ATPMK_MOUSE
ID ATPMK_MOUSE Reviewed; 58 AA.
AC Q78IK2; Q9ER48;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 135.
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};
GN Synonyms=Atp5md {ECO:0000312|MGI:MGI:1891435}, Dapit, Usmg5;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/10; TISSUE=Skeletal muscle;
RA Sadusky T.J., Kemp T.J.;
RT "Isolation and characterisation of genes expressed in response to active
RT stretch of skeletal muscle.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-16 AND LYS-17, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
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 (By similarity). The ATP synthase complex/complex V
CC exists as a monomeric and a dimeric supercomplex that helps shape
CC mitochondrial cristae to optimize proton flow (By similarity).
CC {ECO:0000250|UniProtKB:Q3ZBI7, ECO:0000250|UniProtKB:Q96IX5}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000250|UniProtKB:Q96IX5}; Single-pass membrane protein
CC {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ290947; CAC03620.1; -; mRNA.
DR EMBL; BC087919; AAH87919.1; -; mRNA.
DR CCDS; CCDS38014.1; -.
DR RefSeq; NP_075700.2; NM_023211.4.
DR AlphaFoldDB; Q78IK2; -.
DR SMR; Q78IK2; -.
DR BioGRID; 211501; 28.
DR IntAct; Q78IK2; 5.
DR STRING; 10090.ENSMUSP00000093713; -.
DR iPTMnet; Q78IK2; -.
DR PhosphoSitePlus; Q78IK2; -.
DR SwissPalm; Q78IK2; -.
DR EPD; Q78IK2; -.
DR jPOST; Q78IK2; -.
DR MaxQB; Q78IK2; -.
DR PaxDb; Q78IK2; -.
DR PeptideAtlas; Q78IK2; -.
DR PRIDE; Q78IK2; -.
DR ProteomicsDB; 300202; -.
DR TopDownProteomics; Q78IK2; -.
DR Antibodypedia; 46057; 77 antibodies from 16 providers.
DR Ensembl; ENSMUST00000096014; ENSMUSP00000093713; ENSMUSG00000071528.
DR Ensembl; ENSMUST00000235771; ENSMUSP00000158561; ENSMUSG00000071528.
DR Ensembl; ENSMUST00000236170; ENSMUSP00000158514; ENSMUSG00000071528.
DR Ensembl; ENSMUST00000237720; ENSMUSP00000157712; ENSMUSG00000071528.
DR GeneID; 66477; -.
DR KEGG; mmu:66477; -.
DR UCSC; uc008huo.1; mouse.
DR CTD; 66477; -.
DR MGI; MGI:1891435; Atp5md.
DR VEuPathDB; HostDB:ENSMUSG00000071528; -.
DR eggNOG; ENOG502S82X; Eukaryota.
DR GeneTree; ENSGT00390000015489; -.
DR HOGENOM; CLU_209345_1_0_1; -.
DR InParanoid; Q78IK2; -.
DR OMA; GIAKHFN; -.
DR OrthoDB; 1629213at2759; -.
DR PhylomeDB; Q78IK2; -.
DR TreeFam; TF324671; -.
DR BioGRID-ORCS; 66477; 4 hits in 39 CRISPR screens.
DR ChiTaRS; Atp5md; mouse.
DR PRO; PR:Q78IK2; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q78IK2; protein.
DR Bgee; ENSMUSG00000071528; Expressed in right kidney and 247 other tissues.
DR Genevisible; Q78IK2; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; 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 Acetylation; Membrane; Mitochondrion; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..58
FT /note="ATP synthase membrane subunit K, mitochondrial"
FT /id="PRO_0000231579"
FT TRANSMEM 23..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 16
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 17
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT CONFLICT 5
FT /note="E -> K (in Ref. 1; CAC03620)"
FT /evidence="ECO:0000305"
FT CONFLICT 27
FT /note="R -> K (in Ref. 1; CAC03620)"
FT /evidence="ECO:0000305"
FT CONFLICT 55
FT /note="V -> A (in Ref. 1; CAC03620)"
FT /evidence="ECO:0000305"
FT CONFLICT 58
FT /note="T -> TMDFEMSDLTC (in Ref. 1; CAC03620)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 58 AA; 6382 MW; 7CE34D192253564D CRC64;
MAGAESDGQF QFTGIKKYFN SYTLTGRMNC VLATYGGIAL LVLYFKLRPK KTPAVKAT
