OXA1_YEAST
ID OXA1_YEAST Reviewed; 402 AA.
AC P39952; D3DM61;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Mitochondrial inner membrane protein OXA1 {ECO:0000305};
DE AltName: Full=Cytochrome oxidase biogenesis protein OXA1 {ECO:0000305};
DE AltName: Full=Oxidase assembly protein 1 {ECO:0000303|PubMed:8196054};
DE Flags: Precursor;
GN Name=OXA1 {ECO:0000303|PubMed:8196054};
GN Synonyms=PET1402 {ECO:0000303|PubMed:7816036};
GN OrderedLocusNames=YER154W {ECO:0000312|SGD:S000000956};
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].
RC STRAIN=ATCC 28383 / FL100 / VTT C-80102;
RX PubMed=8196054; DOI=10.1006/jmbi.1994.1363;
RA Bonnefoy N., Chalvet F., Hamel P., Slonimski P.P., Dujardin G.;
RT "OXA1, a Saccharomyces cerevisiae nuclear gene whose sequence is conserved
RT from prokaryotes to eukaryotes controls cytochrome oxidase biogenesis.";
RL J. Mol. Biol. 239:201-212(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7816036; DOI=10.1007/bf00290106;
RA Bauer M., Behrens M., Esser K., Michaelis G., Pratje E.;
RT "PET1402, a nuclear gene required for proteolytic processing of cytochrome
RT oxidase subunit 2 in yeast.";
RL Mol. Gen. Genet. 245:272-278(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP SUBCELLULAR LOCATION, TRANSIT PEPTIDE, AND TOPOLOGY.
RX PubMed=9171337; DOI=10.1093/emboj/16.9.2217;
RA Herrmann J.M., Neupert W., Stuart R.A.;
RT "Insertion into the mitochondrial inner membrane of a polytopic protein,
RT the nuclear-encoded Oxa1p.";
RL EMBO J. 16:2217-2226(1997).
RN [7]
RP FUNCTION.
RX PubMed=9482871; DOI=10.1073/pnas.95.5.2250;
RA Hell K., Herrmann J.M., Pratje E., Neupert W., Stuart R.A.;
RT "Oxa1p, an essential component of the N-tail protein export machinery in
RT mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:2250-2255(1998).
RN [8]
RP INTERACTION WITH MRP20.
RX PubMed=14657017; DOI=10.1093/emboj/cdg624;
RA Jia L., Dienhart M., Schramp M., McCauley M., Hell K., Stuart R.A.;
RT "Yeast Oxa1 interacts with mitochondrial ribosomes: the importance of the
RT C-terminal region of Oxa1.";
RL EMBO J. 22:6438-6447(2003).
RN [9]
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 [10]
RP REVIEW.
RX PubMed=12191770; DOI=10.1016/s0167-4889(02)00266-5;
RA Stuart R.A.;
RT "Insertion of proteins into the inner membrane of mitochondria: the role of
RT the Oxa1 complex.";
RL Biochim. Biophys. Acta 1592:79-87(2002).
RN [11]
RP FUNCTION, AND MUTAGENESIS OF TRP-128; TRP-129; GLY-213; PHE-229; LEU-240;
RP LEU-249; GLN-250; LEU-300 AND TYR-301.
RX PubMed=20025673; DOI=10.1111/j.1365-2958.2009.07001.x;
RA Mathieu L., Bourens M., Marsy S., Hlavacek O., Panozzo C., Dujardin G.;
RT "A mutational analysis reveals new functional interactions between domains
RT of the Oxa1 protein in Saccharomyces cerevisiae.";
RL Mol. Microbiol. 75:474-488(2010).
RN [12]
RP FUNCTION.
RX PubMed=22829595; DOI=10.1074/jbc.m112.387563;
RA Kruger V., Deckers M., Hildenbeutel M., van der Laan M., Hellmers M.,
RA Dreker C., Preuss M., Herrmann J.M., Rehling P., Wagner R., Meinecke M.;
RT "The mitochondrial oxidase assembly protein1 (Oxa1) insertase forms a
RT membrane pore in lipid bilayers.";
RL J. Biol. Chem. 287:33314-33326(2012).
RN [13]
RP FUNCTION, AND BINDING TO MITORIBOSOMES.
