includes
CIAO1, ERCC2, CIAO2B, MMS19 and SLC25A5.
{ECO:0000269|PubMed:20797633}.
-!- SUBUNIT: (Microbial infection) Interacts with HIV-1 Vpr.
{ECO:0000269|PubMed:16120388}.
-!- INTERACTION:
Q5S007:LRRK2; NbExp=2; IntAct=EBI-355133, EBI-5323863;
Q9Y6E7:SIRT4; NbExp=2; IntAct=EBI-355133, EBI-2606540;
Q8N357:SLC35F6; NbExp=2; IntAct=EBI-355133, EBI-713484;
-!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass
membrane protein.
-!- DOMAIN: The transmembrane helices are not perpendicular to the
plane of the membrane, but cross the membrane at an angle. Odd-
numbered transmembrane helices exhibit a sharp kink, due to the
presence of a conserved proline residue.
{ECO:0000250|UniProtKB:P02722}.
-!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29)
family. {ECO:0000305}.
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EMBL; M57424; AAA51737.1; -; Genomic_DNA.
EMBL; J02683; AAA35579.1; -; mRNA.
EMBL; L78810; AAB39266.1; -; Genomic_DNA.
EMBL; AK315292; BAG37698.1; -; mRNA.
EMBL; AC004000; AAB96347.1; -; Genomic_DNA.
EMBL; BC056160; AAH56160.1; -; mRNA.
EMBL; J03591; AAA36749.1; -; mRNA.
CCDS; CCDS14578.1; -.
PIR; A29132; A29132.
RefSeq; NP_001143.2; NM_001152.4.
UniGene; Hs.632282; -.
ProteinModelPortal; P05141; -.
SMR; P05141; -.
BioGrid; 106789; 154.
CORUM; P05141; -.
DIP; DIP-33873N; -.
IntAct; P05141; 93.
MINT; P05141; -.
STRING; 9606.ENSP00000360671; -.
ChEMBL; CHEMBL3709670; -.
DrugBank; DB00720; Clodronate.
TCDB; 2.A.29.1.1; the mitochondrial carrier (mc) family.
iPTMnet; P05141; -.
PhosphoSitePlus; P05141; -.
SwissPalm; P05141; -.
BioMuta; SLC25A5; -.
DMDM; 317373597; -.
EPD; P05141; -.
MaxQB; P05141; -.
PaxDb; P05141; -.
PeptideAtlas; P05141; -.
PRIDE; P05141; -.
ProteomicsDB; 51804; -.
TopDownProteomics; P05141; -.
DNASU; 292; -.
Ensembl; ENST00000317881; ENSP00000360671; ENSG00000005022.
GeneID; 292; -.
KEGG; hsa:292; -.
UCSC; uc004erh.5; human.
CTD; 292; -.
DisGeNET; 292; -.
EuPathDB; HostDB:ENSG00000005022.5; -.
GeneCards; SLC25A5; -.
H-InvDB; HIX0028379; -.
HGNC; HGNC:10991; SLC25A5.
HPA; HPA046835; -.
HPA; HPA071684; -.
MIM; 300150; gene.
neXtProt; NX_P05141; -.
OpenTargets; ENSG00000005022; -.
PharmGKB; PA35867; -.
eggNOG; KOG0749; Eukaryota.
eggNOG; ENOG410XNW0; LUCA.
GeneTree; ENSGT00390000011543; -.
HOVERGEN; HBG108348; -.
InParanoid; P05141; -.
KO; K05863; -.
OMA; FRGIHHF; -.
OrthoDB; EOG091G0ULB; -.
PhylomeDB; P05141; -.
TreeFam; TF300743; -.
Reactome; R-HSA-180897; Vpr-mediated induction of apoptosis by mitochondrial outer membrane permeabilization.
Reactome; R-HSA-422356; Regulation of insulin secretion.
ChiTaRS; SLC25A5; human.
GenomeRNAi; 292; -.
PRO; PR:P05141; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000005022; Expressed in 234 organ(s), highest expression level in cortex of kidney.
CleanEx; HS_SLC25A5; -.
Genevisible; P05141; HS.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0045121; C:membrane raft; IEA:Ensembl.
GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
GO; GO:0042645; C:mitochondrial nucleoid; IDA:BHF-UCL.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0071817; C:MMXD complex; IDA:UniProtKB.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0005634; C:nucleus; HDA:UniProtKB.
GO; GO:0015207; F:adenine transmembrane transporter activity; TAS:Reactome.
GO; GO:0005471; F:ATP:ADP antiporter activity; IBA:GO_Central.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL.
GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
GO; GO:1901029; P:negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; IMP:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:UniProtKB.
GO; GO:0050796; P:regulation of insulin secretion; TAS:Reactome.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
Gene3D; 1.50.40.10; -; 1.
InterPro; IPR002113; Aden_trnslctor.
InterPro; IPR002067; Mit_carrier.
InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
InterPro; IPR023395; Mt_carrier_dom_sf.
Pfam; PF00153; Mito_carr; 3.
PRINTS; PR00927; ADPTRNSLCASE.
PRINTS; PR00926; MITOCARRIER.
