ATPMK_HUMAN
ID ATPMK_HUMAN Reviewed; 58 AA.
AC Q96IX5; B2R4N2; D3DR92;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=ATP synthase membrane subunit K, mitochondrial {ECO:0000305};
DE AltName: Full=ATP synthase membrane subunit DAPIT, mitochondrial {ECO:0000305};
DE AltName: Full=Diabetes-associated protein in insulin-sensitive tissues;
DE AltName: Full=HCV F-transactivated protein 2;
DE AltName: Full=Up-regulated during skeletal muscle growth protein 5 {ECO:0000305};
GN Name=ATP5MK {ECO:0000312|HGNC:HGNC:30889};
GN Synonyms=ATP5MD, DAPIT, HCVFTP2, USMG5; ORFNames=PD04912;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION BY SBP1.
RX PubMed=16222733; DOI=10.3748/wjg.v11.i35.5438;
RA Ji D., Cheng J., Chen G.-F., Liu Y., Wang L., Guo J.;
RT "Study of transactivating effect of pre-S2 protein of hepatitis B virus and
RT cloning of genes transactivated by pre-S2 protein with suppression
RT subtractive hybridization.";
RL World J. Gastroenterol. 11:5438-5443(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skeletal muscle;
RA Frigimelica E., Lanfranchi G.;
RT "Study of 100 skeletal muscle full length mRNA.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Blood, Lung, and Skeletal muscle;
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21345788; DOI=10.1074/jbc.m110.198523;
RA Ohsakaya S., Fujikawa M., Hisabori T., Yoshida M.;
RT "Knockdown of DAPIT (diabetes-associated protein in insulin-sensitive
RT tissue) results in loss of ATP synthase in mitochondria.";
RL J. Biol. Chem. 286:20292-20296(2011).
RN [10]
RP CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [11]
RP INVOLVEMENT IN MC5DN6, FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=29917077; DOI=10.1093/hmg/ddy231;
RA Barca E., Ganetzky R.D., Potluri P., Juanola-Falgarona M., Gai X., Li D.,
RA Jalas C., Hirsch Y., Emmanuele V., Tadesse S., Ziosi M., Akman H.O.,
RA Chung W.K., Tanji K., McCormick E.M., Place E., Consugar M., Pierce E.A.,
RA Hakonarson H., Wallace D.C., Hirano M., Falk M.J.;
RT "USMG5 Ashkenazi Jewish founder mutation impairs mitochondrial complex V
RT dimerization and ATP synthesis.";
RL Hum. Mol. Genet. 27:3305-3312(2018).
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 (PubMed:29917077).
CC ATP5MK is a minor subunit of the mitochondrial membrane ATP synthase
CC required for dimerization of the ATP synthase complex and as such
CC regulates ATP synthesis in the mitochondria (PubMed:21345788,
CC PubMed:29917077). {ECO:0000269|PubMed:21345788,
CC ECO:0000269|PubMed:29917077, ECO:0000303|PubMed:29917077}.
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 (PubMed:29917077).
CC {ECO:0000250|UniProtKB:Q3ZBI7, ECO:0000269|PubMed:29917077}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000269|PubMed:21345788, ECO:0000269|PubMed:29917077}; Single-pass
CC membrane protein {ECO:0000255}.
CC -!- INDUCTION: Transactivated by SBP1. {ECO:0000269|PubMed:16222733}.
CC -!- DISEASE: Mitochondrial complex V deficiency, nuclear type 6 (MC5DN6)
CC [MIM:618683]: An autosomal recessive mitochondrial disorder
CC characterized by gross motor developmental delay manifesting in the
CC first years of life, and subsequent episodic developmental regression.
CC The episodes are associated with metabolic stress, including fever,
CC illness, and general anesthesia. Patients develop gait difficulties or
CC loss of ambulation, as well as other variable abnormalities, including
CC abnormal movements, hemiplegia, and persistent lethargy. Brain imaging
CC shows degenerative features in the basal ganglia and brainstem
CC consistent with a diagnosis of Leigh syndrome.
CC {ECO:0000269|PubMed:29917077}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
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DR EMBL; AY740522; AAU89079.1; -; mRNA.
DR EMBL; AJ272056; CAC81243.1; -; mRNA.
DR EMBL; AK311888; BAG34829.1; -; mRNA.
DR EMBL; AL591408; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471066; EAW49642.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49643.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49644.1; -; Genomic_DNA.
DR EMBL; BC007087; AAH07087.1; -; mRNA.
