INA22_YEAST
ID INA22_YEAST Reviewed; 216 AA.
AC P40576; D6VVV5;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Inner membrane assembly complex subunit 22 {ECO:0000305|PubMed:24942160};
DE AltName: Full=INA complex 22 kDa subunit {ECO:0000303|PubMed:24942160};
DE Flags: Precursor;
GN Name=INA22 {ECO:0000303|PubMed:24942160};
GN OrderedLocusNames=YIR024C {ECO:0000312|SGD:S000001463};
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=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(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 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 [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].
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [6]
RP FUNCTION, INTERACTION WITH INA17, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=24942160; DOI=10.15252/embj.201488076;
RA Lytovchenko O., Naumenko N., Oeljeklaus S., Schmidt B.,
RA von der Malsburg K., Deckers M., Warscheid B., van der Laan M., Rehling P.;
RT "The INA complex facilitates assembly of the peripheral stalk of the
RT mitochondrial F1Fo-ATP synthase.";
RL EMBO J. 33:1624-1638(2014).
CC -!- FUNCTION: Component of the INA complex (INAC) that promotes the
CC biogenesis of mitochondrial F(1)F(0)-ATP synthase. INAC facilitates the
CC assembly of the peripheral stalk and promotes the assembly of the
CC catalytic F(1)-domain with the membrane-embedded F(0)-domain.
CC {ECO:0000269|PubMed:24942160}.
CC -!- SUBUNIT: Component of the inner membrane assembly (INA) complex,
CC composed of INA17 and INA22. Interacts with a subset of F(1)F(0)-ATP
CC synthase subunits of the F(1)-domain and the peripheral stalk.
CC {ECO:0000269|PubMed:24942160}.
CC -!- INTERACTION:
CC P40576; Q02888: INA17; NbExp=4; IntAct=EBI-25429, EBI-7668387;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:24942160}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- MISCELLANEOUS: Present with 589 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z38061; CAA86184.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08571.1; -; Genomic_DNA.
DR PIR; S48486; S48486.
DR RefSeq; NP_012290.1; NM_001179546.1.
DR AlphaFoldDB; P40576; -.
DR BioGRID; 35015; 99.
DR ComplexPortal; CPX-3279; INAC inner membrane assembly complex.
DR DIP; DIP-1203N; -.
DR IntAct; P40576; 13.
DR MINT; P40576; -.
DR STRING; 4932.YIR024C; -.
DR MaxQB; P40576; -.
DR PaxDb; P40576; -.
DR PRIDE; P40576; -.
DR EnsemblFungi; YIR024C_mRNA; YIR024C; YIR024C.
DR GeneID; 854842; -.
DR KEGG; sce:YIR024C; -.
DR SGD; S000001463; INA22.
DR VEuPathDB; FungiDB:YIR024C; -.
DR eggNOG; ENOG502S583; Eukaryota.
DR HOGENOM; CLU_071870_1_0_1; -.
DR InParanoid; P40576; -.
DR OMA; HMMMNQP; -.
DR BioCyc; YEAST:G3O-31443-MON; -.
DR PRO; PR:P40576; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40576; protein.
DR GO; GO:1990524; C:INA complex; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031304; C:intrinsic component of mitochondrial inner membrane; IDA:SGD.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR GO; GO:1990677; C:mitochondrial inner membrane assembly complex; IPI:ComplexPortal.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0033615; P:mitochondrial proton-transporting ATP synthase complex assembly; IDA:ComplexPortal.
PE 1: Evidence at protein level;
KW Chaperone; Coiled coil; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Transit peptide;
KW Transmembrane; Transmembrane helix.
FT TRANSIT 1..26
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 27..216
FT /note="Inner membrane assembly complex subunit 22"
FT /evidence="ECO:0000255"
FT /id="PRO_0000203007"
FT TOPO_DOM 27..43
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305|PubMed:24942160"
FT TRANSMEM 44..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..216
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305|PubMed:24942160"
FT COILED 64..93
FT /evidence="ECO:0000305"
SQ SEQUENCE 216 AA; 24597 MW; E63342B8DD5DDD79 CRC64;
MFMARQVLRN GLFLRSLAPI KITARTVASA NAGIKRKSRF DKTMIKPLLL VMIFGSILNA
VIAEKRNIID MERKYKLKLD KLKELIRRVH DNNGKVDFDA DDELKLVNLR LGIVGKNATG
MKEDETDIVV PKEESLEEIW QSIIDEAKKE VIEKTPDAGV KNKEGIVTDL NVLKDLEKSK
KEDEKVYLSG DVHMMMNQPG DLNEIAKEHD KIPKFL
