ATP68_BOVIN
ID ATP68_BOVIN Reviewed; 60 AA.
AC P14790; Q3ZCB5;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=ATP synthase subunit ATP5MJ, mitochondrial {ECO:0000305};
DE AltName: Full=6.8 kDa mitochondrial proteolipid;
DE AltName: Full=6.8 kDa mitochondrial proteolipid protein;
DE Short=MLQ;
GN Name=ATP5MJ; Synonyms=ATP5MPL, MP68;
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 PROTEIN SEQUENCE, AND MASS SPECTROMETRY.
RC TISSUE=Heart;
RX PubMed=2298292; DOI=10.1016/0014-5793(90)80082-t;
RA Terzi E., Boyot P., van Dorsselaer A., Luu B., Trifilieff E.;
RT "Isolation and amino acid sequence of a novel 6.8-kDa mitochondrial
RT proteolipid from beef heart. Use of FAB-MS for molecular mass
RT determination.";
RL FEBS Lett. 260:122-126(1990).
RN [2]
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.
RN [3]
RP PROTEIN SEQUENCE OF 1-24, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17575325; DOI=10.1074/mcp.m700097-mcp200;
RA Meyer B., Wittig I., Trifilieff E., Karas M., Schaegger H.;
RT "Identification of two proteins associated with mammalian ATP synthase.";
RL Mol. Cell. Proteomics 6:1690-1699(2007).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE ATP SYNTHASE
RP COMPLEX.
RX PubMed=17570365; DOI=10.1016/j.febslet.2007.05.079;
RA Chen R., Runswick M.J., Carroll J., Fearnley I.M., Walker J.E.;
RT "Association of two proteolipids of unknown function with ATP synthase from
RT bovine heart mitochondria.";
RL FEBS Lett. 581:3145-3148(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE ATP SYNTHASE
RP COMPLEX.
RX PubMed=25851905; DOI=10.1074/jbc.m115.645283;
RA Lee J., Ding S., Walpole T.B., Holding A.N., Montgomery M.G.,
RA Fearnley I.M., Walker J.E.;
RT "Organization of Subunits in the Membrane Domain of the Bovine F-ATPase
RT Revealed by Covalent Cross-linking.";
RL J. Biol. Chem. 290:13308-13320(2015).
CC -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or
CC Complex V) produces ATP from ADP in the presence of a proton gradient
CC across the membrane which is generated by electron transport complexes
CC of the respiratory chain. F-type ATPases consist of two structural
CC domains, F(1) - containing the extramembraneous catalytic core and F(0)
CC - containing the membrane proton channel, linked together by a central
CC stalk and a peripheral stalk. During catalysis, ATP synthesis in the
CC catalytic domain of F(1) is coupled via a rotary mechanism of the
CC central stalk subunits to proton translocation. Minor subunit required
CC to maintain the ATP synthase population in the mitochondria.
CC {ECO:0000250|UniProtKB:P56378}.
CC -!- SUBUNIT: Component of an ATP synthase complex composed of ATP5PB,
CC ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-ATP8,
CC ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MK and ATP5MJ.
CC {ECO:0000269|PubMed:17570365, ECO:0000269|PubMed:25851905}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000250|UniProtKB:P56378}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Heart, brain and liver mitochondria.
CC -!- MASS SPECTROMETRY: Mass=6834.1; Method=FAB;
CC Evidence={ECO:0000269|PubMed:2298292};
CC -!- SIMILARITY: Belongs to the small mitochondrial proteolipid family.
CC {ECO:0000305}.
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DR EMBL; BC102582; AAI02583.1; -; mRNA.
DR PIR; A34138; A34138.
DR RefSeq; NP_001106786.1; NM_001113315.1.
DR PDB; 6ZBB; EM; 3.61 A; j=1-60.
DR PDB; 6ZIQ; EM; 4.33 A; j=1-60.
DR PDB; 6ZIT; EM; 3.49 A; j=1-60.
DR PDB; 6ZIU; EM; 6.02 A; j=1-60.
