OXA1L_HUMAN
ID OXA1L_HUMAN Reviewed; 435 AA.
AC Q15070; B4DPA2;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2003, sequence version 3.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Mitochondrial inner membrane protein OXA1L;
DE AltName: Full=Hsa;
DE AltName: Full=OXA1Hs;
DE AltName: Full=Oxidase assembly 1-like protein;
DE Short=OXA1-like protein;
DE Flags: Precursor;
GN Name=OXA1L;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
RC TISSUE=Cervix adenocarcinoma;
RX PubMed=7991568; DOI=10.1073/pnas.91.25.11978;
RA Bonnefoy N., Kermorgant M., Groudinsky O., Minet M., Slonimski P.P.,
RA Dujardin G.;
RT "Cloning of a human gene involved in cytochrome oxidase assembly by
RT functional complementation of an oxa1- mutation in Saccharomyces
RT cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:11978-11982(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9247084; DOI=10.1016/s0925-4439(97)00031-8;
RA Roetig A., Parfait B., Heidet L., Dujardin G., Rustin P., Munnich A.;
RT "Sequence and structure of the human OXA1L gene and its upstream
RT elements.";
RL Biochim. Biophys. Acta 1361:6-10(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 2-435 (ISOFORM 3), AND VARIANT ALA-44.
RC TISSUE=Fetal liver, and T-cell;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17936786; DOI=10.1016/j.jmb.2007.09.044;
RA Stiburek L., Fornuskova D., Wenchich L., Pejznochova M., Hansikova H.,
RA Zeman J.;
RT "Knockdown of human Oxa1l impairs the biogenesis of F1Fo-ATP synthase and
RT NADH:ubiquinone oxidoreductase.";
RL J. Mol. Biol. 374:506-516(2007).
RN [7]
RP INTERACTION WITH MRPL13; MRPL20; MRPL28; MRPL48; MRPL49 AND MRPL51,
RP HOMOOLIGOMERIZATION, SUBUNIT, AND ASSOCIATION WITH MITOCHONDRIAL RIBOSOMES.
RX PubMed=20601428; DOI=10.1074/jbc.m110.148262;
RA Haque M.E., Elmore K.B., Tripathy A., Koc H., Koc E.C., Spremulli L.L.;
RT "Properties of the C-terminal tail of human mitochondrial inner membrane
RT protein Oxa1L and its interactions with mammalian mitochondrial
RT ribosomes.";
RL J. Biol. Chem. 285:28353-28362(2010).
RN [8]
RP HOMOOLIGOMERIZATION, SUBUNIT, ASSOCIATION WITH MITOCHONDRIAL RIBOSOMES, AND
RP MUTAGENESIS OF ALA-337; ALA-372; THR-400 AND SER-426.
RX PubMed=20739282; DOI=10.1074/jbc.m110.163808;
RA Haque M.E., Spremulli L.L., Fecko C.J.;
RT "Identification of protein-protein and protein-ribosome interacting regions
RT of the C-terminal tail of human mitochondrial inner membrane protein
RT Oxa1L.";
RL J. Biol. Chem. 285:34991-34998(2010).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364; THR-400 AND THR-402, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
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.
CC {ECO:0000269|PubMed:17936786, ECO:0000269|PubMed:7991568}.
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.
CC {ECO:0000269|PubMed:20601428, ECO:0000269|PubMed:20739282}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:17936786}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:17936786}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q15070-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15070-2; Sequence=VSP_008942;
CC Name=3;
CC IsoId=Q15070-3; Sequence=VSP_008943, VSP_008944, VSP_008945;
CC -!- SIMILARITY: Belongs to the OXA1/ALB3/YidC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH01669.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA05127.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; X80695; CAA56712.1; -; mRNA.
DR EMBL; AJ001981; CAA05127.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BX248001; CAD62333.1; -; mRNA.
DR EMBL; BX248295; CAD62623.1; -; mRNA.
DR EMBL; AK298249; BAG60514.1; -; mRNA.
DR EMBL; BC001669; AAH01669.2; ALT_INIT; mRNA.
DR CCDS; CCDS9573.1; -. [Q15070-1]
DR PIR; I38079; I38079.
DR RefSeq; NP_005006.3; NM_005015.3.
DR PDB; 6ZM5; EM; 2.89 A; u=1-435.
DR PDBsum; 6ZM5; -.
DR AlphaFoldDB; Q15070; -.
DR SMR; Q15070; -.
DR BioGRID; 111058; 182.
DR IntAct; Q15070; 20.
DR MINT; Q15070; -.
DR STRING; 9606.ENSP00000483491; -.
DR TCDB; 2.A.9.1.2; the membrane protein insertase (yidc/alb3/oxa1) family.
DR iPTMnet; Q15070; -.
DR PhosphoSitePlus; Q15070; -.
DR SwissPalm; Q15070; -.
DR BioMuta; OXA1L; -.
DR DMDM; 38372882; -.
DR EPD; Q15070; -.
DR jPOST; Q15070; -.
DR MassIVE; Q15070; -.
DR MaxQB; Q15070; -.
DR PaxDb; Q15070; -.
DR PeptideAtlas; Q15070; -.
DR PRIDE; Q15070; -.
DR ProteomicsDB; 60423; -. [Q15070-1]
DR ProteomicsDB; 60424; -. [Q15070-2]
DR ProteomicsDB; 60425; -. [Q15070-3]
DR Antibodypedia; 192; 197 antibodies from 26 providers.