SUPFAM; SSF103506; SSF103506; 1.
PROSITE; PS50920; SOLCAR; 3.
1: Evidence at protein level;
Acetylation; Chromosome partition; Complete proteome;
Direct protein sequencing; Host-virus interaction; Membrane;
Methylation; Mitochondrion; Mitochondrion inner membrane;
Phosphoprotein; Polymorphism; Reference proteome; Repeat;
Transmembrane; Transmembrane helix; Transport.
CHAIN 1 298 ADP/ATP translocase 2.
/FTId=PRO_0000423220.
INIT_MET 1 1 Removed; alternate.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:25944712,
ECO:0000269|Ref.7, ECO:0000269|Ref.8}.
CHAIN 2 298 ADP/ATP translocase 2, N-terminally
processed.
/FTId=PRO_0000090579.
TRANSMEM 8 37 Helical; Name=1.
{ECO:0000250|UniProtKB:P02722}.
TRANSMEM 75 99 Helical; Name=2.
{ECO:0000250|UniProtKB:P02722}.
TRANSMEM 110 130 Helical; Name=3.
{ECO:0000250|UniProtKB:P02722}.
TRANSMEM 179 199 Helical; Name=4.
{ECO:0000250|UniProtKB:P02722}.
TRANSMEM 211 231 Helical; Name=5.
{ECO:0000250|UniProtKB:P02722}.
TRANSMEM 274 291 Helical; Name=6.
{ECO:0000250|UniProtKB:P02722}.
REPEAT 6 98 Solcar 1.
REPEAT 111 201 Solcar 2.
REPEAT 212 297 Solcar 3.
REGION 235 240 Important for transport activity.
{ECO:0000250|UniProtKB:P12235}.
MOTIF 235 240 Nucleotide carrier signature motif.
{ECO:0000250|UniProtKB:P02722}.
BINDING 80 80 ADP. {ECO:0000250|UniProtKB:P02722}.
BINDING 92 92 ADP. {ECO:0000250|UniProtKB:P02722}.
BINDING 235 235 ADP. {ECO:0000250|UniProtKB:P02722}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:19413330}.
MOD_RES 2 2 N-acetylthreonine; in ADP/ATP translocase
2, N-terminally processed.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:25944712,
ECO:0000269|Ref.7, ECO:0000269|Ref.8}.
MOD_RES 7 7 Phosphoserine.
{ECO:0000250|UniProtKB:Q09073}.
MOD_RES 23 23 N6-malonyllysine.
{ECO:0000269|PubMed:21908771}.
MOD_RES 43 43 N6-succinyllysine.
{ECO:0000250|UniProtKB:P51881}.
MOD_RES 52 52 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000244|PubMed:24129315}.
MOD_RES 52 52 N6,N6-dimethyllysine; alternate.
{ECO:0000269|Ref.8}.
MOD_RES 52 52 N6-methyllysine; alternate.
{ECO:0000269|Ref.8}.
MOD_RES 92 92 N6-malonyllysine.
{ECO:0000269|PubMed:21908771}.
MOD_RES 96 96 N6-malonyllysine.
{ECO:0000269|PubMed:21908771}.
MOD_RES 105 105 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 105 105 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P51881}.
MOD_RES 147 147 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P51881}.
MOD_RES 147 147 N6-malonyllysine; alternate.
{ECO:0000269|PubMed:21908771}.
MOD_RES 147 147 N6-methyllysine; alternate.
{ECO:0000244|PubMed:24129315}.
MOD_RES 147 147 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P51881}.
MOD_RES 163 163 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 166 166 N6-acetyllysine.
{ECO:0000250|UniProtKB:P51881}.
MOD_RES 268 268 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P51881}.
MOD_RES 268 268 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P51881}.
VARIANT 111 111 L -> R (in dbSNP:rs371749).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:2168878,
ECO:0000269|PubMed:3031073,
ECO:0000269|PubMed:8918809}.
/FTId=VAR_030039.
CONFLICT 6 6 V -> L (in Ref. 2; AAA35579).
{ECO:0000305}.
CONFLICT 43 43 K -> M (in Ref. 4; BAG37698).
{ECO:0000305}.
CONFLICT 66 66 G -> E (in Ref. 2; AAA35579).
{ECO:0000305}.
CONFLICT 162 162 V -> G (in Ref. 9; AAA36749).
{ECO:0000305}.
SEQUENCE 298 AA; 32852 MW; DC53D083E7217AFE CRC64;
MTDAAVSFAK DFLAGGVAAA ISKTAVAPIE RVKLLLQVQH ASKQITADKQ YKGIIDCVVR
IPKEQGVLSF WRGNLANVIR YFPTQALNFA FKDKYKQIFL GGVDKRTQFW LYFAGNLASG
GAAGATSLCF VYPLDFARTR LAADVGKAGA EREFRGLGDC LVKIYKSDGI KGLYQGFNVS
VQGIIIYRAA YFGIYDTAKG MLPDPKNTHI VISWMIAQTV TAVAGLTSYP FDTVRRRMMM
QSGRKGTDIM YTGTLDCWRK IARDEGGKAF FKGAWSNVLR GMGGAFVLVL YDEIKKYT


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