DR PDB; 6ZPO; EM; 4.00 A; j=1-60.
DR PDB; 6ZQM; EM; 3.29 A; j=1-60.
DR PDB; 6ZQN; EM; 4.00 A; j=1-60.
DR PDB; 7AJB; EM; 9.20 A; Aj/j=1-60.
DR PDB; 7AJC; EM; 11.90 A; Aj/j=1-60.
DR PDB; 7AJD; EM; 9.00 A; Aj/j=1-60.
DR PDB; 7AJE; EM; 9.40 A; Aj/j=1-60.
DR PDB; 7AJF; EM; 8.45 A; Aj/j=1-60.
DR PDB; 7AJG; EM; 10.70 A; Aj/j=1-60.
DR PDB; 7AJH; EM; 9.70 A; Aj/j=1-60.
DR PDB; 7AJI; EM; 11.40 A; Aj/j=1-60.
DR PDB; 7AJJ; EM; 13.10 A; Aj/j=1-60.
DR PDBsum; 6ZBB; -.
DR PDBsum; 6ZIQ; -.
DR PDBsum; 6ZIT; -.
DR PDBsum; 6ZIU; -.
DR PDBsum; 6ZPO; -.
DR PDBsum; 6ZQM; -.
DR PDBsum; 6ZQN; -.
DR PDBsum; 7AJB; -.
DR PDBsum; 7AJC; -.
DR PDBsum; 7AJD; -.
DR PDBsum; 7AJE; -.
DR PDBsum; 7AJF; -.
DR PDBsum; 7AJG; -.
DR PDBsum; 7AJH; -.
DR PDBsum; 7AJI; -.
DR PDBsum; 7AJJ; -.
DR AlphaFoldDB; P14790; -.
DR SMR; P14790; -.
DR IntAct; P14790; 1.
DR MINT; P14790; -.
DR STRING; 9913.ENSBTAP00000038273; -.
DR PaxDb; P14790; -.
DR PRIDE; P14790; -.
DR Ensembl; ENSBTAT00000038460; ENSBTAP00000038273; ENSBTAG00000026886.
DR GeneID; 767909; -.
DR KEGG; bta:767909; -.
DR CTD; 9556; -.
DR VEuPathDB; HostDB:ENSBTAG00000026886; -.
DR VGNC; VGNC:49542; ATP5MJ.
DR eggNOG; ENOG502SVSA; Eukaryota.
DR GeneTree; ENSGT00390000016760; -.
DR HOGENOM; CLU_198465_0_0_1; -.
DR InParanoid; P14790; -.
DR OMA; RSDISHF; -.
DR OrthoDB; 1625753at2759; -.
DR TreeFam; TF338412; -.
DR Proteomes; UP000009136; Chromosome 21.
DR Bgee; ENSBTAG00000026886; Expressed in tongue muscle and 105 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IDA:UniProtKB.
DR InterPro; IPR012574; ATP5MJ.
DR PANTHER; PTHR15233; PTHR15233; 1.
DR Pfam; PF08039; Mit_proteolip; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Membrane; Mitochondrion;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..60
FT /note="ATP synthase subunit ATP5MJ, mitochondrial"
FT /id="PRO_0000064392"
FT TRANSMEM 20..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT HELIX 3..9
FT /evidence="ECO:0007829|PDB:6ZIT"
FT TURN 10..13
FT /evidence="ECO:0007829|PDB:6ZIT"
FT HELIX 14..18
FT /evidence="ECO:0007829|PDB:6ZIT"
FT TURN 19..21
FT /evidence="ECO:0007829|PDB:6ZIT"
FT HELIX 22..45
FT /evidence="ECO:0007829|PDB:6ZIT"
SQ SEQUENCE 60 AA; 6834 MW; 0D8AF6566B0AFD12 CRC64;
MLQSLIKKVW IPMKPYYTQA YQEIWVGTGL MAYIVYKIRS ADKRSKALKA SSAAPAHGHH
