ATP23_YEAST
ID ATP23_YEAST Reviewed; 227 AA.
AC P53722; D6W1J5; Q6TQT3; Q6TQT4;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Mitochondrial inner membrane protease ATP23;
DE EC=3.4.24.-;
GN Name=ATP23; OrderedLocusNames=YNR020C; ORFNames=N3212;
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=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(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 NUCLEOTIDE SEQUENCE [MRNA] OF 1-84 AND 198-227.
RC STRAIN=ATCC 204511 / S288c / AB972;
RA Kennedy M.C., Dietrich F.S.;
RT "Verification of 3' and 5' ends of S.cerevisiae transcripts.";
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, MUTAGENESIS OF GLU-125, AND SUBCELLULAR LOCATION.
RX PubMed=17135290; DOI=10.1091/mbc.e06-09-0801;
RA Zeng X., Neupert W., Tzagoloff A.;
RT "The metalloprotease encoded by ATP23 has a dual function in processing and
RT assembly of subunit 6 of mitochondrial ATPase.";
RL Mol. Biol. Cell 18:617-626(2007).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ATP6, AND MUTAGENESIS OF
RP HIS-124; GLU-125 AND HIS-128.
RX PubMed=17135288; DOI=10.1091/mbc.e06-09-0839;
RA Osman C., Wilmes C., Tatsuta T., Langer T.;
RT "Prohibitins interact genetically with Atp23, a novel processing peptidase
RT and chaperone for the F1F0-ATP synthase.";
RL Mol. Biol. Cell 18:627-635(2007).
CC -!- FUNCTION: Has a dual role in the assembly of mitochondrial ATPase. Acts
CC as a protease that removes the N-terminal 10 residues of mitochondrial
CC ATPase CF(0) subunit 6 (ATP6) at the intermembrane space side. Also
CC involved in the correct assembly of the membrane-embedded ATPase CF(0)
CC particle, probably mediating association of ATP6 with the subunit 9
CC ring. {ECO:0000269|PubMed:17135288, ECO:0000269|PubMed:17135290}.
CC -!- SUBUNIT: Interacts with ATP6. {ECO:0000269|PubMed:17135288}.
CC -!- INTERACTION:
CC P53722; P36046: MIA40; NbExp=5; IntAct=EBI-8059929, EBI-26978;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:17135288, ECO:0000269|PubMed:17135290}; Peripheral
CC membrane protein {ECO:0000269|PubMed:17135288,
CC ECO:0000269|PubMed:17135290}; Intermembrane side
CC {ECO:0000269|PubMed:17135288, ECO:0000269|PubMed:17135290}.
CC Note=Associates loosely with the inner membrane.
CC -!- SIMILARITY: Belongs to the peptidase M76 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA96299.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=DAA10561.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; Z71635; CAA96299.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY389304; AAQ97236.1; -; mRNA.
DR EMBL; AY389305; AAQ97237.1; -; mRNA.
DR EMBL; BK006947; DAA10561.1; ALT_INIT; Genomic_DNA.
DR PIR; S63351; S63351.
DR RefSeq; NP_014417.3; NM_001183197.3.
DR AlphaFoldDB; P53722; -.
DR SMR; P53722; -.
DR BioGRID; 35845; 479.
DR IntAct; P53722; 1.
DR MINT; P53722; -.
DR STRING; 4932.YNR020C; -.
DR MEROPS; M67.A11; -.
DR MEROPS; M76.002; -.
DR MaxQB; P53722; -.
DR PaxDb; P53722; -.
DR PRIDE; P53722; -.
DR GeneID; 855754; -.
DR KEGG; sce:YNR020C; -.
DR SGD; S000005303; ATP23.
DR eggNOG; KOG3314; Eukaryota.
DR HOGENOM; CLU_079125_0_0_1; -.
DR InParanoid; P53722; -.
DR BioCyc; YEAST:G3O-33334-MON; -.
DR PRO; PR:P53722; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53722; protein.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IDA:SGD.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0034982; P:mitochondrial protein processing; IMP:SGD.
DR GO; GO:0033615; P:mitochondrial proton-transporting ATP synthase complex assembly; IMP:SGD.
DR InterPro; IPR019165; Peptidase_M76_ATP23.
DR PANTHER; PTHR21711; PTHR21711; 1.
DR Pfam; PF09768; Peptidase_M76; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Membrane; Metal-binding; Metalloprotease; Mitochondrion;
KW Mitochondrion inner membrane; Protease; Reference proteome.
FT CHAIN 1..227
FT /note="Mitochondrial inner membrane protease ATP23"
FT /id="PRO_0000203472"
FT ACT_SITE 125
FT BINDING 124
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305"
FT BINDING 128
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305"
FT MUTAGEN 124
FT /note="H->A: Abolishes proteolytic processing of ATP6, but
FT still promotes assembly of the ATP6 precursor into the
FT ATPase CF(0) particle."
FT /evidence="ECO:0000269|PubMed:17135288"
FT MUTAGEN 125
FT /note="E->Q: Abolishes proteolytic processing of ATP6, but
FT still promotes assembly of the ATP6 precursor into the
FT ATPase CF(0) particle."
FT /evidence="ECO:0000269|PubMed:17135288,
FT ECO:0000269|PubMed:17135290"
FT MUTAGEN 128
FT /note="H->A: Abolishes proteolytic processing of ATP6, but
FT still promotes assembly of the ATP6 precursor into the
FT ATPase CF(0) particle."
FT /evidence="ECO:0000269|PubMed:17135288"
SQ SEQUENCE 227 AA; 26890 MW; 93232C45DB1DB10E CRC64;
MNSSGDNAGF EWWRRTMQYK TGIGLTPEEK TRYEDDSKAR ELKKECLKCY EYRDWMLKYS
PTVRFMVQAI TKLNKGSDSK FDDSKIICDY CPDWKGGGFH PELGILLCQN RLRDKWHLED
TLSHELIHYF DDLKWQIDWL NLKHHACSEI RASSLSGECR FWEEFKRRGF RTGFHVARGH
QDCVRRRAII SVSGNPNCQS KEHAAKIVDE VWDSCFADTR PFDEIYR
