Q15070 (OXA1L_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Mitochondrial inner membrane protein OXA1L

Alternative name(s):
Hsa
OXA1Hs
Oxidase assembly 1-like protein
Short name=OXA1-like protein

Gene names

Name:

OXA1L

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	435 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Required for the insertion of integral membrane proteins into the mitochondrial inner membrane. Essential for the activity and assembly of cytochrome oxidase. Required for the correct biogenesis of ATP synthase and complex I in mitochondria. Ref.1 Ref.6
Subunit structure	Monomer; predominantly monomeric at low salt concentrations. Homooligomer; predominantly homooligomeric at high salt concentrations. Homodimer. Homotetramer. Interacts with MRPL13, MRPL20, MRPL28, MRPL48, MRPL49 and MRPL51. Associates preferentially as a dimer with the large ribosomal subunit 39S of the mitochondrial ribosome. Ref.7 Ref.8
Subcellular location	Mitochondrion inner membrane; Multi-pass membrane protein Ref.6.
Sequence similarities	Belongs to the OXA1/ALB3/YidC family.
Sequence caution	The sequence AAH01669.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence CAA05127.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Transit peptide Transmembrane Transmembrane helix
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	aerobic respiration Inferred from mutant phenotype Ref.1. Source: UniProtKB mitochondrial proton-transporting ATP synthase complex assembly Inferred from mutant phenotype Ref.6. Source: UniProtKB mitochondrial respiratory chain complex I assembly Inferred from mutant phenotype Ref.6. Source: UniProtKB negative regulation of ATPase activity Inferred from mutant phenotype Ref.6. Source: UniProtKB negative regulation of oxidoreductase activity Inferred from mutant phenotype Ref.6. Source: UniProtKB protein insertion into membrane Inferred from electronic annotation. Source: InterPro protein tetramerization Inferred from direct assay Ref.7Ref.8. Source: UniProtKB
Cellular_component	integral to mitochondrial membrane Inferred from direct assay Ref.6. Source: UniProtKB mitochondrial respiratory chain Non-traceable author statement Ref.2. Source: UniProtKB protein complex Inferred from direct assay Ref.6. Source: UniProtKB
Molecular_function	mitochondrial ribosome binding Inferred from direct assay Ref.8. Source: UniProtKB protein homodimerization activity Inferred from direct assay Ref.7Ref.8. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q15070-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q15070-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: MAMGLMCGRRELLRLLQSGRR → MRGTQ

Note: No experimental confirmation available.

Isoform 3 (identifier: Q15070-3)

