ATP12_YEAST
ID ATP12_YEAST Reviewed; 325 AA.
AC P22135; D6VW09;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Protein ATP12, mitochondrial;
DE Flags: Precursor;
GN Name=ATP12; OrderedLocusNames=YJL180C; ORFNames=J0486;
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 [GENOMIC DNA], FUNCTION, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RX PubMed=1826907; DOI=10.1016/s0021-9258(20)89477-0;
RA Bowman S., Ackerman S.H., Griffiths D.E., Tzagoloff A.;
RT "Characterization of ATP12, a yeast nuclear gene required for the assembly
RT of the mitochondrial F1-ATPase.";
RL J. Biol. Chem. 266:7517-7523(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [3]
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 [4]
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 [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16823961; DOI=10.1021/pr050477f;
RA Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
RT "Toward the complete yeast mitochondrial proteome: multidimensional
RT separation techniques for mitochondrial proteomics.";
RL J. Proteome Res. 5:1543-1554(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=22984289; DOI=10.1074/mcp.m112.021105;
RA Voegtle F.N., Burkhart J.M., Rao S., Gerbeth C., Hinrichs J.,
RA Martinou J.C., Chacinska A., Sickmann A., Zahedi R.P., Meisinger C.;
RT "Intermembrane space proteome of yeast mitochondria.";
RL Mol. Cell. Proteomics 11:1840-1852(2012).
CC -!- FUNCTION: Essential for the assembly of the mitochondrial F1-F0
CC complex. {ECO:0000269|PubMed:1826907}.
CC -!- SUBUNIT: Exists either as a homo- or heterooligomer.
CC {ECO:0000269|PubMed:1826907}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16823961,
CC ECO:0000269|PubMed:1826907}. Mitochondrion intermembrane space
CC {ECO:0000269|PubMed:22984289}. Note=Mitochondrial, either as a
CC constituent of the matrix, or in tenous association with the internal
CC side of the inner membrane.
CC -!- MISCELLANEOUS: Present with 6370 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ATP12 family. {ECO:0000305}.
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DR EMBL; M61773; AAA34442.1; -; Genomic_DNA.
DR EMBL; Z49455; CAA89475.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08625.1; -; Genomic_DNA.
DR PIR; S56963; S56963.
DR RefSeq; NP_012355.1; NM_001181613.1.
DR AlphaFoldDB; P22135; -.
DR SMR; P22135; -.
DR BioGRID; 33581; 146.
DR DIP; DIP-3027N; -.
DR IntAct; P22135; 1.
DR MINT; P22135; -.
DR STRING; 4932.YJL180C; -.
DR MaxQB; P22135; -.
DR PaxDb; P22135; -.
DR PRIDE; P22135; -.
DR EnsemblFungi; YJL180C_mRNA; YJL180C; YJL180C.
DR GeneID; 853259; -.
DR KEGG; sce:YJL180C; -.
DR SGD; S000003716; ATP12.
DR VEuPathDB; FungiDB:YJL180C; -.
DR eggNOG; KOG3015; Eukaryota.
DR GeneTree; ENSGT00390000009492; -.
DR HOGENOM; CLU_047893_1_2_1; -.
DR InParanoid; P22135; -.
DR OMA; QGWVMGL; -.
DR BioCyc; YEAST:G3O-31615-MON; -.
DR PRO; PR:P22135; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P22135; protein.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0019904; F:protein domain specific binding; IPI:SGD.
DR GO; GO:0033615; P:mitochondrial proton-transporting ATP synthase complex assembly; IMP:SGD.
DR Gene3D; 1.10.3580.10; -; 1.
DR Gene3D; 3.30.2180.10; -; 1.
DR InterPro; IPR011419; ATP12_ATP_synth-F1-assembly.
DR InterPro; IPR042272; ATP12_ATP_synth-F1-assembly_N.
DR InterPro; IPR023335; ATP12_ortho_dom_sf.
DR PANTHER; PTHR21013; PTHR21013; 1.
DR Pfam; PF07542; ATP12; 1.
PE 1: Evidence at protein level;
KW Chaperone; Mitochondrion; Reference proteome; Transit peptide.
FT TRANSIT 1..?32
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?33..325
FT /note="Protein ATP12, mitochondrial"
FT /id="PRO_0000002421"
FT CONFLICT 48
FT /note="S -> N (in Ref. 1; AAA34442)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 325 AA; 36554 MW; 0571C6C493E12CB1 CRC64;
MLPSLRKGCF IVNSIRLKLP RFYSLNAQPL GTDNTIENNT PTETNRLSKT SQKFWEKVSL
NRDVEKGKIA LQLDGRTIKT PLGNGIIVDN AKSLLAYLLK LEWSSLSSLS IKTHSLPLTS
LVARCIDLQM TNEPGCDPQL VAKIGGNSDV IKNQLLRYLD TDTLLVFSPM NEFEGRLRNA
QNELYIPIIK GMEEFLRNFS SESNIRLQIL DADIHGLRGN QQSDIVKNAA KKYMSSLSPW
DLAILEKTVL TTKSFICGVL LLENKKDTAN LIPALKTDMD NIVRAATLET IFQVEKWGEV
EDTHDVDKRD IRRKIHTAAI AAFKQ
