OXA1L_MOUSE
ID OXA1L_MOUSE Reviewed; 433 AA.
AC Q8BGA9; Q8BK01; Q8R091; Q9D8X7;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Mitochondrial inner membrane protein OXA1L;
DE AltName: Full=Oxidase assembly 1-like protein;
DE Short=OXA1-like protein;
DE Flags: Precursor;
GN Name=Oxa1l;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, Lung, and Pancreas;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Required for the insertion of integral membrane proteins into
CC the mitochondrial inner membrane. Essential for the activity and
CC assembly of cytochrome oxidase. Required for the correct biogenesis of
CC ATP synthase and complex I in mitochondria (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Monomer; predominantly monomeric at low salt concentrations.
CC Homooligomer; predominantly homooligomeric at high salt concentrations.
CC Homodimer. Homotetramer. Interacts with MRPL13, MRPL20, MRPL28, MRPL48,
CC MRPL49 and MRPL51. Associates preferentially as a dimer with the large
CC ribosomal subunit 39S of the mitochondrial ribosome (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
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; AK007567; BAB25113.1; -; mRNA.
DR EMBL; AK044817; BAC32104.1; -; mRNA.
DR EMBL; AK052432; BAC34985.1; -; mRNA.
DR EMBL; AK077624; BAC36908.1; -; mRNA.
DR EMBL; BC027191; AAH27191.1; -; mRNA.
DR CCDS; CCDS27086.1; -.
DR RefSeq; NP_081212.1; NM_026936.3.
DR AlphaFoldDB; Q8BGA9; -.
DR SMR; Q8BGA9; -.
DR BioGRID; 213221; 4.
DR STRING; 10090.ENSMUSP00000000985; -.
DR iPTMnet; Q8BGA9; -.
DR PhosphoSitePlus; Q8BGA9; -.
DR SwissPalm; Q8BGA9; -.
DR EPD; Q8BGA9; -.
DR jPOST; Q8BGA9; -.
DR MaxQB; Q8BGA9; -.
DR PaxDb; Q8BGA9; -.
DR PRIDE; Q8BGA9; -.
DR ProteomicsDB; 295493; -.
DR Antibodypedia; 192; 197 antibodies from 26 providers.
DR DNASU; 69089; -.
DR Ensembl; ENSMUST00000000985; ENSMUSP00000000985; ENSMUSG00000000959.
DR GeneID; 69089; -.
DR KEGG; mmu:69089; -.
DR UCSC; uc007tvu.1; mouse.
DR CTD; 5018; -.
DR MGI; MGI:1916339; Oxa1l.
DR VEuPathDB; HostDB:ENSMUSG00000000959; -.
DR eggNOG; KOG1239; Eukaryota.
DR GeneTree; ENSGT00530000063506; -.
DR HOGENOM; CLU_029282_3_1_1; -.
DR InParanoid; Q8BGA9; -.
DR OMA; KNAEMAH; -.
DR OrthoDB; 1314061at2759; -.
DR PhylomeDB; Q8BGA9; -.
DR TreeFam; TF354324; -.
DR Reactome; R-MMU-5389840; Mitochondrial translation elongation.
DR Reactome; R-MMU-5419276; Mitochondrial translation termination.
DR BioGRID-ORCS; 69089; 20 hits in 74 CRISPR screens.
DR ChiTaRS; Oxa1l; mouse.
DR PRO; PR:Q8BGA9; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q8BGA9; protein.
DR Bgee; ENSMUSG00000000959; Expressed in hindlimb stylopod muscle and 248 other tissues.
DR ExpressionAtlas; Q8BGA9; baseline and differential.
DR Genevisible; Q8BGA9; MM.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0032592; C:integral component of mitochondrial membrane; ISO:MGI.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0031966; C:mitochondrial membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0032977; F:membrane insertase activity; IBA:GO_Central.
DR GO; GO:0097177; F:mitochondrial ribosome binding; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0009060; P:aerobic respiration; ISO:MGI.
DR GO; GO:0033615; P:mitochondrial proton-transporting ATP synthase complex assembly; ISO:MGI.
DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; ISS:UniProtKB.
DR GO; GO:0032780; P:negative regulation of ATP-dependent activity; ISO:MGI.
DR GO; GO:0051354; P:negative regulation of oxidoreductase activity; ISO:MGI.
DR GO; GO:0051205; P:protein insertion into membrane; IBA:GO_Central.
DR GO; GO:0032979; P:protein insertion into mitochondrial inner membrane from matrix; IBA:GO_Central.
DR GO; GO:0051262; P:protein tetramerization; ISS:UniProtKB.
DR InterPro; IPR028055; Membr_insert_YidC/Oxa1_C.
DR InterPro; IPR001708; YidC/ALB3/OXA1/COX18.
DR PANTHER; PTHR12428; PTHR12428; 1.
DR Pfam; PF02096; 60KD_IMP; 1.
DR TIGRFAMs; TIGR03592; yidC_oxa1_cterm; 1.
PE 1: Evidence at protein level;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Phosphoprotein;
KW Reference proteome; Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..433
FT /note="Mitochondrial inner membrane protein OXA1L"
FT /id="PRO_0000020353"
FT TOPO_DOM 1..108
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..134
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 156..207
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 229..255
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 277..293
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 315..433
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT REGION 397..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 359
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15070"
FT MOD_RES 395
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15070"
FT MOD_RES 397
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15070"
FT CONFLICT 18
FT /note="P -> L (in Ref. 2; AAH27191)"
FT /evidence="ECO:0000305"
FT CONFLICT 42
FT /note="G -> S (in Ref. 2; AAH27191)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="C -> Y (in Ref. 2; AAH27191)"
FT /evidence="ECO:0000305"
FT CONFLICT 77
FT /note="I -> V (in Ref. 2; AAH27191)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="P -> L (in Ref. 2; AAH27191)"
FT /evidence="ECO:0000305"
FT CONFLICT 109..130
FT /note="Missing (in Ref. 2; AAH27191)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="Q -> H (in Ref. 1; BAB25113)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="G -> D (in Ref. 1; BAC36908)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 433 AA; 48220 MW; AF57459B86D2D627 CRC64;
MARNLVCGRW QLLRLLRPQR SYHSVAVSLR PLAAELLAAR RGNGRPPCAL LAVFTPRCIS
TSATLFAEAQ VQAPPVIPAT SIPAAVPEVA SGGAADVVQC ATEPSFTELG LGSYTPVGLI
QNLLEYIHVD LGLPWWGAIA TCTVLARCLV FPLIVKGQRE AAKIHNHMPE MQKFSARIRE
AKLAGDQAEF YKATIEMTRY QKKHDIKLLR PLILPLTQAP VFISFFIALR EMANLPVPSL
QTGGLWWFQD LTVSDPIYVL PLVVTATMWC VLELGAETGV QSNDLQFMRN IIRVMPLVVL
PVTIHFPSAV FMYWLSSNVF SLCQVACLRI PAVRTVLKIP QRVVHDPDKL PPREGFLKSF
KKGWKNAEIA QQLREREQRM QKHLDLAARG PLRQTFTHNP LLQHDPSHPP KAPNSNNSSI
KANAKKPWQD TLG