The sequence of this isoform differs from the canonical sequence as follows:
     147-149: CTV → F
     224-265: APIFISFFIA...LTVSDPIYIL → VSKNISFLIS...VDYTWLSVVG
     266-435: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Mitochondrion Potential
	Chain	? – 435		Mitochondrial inner membrane protein OXA1L		PRO_0000020352
Regions
	Topological domain	1 – 113	113	Mitochondrial intermembrane Potential
	Transmembrane	114 – 134	21	Helical; Potential
	Topological domain	135 – 139	5	Mitochondrial matrix Potential
	Transmembrane	140 – 160	21	Helical; Potential
	Topological domain	161 – 212	52	Mitochondrial intermembrane Potential
	Transmembrane	213 – 233	21	Helical; Potential
	Topological domain	234 – 260	27	Mitochondrial matrix Potential
	Transmembrane	261 – 281	21	Helical; Potential
	Topological domain	282 – 299	18	Mitochondrial intermembrane Potential
	Transmembrane	300 – 320	21	Helical; Potential
	Topological domain	321 – 435	115	Mitochondrial matrix Potential
Natural variations
	Alternative sequence	1 – 21	21	MAMGL…QSGRR → MRGTQ in isoform 2.		VSP_008942
	Alternative sequence	147 – 149	3	CTV → F in isoform 3.		VSP_008943
	Alternative sequence	224 – 265	42	APIFI…PIYIL → VSKNISFLISSSTHEISSLC FMCPRSPKKQVVVDYTWLSV VG in isoform 3.		VSP_008944
	Alternative sequence	266 – 435	170	Missing in isoform 3.		VSP_008945
	Natural variant	44	1	V → A. Ref.3 Corresponds to variant rs8572 [ dbSNP | Ensembl ].		VAR_014932
	Natural variant	91	1	V → I. Corresponds to variant rs17619 [ dbSNP | Ensembl ].		VAR_014933
Experimental info
	Mutagenesis	337	1	A → C: Increases weakly homooligomer formation in presence or absence of magnesium. Ref.8
	Mutagenesis	372	1	A → C: Increases strongly homooligomer formation in presence of magnesium, but weakly in absence of magnesium. Ref.8
	Mutagenesis	400	1	T → C: Increases homooligomer formation in presence or absence of magnesium. Ref.8
	Mutagenesis	426	1	S → C: Increases weakly homooligomer formation in presence of magnesium, but strongly in absence of magnesium. Ref.8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 14, 2003. Version 3. Checksum: CE959F07BCC56041	FASTA	435	48,548
	10 20 30 40 50 60 MAMGLMCGRR ELLRLLQSGR RVHSVAGPSQ WLGKPLTTRL LFPVAPCCCR PHYLFLAASG 70 80 90 100 110 120 PRSLSTSAIS FAEVQVQAPP VVAATPSPTA VPEVASGETA DVVQTAAEQS FAELGLGSYT 130 140 150 160 170 180 PVGLIQNLLE FMHVDLGLPW WGAIAACTVF ARCLIFPLIV TGQREAARIH NHLPEIQKFS 190 200 210 220 230 240 SRIREAKLAG DHIEYYKASS EMALYQKKHG IKLYKPLILP VTQAPIFISF FIALREMANL 250 260 270 280 290 300 PVPSLQTGGL WWFQDLTVSD PIYILPLAVT ATMWAVLELG AETGVQSSDL QWMRNVIRMM 310 320 330 340 350 360 PLITLPITMH FPTAVFMYWL SSNLFSLVQV SCLRIPAVRT VLKIPQRVVH DLDKLPPREG 370 380 390 400 410 420 FLESFKKGWK NAEMTRQLRE REQRMRNQLE LAARGPLRQT FTHNPLLQPG KDNPPNIPSS 430 SSKPKSKYPW HDTLG
	Isoform 2 [UniParc]. Checksum: 54AC7CD4BB1A241B	FASTA	419	46,691
	10 20 30 40 50 60 MRGTQVHSVA GPSQWLGKPL TTRLLFPVAP CCCRPHYLFL AASGPRSLST SAISFAEVQV 70 80 90 100 110 120 QAPPVVAATP SPTAVPEVAS GETADVVQTA AEQSFAELGL GSYTPVGLIQ NLLEFMHVDL 130 140 150 160 170 180 GLPWWGAIAA CTVFARCLIF PLIVTGQREA ARIHNHLPEI QKFSSRIREA KLAGDHIEYY 190 200 210 220 230 240 KASSEMALYQ KKHGIKLYKP LILPVTQAPI FISFFIALRE MANLPVPSLQ TGGLWWFQDL 250 260 270 280 290 300 TVSDPIYILP LAVTATMWAV LELGAETGVQ SSDLQWMRNV IRMMPLITLP ITMHFPTAVF 310 320 330 340 350 360 MYWLSSNLFS LVQVSCLRIP AVRTVLKIPQ RVVHDLDKLP PREGFLESFK KGWKNAEMTR 370 380 390 400 410 QLREREQRMR NQLELAARGP LRQTFTHNPL LQPGKDNPPN IPSSSSKPKS KYPWHDTLG
	Isoform 3 [UniParc]. Checksum: 84069C19904FB7F5	FASTA	263	28,803
	10 20 30 40 50 60 MAMGLMCGRR ELLRLLQSGR RVHSVAGPSQ WLGKPLTTRL LFPVAPCCCR PHYLFLAASG 70 80 90 100 110 120 PRSLSTSAIS FAEVQVQAPP VVAATPSPTA VPEVASGETA DVVQTAAEQS FAELGLGSYT 130 140 150 160 170 180 PVGLIQNLLE FMHVDLGLPW WGAIAAFFAR CLIFPLIVTG QREAARIHNH LPEIQKFSSR 190 200 210 220 230 240 IREAKLAGDH IEYYKASSEM ALYQKKHGIK LYKPLILPVT QVSKNISFLI SSSTHEISSL 250 260 CFMCPRSPKK QVVVDYTWLS VVG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of a human gene involved in cytochrome oxidase assembly by functional complementation of an oxa1- mutation in Saccharomyces cerevisiae." Bonnefoy N., Kermorgant M., Groudinsky O., Minet M., Slonimski P.P., Dujardin G. Proc. Natl. Acad. Sci. U.S.A. 91:11978-11982(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION. Tissue: Cervix adenocarcinoma.
