OXA1L_BOVIN
ID OXA1L_BOVIN Reviewed; 441 AA.
AC Q3SYV3;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; BC103367; AAI03368.1; -; mRNA.
DR RefSeq; NP_001030412.1; NM_001035335.2.
DR AlphaFoldDB; Q3SYV3; -.
DR STRING; 9913.ENSBTAP00000019736; -.
DR PaxDb; Q3SYV3; -.
DR PRIDE; Q3SYV3; -.
DR Ensembl; ENSBTAT00000019736; ENSBTAP00000019736; ENSBTAG00000014820.
DR GeneID; 520335; -.
DR KEGG; bta:520335; -.
DR CTD; 5018; -.
DR VEuPathDB; HostDB:ENSBTAG00000014820; -.
DR VGNC; VGNC:32507; OXA1L.
DR eggNOG; KOG1239; Eukaryota.
DR GeneTree; ENSGT00530000063506; -.
DR HOGENOM; CLU_029282_3_1_1; -.
DR InParanoid; Q3SYV3; -.
DR OMA; KNAEMAH; -.
DR OrthoDB; 1314061at2759; -.
DR TreeFam; TF354324; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000014820; Expressed in corpus luteum and 106 other tissues.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0031966; C:mitochondrial membrane; ISS:UniProtKB.
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:0032981; P:mitochondrial respiratory chain complex I assembly; ISS: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; 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 2: Evidence at transcript 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 ?..441
FT /note="Mitochondrial inner membrane protein OXA1L"
FT /id="PRO_0000271431"
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..298
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 299..319
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 320..441
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT REGION 405..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 364
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15070"
FT MOD_RES 400
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15070"
SQ SEQUENCE 441 AA; 48987 MW; A4597CA05557CDCE CRC64;
MALALMCGRR QLLCLLRPQR QFHSVAGPCQ WPRKPLTAGL GFPADRCLGH PRYVLLMAPG
PRGLSTSAVS FGEAQVPAPP VIPATPPPTA VPEVASGEAA DVIQAAAEQS FAELGLGSYT
PVGLIQNLLE FMHVNLGLPW WGAIAACTVL ARCLVFPLIV KGQREAAKIH NHLPEIQKFS
ARIREAKLTG NHTEFYRASS EMTFYQKKHD IKLFRPLILP LTQAPIFISF FIALREMANL
PVPSLQTGGL WWFQDLTLSD PIYVLPLVVT ATMWGVLELG AETGMQSSDL QWMRNFIRLM
PLAVLPITIH FPTAVFMYWL SSNMFSLGQV ACLRIPAVRT VLKIPQRVVH DPDKLAPREG
FLKSFKQGWK NAEMAHQLQE RERRMQNHLE LAARGPLRQT FAHNPLLQHG KNDPPNTPNS
SSSSSSSNKA KSKQPWRDTL G