RX PubMed=22904327; DOI=10.1074/jbc.m112.382630;
RA Keil M., Bareth B., Woellhaf M.W., Peleh V., Prestele M., Rehling P.,
RA Herrmann J.M.;
RT "Oxa1-ribosome complexes coordinate the assembly of cytochrome C oxidase in
RT mitochondria.";
RL J. Biol. Chem. 287:34484-34493(2012).
RN [14]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=22846909; DOI=10.1016/j.jmb.2012.07.018;
RA Hildenbeutel M., Theis M., Geier M., Haferkamp I., Neuhaus H.E.,
RA Herrmann J.M., Ott M.;
RT "The membrane insertase Oxa1 is required for efficient import of carrier
RT proteins into mitochondria.";
RL J. Mol. Biol. 423:590-599(2012).
RN [15]
RP SUBCELLULAR LOCATION.
RX PubMed=22513091; DOI=10.1091/mbc.e11-06-0538;
RA Stoldt S., Wenzel D., Hildenbeutel M., Wurm C.A., Herrmann J.M., Jakobs S.;
RT "The inner-mitochondrial distribution of Oxa1 depends on the growth
RT conditions and on the availability of substrates.";
RL Mol. Biol. Cell 23:2292-2301(2012).
RN [16]
RP INTERACTION WITH MBA1.
RX PubMed=25609543; DOI=10.1038/ncomms7019;
RA Pfeffer S., Woellhaf M.W., Herrmann J.M., Forster F.;
RT "Organization of the mitochondrial translation machinery studied in situ by
RT cryoelectron tomography.";
RL Nat. Commun. 6:6019-6019(2015).
CC -!- FUNCTION: Mitochondrial inner membrane insertase that mediates the
CC insertion of both mitochondrion-encoded precursors and nuclear-encoded
CC proteins from the matrix into the inner membrane. Links mitoribosomes
CC with the inner membrane (PubMed:22904327). Forms pores capable of
CC accommodating translocating protein segments (PubMed:22829595).
CC Essential for the activity and assembly of cytochrome c oxidase
CC (PubMed:22904327). Plays a central role in the translocation and export
CC of the N-terminal part of the COX2 protein into the mitochondrial
CC intermembrane space. {ECO:0000269|PubMed:20025673,
CC ECO:0000269|PubMed:22829595, ECO:0000269|PubMed:22846909,
CC ECO:0000269|PubMed:22904327, ECO:0000269|PubMed:9482871}.
CC -!- SUBUNIT: Interacts with the large ribosome subunit of mitochondrial
CC ribosome (PubMed:14657017, PubMed:22904327). Interacts directly with
CC MRP20 (PubMed:14657017). Interacts with OXA1 (PubMed:25609543).
CC {ECO:0000269|PubMed:14657017, ECO:0000269|PubMed:22904327,
CC ECO:0000269|PubMed:25609543}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:22513091, ECO:0000269|PubMed:9171337}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:9171337}. Note=The availability of
CC nuclear- and mitochondrial-encoded substrates influences the
CC inner- membrane distribution. {ECO:0000269|PubMed:22513091}.
CC -!- DISRUPTION PHENOTYPE: Leads to reduced steady-state levels and
CC activities of the mitochondrial ATP/ADP carrier protein AAC2.
CC {ECO:0000269|PubMed:22846909}.
CC -!- MISCELLANEOUS: Present with 6550 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the OXA1/ALB3/YidC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X77558; CAA54675.1; -; Genomic_DNA.
DR EMBL; X74456; CAA52465.1; -; Genomic_DNA.
DR EMBL; U18917; AAB64681.1; -; Genomic_DNA.
DR EMBL; AY693132; AAT93151.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07815.1; -; Genomic_DNA.
DR PIR; S47329; S47329.
DR RefSeq; NP_011081.1; NM_001179044.1.
DR AlphaFoldDB; P39952; -.
DR BioGRID; 36904; 151.
DR DIP; DIP-3870N; -.
DR IntAct; P39952; 13.
DR MINT; P39952; -.
DR STRING; 4932.YER154W; -.
DR TCDB; 2.A.9.1.1; the membrane protein insertase (yidc/alb3/oxa1) family.
DR MaxQB; P39952; -.
DR PaxDb; P39952; -.
DR PRIDE; P39952; -.
DR EnsemblFungi; YER154W_mRNA; YER154W; YER154W.
DR GeneID; 856898; -.
DR KEGG; sce:YER154W; -.
DR SGD; S000000956; OXA1.
DR VEuPathDB; FungiDB:YER154W; -.
DR eggNOG; KOG1239; Eukaryota.