[2]	"Sequence and structure of the human OXA1L gene and its upstream elements." Roetig A., Parfait B., Heidet L., Dujardin G., Rustin P., Munnich A. Biochim. Biophys. Acta 1361:6-10(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Full-length cDNA libraries and normalization." Li W.B., Gruber C., Jessee J., Polayes D. Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-435 (ISOFORM 3), VARIANT ALA-44. Tissue: Fetal liver and T-cell.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Kidney.
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Lung.
[6]	"Knockdown of human Oxa1l impairs the biogenesis of F1Fo-ATP synthase and NADH:ubiquinone oxidoreductase." Stiburek L., Fornuskova D., Wenchich L., Pejznochova M., Hansikova H., Zeman J. J. Mol. Biol. 374:506-516(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[7]	"Properties of the C-terminal tail of human mitochondrial inner membrane protein Oxa1L and its interactions with mammalian mitochondrial ribosomes." Haque M.E., Elmore K.B., Tripathy A., Koc H., Koc E.C., Spremulli L.L. J. Biol. Chem. 285:28353-28362(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MRPL13; MRPL20; MRPL28; MRPL48; MRPL49 AND MRPL51, HOMOOLIGOMERIZATION, SUBUNIT, ASSOCIATION WITH MITOCHONDRIAL RIBOSOMES.
[8]	"Identification of protein-protein and protein-ribosome interacting regions of the C-terminal tail of human mitochondrial inner membrane protein Oxa1L." Haque M.E., Spremulli L.L., Fecko C.J. J. Biol. Chem. 285:34991-34998(2010) [PubMed] [Europe PMC] [Abstract] Cited for: HOMOOLIGOMERIZATION, SUBUNIT, ASSOCIATION WITH MITOCHONDRIAL RIBOSOMES, MUTAGENESIS OF ALA-337; ALA-372; THR-400 AND SER-426.
[9]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X80695 mRNA. Translation: CAA56712.1. AJ001981 Genomic DNA. Translation: CAA05127.1. Sequence problems. BX248001 mRNA. Translation: CAD62333.1. BX248295 mRNA. Translation: CAD62623.1. AK298249 mRNA. Translation: BAG60514.1. BC001669 mRNA. Translation: AAH01669.2. Different initiation.
IPI	IPI00014301. IPI00395015. IPI00395016.
PIR	I38079.
RefSeq	NP_005006.3. NM_005015.3.
UniGene	Hs.151134.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q15070. 1 interaction.
STRING	9606.ENSP00000285848.
Protein family/group databases
TCDB	2.A.9.1.2. cytochrome oxidase biogenesis (Oxa1) family.
PTM databases
PhosphoSite	Q15070.
Polymorphism databases
DMDM	38372882.
Proteomic databases
PaxDb	Q15070.
PRIDE	Q15070.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000358043; ENSP00000350740; ENSG00000155463.
GeneID	5018.
KEGG	hsa:5018.
UCSC	uc001wgp.2. human.
Organism-specific databases
CTD	5018.
GeneCards	GC14P023235.
H-InvDB	HIX0011519.
HGNC	HGNC:8526. OXA1L.
HPA	HPA003531.
MIM	601066. gene.
neXtProt	NX_Q15070.
PharmGKB	PA32854.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0706.
HOVERGEN	HBG053388.
InParanoid	Q15070.
KO	K03217.
OrthoDB	EOG4QRH4J.
Gene expression databases
ArrayExpress	Q15070.
Bgee	Q15070.
CleanEx	HS_OXA1L.
Genevestigator	Q15070.
GermOnline	ENSG00000155463. Homo sapiens.
Family and domain databases
InterPro	IPR001708. Membrane_insert_OXA1/ALB3/YidC. [Graphical view]
PANTHER	PTHR12428. PTHR12428. 1 hit.
Pfam	PF02096. 60KD_IMP. 1 hit. [Graphical view]
TIGRFAMs	TIGR03592. yidC_oxa1_cterm. 1 hit.
ProtoNet	Search...
Other
ChiTaRS	OXA1L. human.
GenomeRNAi	5018.
NextBio	19320.
SOURCE	Search...

Entry information

Entry name

OXA1L_HUMAN

Accession

Primary (citable) accession number: Q15070
Secondary accession number(s): B4DPA2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2001
Last sequence update:	November 14, 2003
Last modified:	April 3, 2013
This is version 111 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.