DR DNASU; 5018; -.
DR Ensembl; ENST00000358043.5; ENSP00000350740.5; ENSG00000155463.14.
DR GeneID; 5018; -.
DR KEGG; hsa:5018; -.
DR UCSC; uc001wgp.3; human. [Q15070-1]
DR CTD; 5018; -.
DR DisGeNET; 5018; -.
DR GeneCards; OXA1L; -.
DR HGNC; HGNC:8526; OXA1L.
DR HPA; ENSG00000155463; Low tissue specificity.
DR MalaCards; OXA1L; -.
DR MIM; 601066; gene.
DR neXtProt; NX_Q15070; -.
DR PharmGKB; PA32854; -.
DR VEuPathDB; HostDB:ENSG00000155463; -.
DR eggNOG; KOG1239; Eukaryota.
DR InParanoid; Q15070; -.
DR OrthoDB; 1314061at2759; -.
DR PhylomeDB; Q15070; -.
DR PathwayCommons; Q15070; -.
DR Reactome; R-HSA-5368286; Mitochondrial translation initiation.
DR Reactome; R-HSA-5389840; Mitochondrial translation elongation.
DR Reactome; R-HSA-5419276; Mitochondrial translation termination.
DR SignaLink; Q15070; -.
DR BioGRID-ORCS; 5018; 188 hits in 1091 CRISPR screens.
DR ChiTaRS; OXA1L; human.
DR GenomeRNAi; 5018; -.
DR Pharos; Q15070; Tbio.
DR PRO; PR:Q15070; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q15070; protein.
DR Bgee; ENSG00000155463; Expressed in hindlimb stylopod muscle and 202 other tissues.
DR ExpressionAtlas; Q15070; baseline and differential.
DR Genevisible; Q15070; HS.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0032592; C:integral component of mitochondrial membrane; IDA:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0032977; F:membrane insertase activity; IBA:GO_Central.
DR GO; GO:0097177; F:mitochondrial ribosome binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0009060; P:aerobic respiration; IMP:UniProtKB.
DR GO; GO:0033615; P:mitochondrial proton-transporting ATP synthase complex assembly; IMP:UniProtKB.
DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; IMP:UniProtKB.
DR GO; GO:0032780; P:negative regulation of ATP-dependent activity; IMP:UniProtKB.
DR GO; GO:0051354; P:negative regulation of oxidoreductase activity; IMP:UniProtKB.
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; IDA: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 3D-structure; Alternative splicing; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Phosphoprotein; Reference proteome;
KW Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..435
FT /note="Mitochondrial inner membrane protein OXA1L"
FT /id="PRO_0000020352"
FT TOPO_DOM 1..113
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 135..139
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161..212
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 234..260
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 282..299
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 300..320
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 321..435
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT REGION 400..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 364
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 400
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 402
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..21
FT /note="MAMGLMCGRRELLRLLQSGRR -> MRGTQ (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_008942"
FT VAR_SEQ 147..149
FT /note="CTV -> F (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_008943"
FT VAR_SEQ 224..265
FT /note="APIFISFFIALREMANLPVPSLQTGGLWWFQDLTVSDPIYIL -> VSKNIS
FT FLISSSTHEISSLCFMCPRSPKKQVVVDYTWLSVVG (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_008944"
FT VAR_SEQ 266..435
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_008945"
FT VARIANT 44
FT /note="V -> A (in dbSNP:rs8572)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_014932"
FT VARIANT 91
FT /note="V -> I (in dbSNP:rs17619)"
FT /id="VAR_014933"
FT MUTAGEN 337
FT /note="A->C: Increases weakly homooligomer formation in
FT presence or absence of magnesium."
FT /evidence="ECO:0000269|PubMed:20739282"
FT MUTAGEN 372
FT /note="A->C: Increases strongly homooligomer formation in
FT presence of magnesium, but weakly in absence of magnesium."
FT /evidence="ECO:0000269|PubMed:20739282"
FT MUTAGEN 400
FT /note="T->C: Increases homooligomer formation in presence
FT or absence of magnesium."
FT /evidence="ECO:0000269|PubMed:20739282"
FT MUTAGEN 426
FT /note="S->C: Increases weakly homooligomer formation in
FT presence of magnesium, but strongly in absence of
FT magnesium."
FT /evidence="ECO:0000269|PubMed:20739282"
SQ SEQUENCE 435 AA; 48548 MW; CE959F07BCC56041 CRC64;
MAMGLMCGRR ELLRLLQSGR RVHSVAGPSQ WLGKPLTTRL LFPVAPCCCR PHYLFLAASG
PRSLSTSAIS FAEVQVQAPP VVAATPSPTA VPEVASGETA DVVQTAAEQS FAELGLGSYT
PVGLIQNLLE FMHVDLGLPW WGAIAACTVF ARCLIFPLIV TGQREAARIH NHLPEIQKFS
SRIREAKLAG DHIEYYKASS EMALYQKKHG IKLYKPLILP VTQAPIFISF FIALREMANL
PVPSLQTGGL WWFQDLTVSD PIYILPLAVT ATMWAVLELG AETGVQSSDL QWMRNVIRMM
PLITLPITMH FPTAVFMYWL SSNLFSLVQV SCLRIPAVRT VLKIPQRVVH DLDKLPPREG
FLESFKKGWK NAEMTRQLRE REQRMRNQLE LAARGPLRQT FTHNPLLQPG KDNPPNIPSS
SSKPKSKYPW HDTLG
