ATPMK_BOVIN
ID ATPMK_BOVIN Reviewed; 58 AA.
AC Q3ZBI7;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=ATP synthase membrane subunit K, mitochondrial;
DE AltName: Full=ATP synthase membrane subunit DAPIT, mitochondrial {ECO:0000305};
DE AltName: Full=Diabetes-associated protein in insulin-sensitive tissues;
DE AltName: Full=Up-regulated during skeletal muscle growth protein 5 {ECO:0000305};
GN Name=ATP5MK {ECO:0000250|UniProtKB:Q96IX5}; Synonyms=ATPMD, DAPIT, USMG5;
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=Hereford; TISSUE=Rumen;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 2-20, 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 [3]
RP PROTEIN SEQUENCE OF 2-17, SUBCELLULAR LOCATION, CLEAVAGE OF INITIATOR
RP METHIONINE, AND MASS SPECTROMETRY.
RX PubMed=17060615; DOI=10.1073/pnas.0607719103;
RA Carroll J., Fearnley I.M., Walker J.E.;
RT "Definition of the mitochondrial proteome by measurement of molecular
RT masses of membrane proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:16170-16175(2006).
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. ATP5MK is a minor
CC subunit of the mitochondrial membrane ATP synthase required for
CC dimerization of the ATP synthase complex and as such regulates ATP
CC synthesis in the mitochondria. {ECO:0000250|UniProtKB:Q96IX5}.
CC -!- SUBUNIT: Component of the ATP synthase complex/complex V which is
CC composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF,
CC MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG,
CC ATP5MK and ATP5MJ (PubMed:17570365, PubMed:25851905). The ATP synthase
CC complex/complex V exists as a monomeric and a dimeric supercomplex that
CC helps shape mitochondrial cristae to optimize proton flow (By
CC similarity). {ECO:0000250|UniProtKB:Q96IX5,
CC ECO:0000269|PubMed:17570365, ECO:0000269|PubMed:25851905}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000269|PubMed:17060615}; Single-pass membrane protein
CC {ECO:0000269|PubMed:17060615}.
CC -!- MASS SPECTROMETRY: Mass=6303.5; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:17060615};
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DR EMBL; BC103275; AAI03276.1; -; mRNA.
DR RefSeq; NP_001106789.1; NM_001113318.1.
DR RefSeq; XP_010814877.1; XM_010816575.2.
DR RefSeq; XP_010822590.1; XM_010824288.2.
DR PDB; 6ZBB; EM; 3.61 A; k=2-58.
DR PDB; 6ZIQ; EM; 4.33 A; k=2-58.
DR PDB; 6ZIT; EM; 3.49 A; k=2-58.
DR PDB; 6ZPO; EM; 4.00 A; k=2-58.
DR PDB; 6ZQM; EM; 3.29 A; k=2-58.
DR PDB; 6ZQN; EM; 4.00 A; k=2-58.
DR PDB; 7AJB; EM; 9.20 A; Ak/k=2-58.
DR PDB; 7AJC; EM; 11.90 A; Ak/k=2-58.
DR PDB; 7AJD; EM; 9.00 A; Ak/k=2-58.
DR PDB; 7AJE; EM; 9.40 A; Ak/k=2-58.
DR PDB; 7AJF; EM; 8.45 A; Ak/k=2-58.
DR PDB; 7AJG; EM; 10.70 A; Ak/k=2-58.
DR PDB; 7AJH; EM; 9.70 A; Ak/k=2-58.
DR PDB; 7AJI; EM; 11.40 A; Ak/k=2-58.
DR PDB; 7AJJ; EM; 13.10 A; Ak/k=2-58.
DR PDBsum; 6ZBB; -.
DR PDBsum; 6ZIQ; -.
DR PDBsum; 6ZIT; -.
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; Q3ZBI7; -.
DR SMR; Q3ZBI7; -.
DR IntAct; Q3ZBI7; 1.
DR MINT; Q3ZBI7; -.
DR STRING; 9913.ENSBTAP00000012810; -.
DR PaxDb; Q3ZBI7; -.
DR PRIDE; Q3ZBI7; -.
DR Ensembl; ENSBTAT00000012810; ENSBTAP00000012810; ENSBTAG00000009713.
DR Ensembl; ENSBTAT00000042591; ENSBTAP00000040226; ENSBTAG00000030186.
DR Ensembl; ENSBTAT00000064624; ENSBTAP00000057922; ENSBTAG00000045783.
DR GeneID; 101907000; -.
DR GeneID; 767982; -.
DR KEGG; bta:101907000; -.
DR KEGG; bta:767982; -.
DR CTD; 84833; -.
DR VEuPathDB; HostDB:ENSBTAG00000009713; -.
DR VEuPathDB; HostDB:ENSBTAG00000030186; -.
DR VEuPathDB; HostDB:ENSBTAG00000045783; -.
DR VGNC; VGNC:54246; ATP5MK.
DR eggNOG; ENOG502S82X; Eukaryota.
DR GeneTree; ENSGT00390000015489; -.
DR HOGENOM; CLU_209345_1_0_1; -.
DR InParanoid; Q3ZBI7; -.
DR OMA; GIAKHFN; -.
DR OrthoDB; 1629213at2759; -.
DR TreeFam; TF324671; -.
DR Proteomes; UP000009136; Chromosome 16.
DR Proteomes; UP000009136; Chromosome 19.
DR Proteomes; UP000009136; Chromosome 26.
DR Bgee; ENSBTAG00000009713; Expressed in cardiac ventricle and 104 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; IPR009125; ATPMK.
DR PANTHER; PTHR34038; PTHR34038; 1.
DR Pfam; PF14960; ATP_synth_reg; 1.
DR PRINTS; PR01821; DAPIT.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Membrane;
KW Mitochondrion; Reference proteome; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:17060615,
FT ECO:0000269|PubMed:17575325"
FT CHAIN 2..58
FT /note="ATP synthase membrane subunit K, mitochondrial"
FT /id="PRO_0000231577"
FT TRANSMEM 23..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 16
FT /note="N6-acetyllysine; partial"
FT /evidence="ECO:0000250|UniProtKB:Q78IK2"
FT MOD_RES 17
FT /note="N6-acetyllysine; partial"
FT /evidence="ECO:0000250|UniProtKB:Q78IK2"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:6ZIT"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:6ZIT"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:6ZIT"
FT HELIX 24..45
FT /evidence="ECO:0007829|PDB:6ZIT"
SQ SEQUENCE 58 AA; 6435 MW; 1341E9CFE6C0B127 CRC64;
MAGPEADAQF HFTGIKKYFN SYTLTGRMNC VLATYGSIAL IVLYFKLRSK KTPAVKAT
