INA17_YEAST
ID INA17_YEAST Reviewed; 182 AA.
AC Q02888; D6W3R7;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Inner membrane assembly complex subunit 17 {ECO:0000305|PubMed:24942160};
DE AltName: Full=Altered inheritance of mitochondria protein 43 {ECO:0000303|PubMed:19300474};
DE AltName: Full=Found in mitochondrial proteome protein 14 {ECO:0000303|PubMed:14576278};
DE AltName: Full=INA complex 17 kDa subunit {ECO:0000303|PubMed:24942160};
DE Flags: Precursor;
GN Name=INA17 {ECO:0000303|PubMed:24942160};
GN Synonyms=AIM43 {ECO:0000303|PubMed:19300474},
GN FMP14 {ECO:0000303|PubMed:14576278};
GN OrderedLocusNames=YPL099C {ECO:0000312|SGD:S000006020};
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=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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].
RC STRAIN=ATCC 76625 / YPH499;
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 [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=19300474; DOI=10.1371/journal.pgen.1000407;
RA Hess D.C., Myers C.L., Huttenhower C., Hibbs M.A., Hayes A.P., Paw J.,
RA Clore J.J., Mendoza R.M., Luis B.S., Nislow C., Giaever G., Costanzo M.,
RA Troyanskaya O.G., Caudy A.A.;
RT "Computationally driven, quantitative experiments discover genes required
RT for mitochondrial biogenesis.";
RL PLoS Genet. 5:E1000407-E1000407(2009).
RN [5]
RP FUNCTION, INTERACTION WITH INA22, 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 Q02888; P00830: ATP2; NbExp=2; IntAct=EBI-7668387, EBI-3242;
CC Q02888; P40576: INA22; NbExp=4; IntAct=EBI-7668387, EBI-25429;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:24942160}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Increases frequency of mitochondrial genome loss.
CC {ECO:0000269|PubMed:19300474}.
CC -!- SIMILARITY: Belongs to the INA17 family. {ECO:0000305}.
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DR EMBL; U43281; AAB68200.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11333.1; -; Genomic_DNA.
DR PIR; S61967; S61967.
DR RefSeq; NP_015226.1; NM_001183913.1.
DR AlphaFoldDB; Q02888; -.
DR SMR; Q02888; -.
DR BioGRID; 36081; 119.
DR ComplexPortal; CPX-3279; INAC inner membrane assembly complex.
DR IntAct; Q02888; 4.
DR MINT; Q02888; -.
DR STRING; 4932.YPL099C; -.
DR MaxQB; Q02888; -.
DR PaxDb; Q02888; -.
DR PRIDE; Q02888; -.
DR EnsemblFungi; YPL099C_mRNA; YPL099C; YPL099C.
DR GeneID; 856005; -.
DR KEGG; sce:YPL099C; -.
DR SGD; S000006020; INA17.
DR VEuPathDB; FungiDB:YPL099C; -.
DR eggNOG; ENOG502S3U1; Eukaryota.
DR HOGENOM; CLU_127263_0_0_1; -.
DR InParanoid; Q02888; -.
DR OMA; HYVWWKL; -.
DR BioCyc; YEAST:G3O-34002-MON; -.
DR PRO; PR:Q02888; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q02888; 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..45
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 46..182
FT /note="Inner membrane assembly complex subunit 17"
FT /evidence="ECO:0000255"
FT /id="PRO_0000238621"
FT TOPO_DOM 46..107
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305|PubMed:24942160"
FT TRANSMEM 108..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 128..182
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305|PubMed:24942160"
FT COILED 128..158
FT /evidence="ECO:0000255"
SQ SEQUENCE 182 AA; 21842 MW; 208F9FC141D31F4E CRC64;
MLKRRSNALI TLSRTKLFPI TTVAYYHRRL LNQQRRAVST SPKKEIKSLE DLANLDSLDG
VDTELIRDLI NEHTTKLNIK KELDMLKKFS QEEESGHEIP VKRFIRPLWM FILMGSSVYL
LLHFSWWKLE HEERESQLKK EVEILEHQLN ELIVQDKTHN TSRGKGSNES THMKPWYRRW
FW