DR EMBL; BC072683; AAH72683.1; -; mRNA.
DR EMBL; BC091507; AAH91507.1; -; mRNA.
DR CCDS; CCDS7548.1; -.
DR RefSeq; NP_001193355.1; NM_001206426.1.
DR RefSeq; NP_001193356.1; NM_001206427.1.
DR RefSeq; NP_116136.1; NM_032747.3.
DR AlphaFoldDB; Q96IX5; -.
DR SMR; Q96IX5; -.
DR BioGRID; 124287; 95.
DR ComplexPortal; CPX-6151; Mitochondrial proton-transporting ATP synthase complex.
DR IntAct; Q96IX5; 67.
DR MINT; Q96IX5; -.
DR STRING; 9606.ENSP00000358840; -.
DR GlyGen; Q96IX5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96IX5; -.
DR PhosphoSitePlus; Q96IX5; -.
DR SwissPalm; Q96IX5; -.
DR BioMuta; USMG5; -.
DR EPD; Q96IX5; -.
DR jPOST; Q96IX5; -.
DR MassIVE; Q96IX5; -.
DR MaxQB; Q96IX5; -.
DR PaxDb; Q96IX5; -.
DR PeptideAtlas; Q96IX5; -.
DR PRIDE; Q96IX5; -.
DR ProteomicsDB; 76865; -.
DR TopDownProteomics; Q96IX5; -.
DR Antibodypedia; 46057; 77 antibodies from 16 providers.
DR DNASU; 84833; -.
DR Ensembl; ENST00000309579.7; ENSP00000311245.3; ENSG00000173915.16.
DR Ensembl; ENST00000337003.4; ENSP00000337705.4; ENSG00000173915.16.
DR Ensembl; ENST00000369811.5; ENSP00000358826.1; ENSG00000173915.16.
DR Ensembl; ENST00000369815.6; ENSP00000358830.1; ENSG00000173915.16.
DR Ensembl; ENST00000369825.6; ENSP00000358840.1; ENSG00000173915.16.
DR GeneID; 84833; -.
DR KEGG; hsa:84833; -.
DR MANE-Select; ENST00000369815.6; ENSP00000358830.1; NM_001206427.2; NP_001193356.1.
DR UCSC; uc001kww.4; human.
DR CTD; 84833; -.
DR DisGeNET; 84833; -.
DR GeneCards; ATP5MK; -.
DR HGNC; HGNC:30889; ATP5MK.
DR HPA; ENSG00000173915; Low tissue specificity.
DR MalaCards; ATP5MK; -.
DR MIM; 615204; gene.
DR MIM; 618683; phenotype.
DR neXtProt; NX_Q96IX5; -.
DR OpenTargets; ENSG00000173915; -.
DR Orphanet; 254913; Isolated ATP synthase deficiency.
DR PharmGKB; PA134968209; -.
DR VEuPathDB; HostDB:ENSG00000173915; -.
DR eggNOG; ENOG502S82X; Eukaryota.
DR GeneTree; ENSGT00390000015489; -.
DR HOGENOM; CLU_209345_1_0_1; -.
DR InParanoid; Q96IX5; -.
DR OMA; GIAKHFN; -.
DR OrthoDB; 1629213at2759; -.
DR PhylomeDB; Q96IX5; -.
DR TreeFam; TF324671; -.
DR PathwayCommons; Q96IX5; -.
DR SignaLink; Q96IX5; -.
DR BioGRID-ORCS; 84833; 17 hits in 936 CRISPR screens.
DR ChiTaRS; USMG5; human.
DR GenomeRNAi; 84833; -.
DR Pharos; Q96IX5; Tbio.
DR PRO; PR:Q96IX5; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q96IX5; protein.
DR Bgee; ENSG00000173915; Expressed in quadriceps femoris and 102 other tissues.
DR Genevisible; Q96IX5; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IC:ComplexPortal.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IMP:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IC:ComplexPortal.
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; Primary mitochondrial disease;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:25944712"
FT CHAIN 2..58
FT /note="ATP synthase membrane subunit K, mitochondrial"
FT /id="PRO_0000231578"
FT TRANSMEM 23..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 16
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q78IK2"
FT MOD_RES 17
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q78IK2"
SQ SEQUENCE 58 AA; 6458 MW; 3BFC4C9E2920B126 CRC64;
MAGPESDAQY QFTGIKKYFN SYTLTGRMNC VLATYGSIAL IVLYFKLRSK KTPAVKAT