DR GeneTree; ENSGT00530000063506; -.
DR HOGENOM; CLU_029282_3_0_1; -.
DR InParanoid; P39952; -.
DR OMA; KNAEMAH; -.
DR BioCyc; YEAST:G3O-30315-MON; -.
DR PRO; PR:P39952; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P39952; protein.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0030061; C:mitochondrial crista; IDA:SGD.
DR GO; GO:0097002; C:mitochondrial inner boundary membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0032977; F:membrane insertase activity; IMP:SGD.
DR GO; GO:0097177; F:mitochondrial ribosome binding; IDA:SGD.
DR GO; GO:0033615; P:mitochondrial proton-transporting ATP synthase complex assembly; IMP:SGD.
DR GO; GO:0051205; P:protein insertion into membrane; IBA:GO_Central.
DR GO; GO:0045039; P:protein insertion into mitochondrial inner membrane; IMP:SGD.
DR GO; GO:0032979; P:protein insertion into mitochondrial inner membrane from matrix; IMP:SGD.
DR InterPro; IPR001708; YidC/ALB3/OXA1/COX18.
DR PANTHER; PTHR12428; PTHR12428; 1.
DR Pfam; PF02096; 60KD_IMP; 1.
PE 1: Evidence at protein level;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..42
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:9171337"
FT CHAIN 43..402
FT /note="Mitochondrial inner membrane protein OXA1"
FT /id="PRO_0000020362"
FT TOPO_DOM 43..118
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:9171337"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 140..199
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 221..239
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 261..275
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305"
FT TRANSMEM 276..292
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 293..297
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT TRANSMEM 298..316
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 317..402
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305"
FT REGION 366..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 128
FT /note="W->R: Leads to respiratory deficiency."
FT /evidence="ECO:0000269|PubMed:20025673"
FT MUTAGEN 129
FT /note="W->R: Leads to a defect in complex V assembly and
FT subsequent respiratory deficiency."
FT /evidence="ECO:0000269|PubMed:20025673"
FT MUTAGEN 213
FT /note="G->R: Leads to a defect in complex V assembly and
FT subsequent respiratory deficiency."
FT /evidence="ECO:0000269|PubMed:20025673"
FT MUTAGEN 229
FT /note="F->S: Leads to a defect in complexes IV and V
FT assembly, and subsequent respiratory deficiency."
FT /evidence="ECO:0000269|PubMed:20025673"
FT MUTAGEN 240
FT /note="L->S: Leads to a defect in complex IV assembly and
FT subsequent respiratory deficiency."
FT /evidence="ECO:0000269|PubMed:20025673"
FT MUTAGEN 249
FT /note="L->S: Leads to respiratory deficiency."
FT /evidence="ECO:0000269|PubMed:20025673"
FT MUTAGEN 250
FT /note="Q->R: Leads to respiratory deficiency."
FT /evidence="ECO:0000269|PubMed:20025673"
FT MUTAGEN 300
FT /note="L->P: Leads to a defect in complex V assembly and
FT subsequent respiratory deficiency."
FT /evidence="ECO:0000269|PubMed:20025673"
FT MUTAGEN 301
FT /note="Y->D: Leads to respiratory deficiency."
FT /evidence="ECO:0000269|PubMed:20025673"
FT CONFLICT 108
FT /note="W -> R (in Ref. 1; CAA54675)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 402 AA; 44816 MW; 108890B8F2EE67ED CRC64;
MFKLTSRLVT SRFAASSRLA TARTIVLPRP HPSWISFQAK RFNSTGPNAN DVSEIQTQLP
SIDELTSSAP SLSASTSDLI ANTTQTVGEL SSHIGYLNSI GLAQTWYWPS DIIQHVLEAV
HVYSGLPWWG TIAATTILIR CLMFPLYVKS SDTVARNSHI KPELDALNNK LMSTTDLQQG
QLVAMQRKKL LSSHGIKNRW LAAPMLQIPI ALGFFNALRH MANYPVDGFA NQGVAWFTDL
TQADPYLGLQ VITAAVFISF TRLGGETGAQ QFSSPMKRLF TILPIISIPA TMNLSSAVVL
YFAFNGAFSV LQTMILRNKW VRSKLKITEV AKPRTPIAGA SPTENMGIFQ SLKHNIQKAR
DQAERRQLMQ DNEKKLQESF KEKRQNSKIK IVHKSNFINN KK
