ID   ATPK_HUMAN              Reviewed;          94 AA.
AC   P56134; C9J8H9; F8W7V3; O76079; Q6IBB3; Q96L83; Q9BTI8;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 202.
DE   RecName: Full=ATP synthase subunit f, mitochondrial {ECO:0000305};
DE   AltName: Full=ATP synthase membrane subunit f {ECO:0000305};
GN   Name=ATP5MF {ECO:0000312|HGNC:HGNC:848}; Synonyms=ATP5J2, ATP5JL;
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] (ISOFORM 1).
RC   TISSUE=Thymus;
RA   Lee H.C., Kang Y.J., Park D.S., Lee C.M., Cho W.K., Ahn H.J., Lee M.Y.,
RA   Hwang M.Y., Jin S.W., Sohn U.I.K.;
RT   "cDNA cloning, and chromosomal localization of a human F1F0-type ATPase
RT   subunit f.";
RL   Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Umbilical cord blood;
RX   PubMed=9653160; DOI=10.1073/pnas.95.14.8175;
RA   Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H.,
RA   He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H.,
RA   Wang Y.-X., Chen S.-J., Chen Z.;
RT   "Identification of genes expressed in human CD34(+) hematopoietic
RT   stem/progenitor cells by expressed sequence tags and efficient full-length
RT   cDNA cloning.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA   Guo J.H., Yu L., Dai F.Y., She X.Y.;
RT   "F1Fo-ATP synthase complex Fo membrane domain f subunit of Homo sapiens.";
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA   Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA   Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA   Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA   Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA   Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA   Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA   Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA   Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA   Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA   Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA   Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA   Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA   Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA   Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA   McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA   Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12690205; DOI=10.1126/science.1083423;
RA   Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA   Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA   Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA   Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA   Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA   Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA   Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA   Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA   Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA   Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA   Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA   Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA   Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA   Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA   Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA   Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA   Adams M.D., Tsui L.-C.;
RT   "Human chromosome 7: DNA sequence and biology.";
RL   Science 300:767-772(2003).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton 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   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Kidney;
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   [9]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [10]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [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).
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. Part of the complex
CC       F(0) domain. Minor subunit located with subunit a in the membrane.
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC       - and CF(0) - the membrane proton channel. CF(0) seems to have nine
CC       subunits: a, b, c, d, e, f, g, F6 and 8 (or A6L). Component of an ATP
CC       synthase complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5H, ATP5ME,
CC       ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C,
CC       ATP5PO, ATP5MG, ATP5MK and ATP5MJ (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane
CC       {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=P56134-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P56134-2; Sequence=VSP_000437;
CC       Name=3;
CC         IsoId=P56134-3; Sequence=VSP_046746;
CC       Name=4;
CC         IsoId=P56134-4; Sequence=VSP_000437, VSP_046746;
CC   -!- SIMILARITY: Belongs to the ATPase F chain family. {ECO:0000305}.
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DR   EMBL; AF088918; AAC34895.1; -; mRNA.
DR   EMBL; AF047436; AAC39887.1; -; mRNA.
DR   EMBL; AY046911; AAL06647.1; -; mRNA.
DR   EMBL; CR456891; CAG33172.1; -; mRNA.
DR   EMBL; CR542155; CAG46952.1; -; mRNA.
DR   EMBL; AC073063; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH236956; EAL23877.1; -; Genomic_DNA.
DR   EMBL; CH471091; EAW76661.1; -; Genomic_DNA.
DR   EMBL; BC003678; AAH03678.1; -; mRNA.
DR   CCDS; CCDS34692.1; -. [P56134-3]
DR   CCDS; CCDS47653.1; -. [P56134-4]
DR   CCDS; CCDS47654.1; -. [P56134-2]
DR   CCDS; CCDS5665.1; -. [P56134-1]
DR   RefSeq; NP_001003713.1; NM_001003713.2. [P56134-2]
DR   RefSeq; NP_001003714.1; NM_001003714.2. [P56134-3]
DR   RefSeq; NP_001034267.1; NM_001039178.2. [P56134-4]
DR   RefSeq; NP_004880.1; NM_004889.3. [P56134-1]
DR   PDB; 8H9F; EM; 2.69 A; R=2-94.
DR   PDB; 8H9J; EM; 3.26 A; R=2-94.
DR   PDB; 8H9M; EM; 3.00 A; R=2-94.
DR   PDB; 8H9Q; EM; 3.47 A; R=2-94.
DR   PDB; 8H9S; EM; 2.53 A; R=2-94.
DR   PDB; 8H9T; EM; 2.77 A; R=2-94.
DR   PDB; 8H9U; EM; 2.61 A; R=2-94.
DR   PDB; 8H9V; EM; 3.02 A; R=2-94.
DR   PDBsum; 8H9F; -.
DR   PDBsum; 8H9J; -.
DR   PDBsum; 8H9M; -.
DR   PDBsum; 8H9Q; -.
DR   PDBsum; 8H9S; -.
DR   PDBsum; 8H9T; -.
DR   PDBsum; 8H9U; -.
DR   PDBsum; 8H9V; -.
DR   AlphaFoldDB; P56134; -.
DR   EMDB; EMD-34565; -.
DR   EMDB; EMD-34569; -.
DR   EMDB; EMD-34573; -.
DR   EMDB; EMD-34577; -.
DR   EMDB; EMD-34580; -.
DR   EMDB; EMD-34581; -.
DR   EMDB; EMD-34582; -.
DR   EMDB; EMD-34583; -.
DR   SMR; P56134; -.
DR   BioGRID; 114923; 121.
DR   ComplexPortal; CPX-6151; Mitochondrial proton-transporting ATP synthase complex.
DR   CORUM; P56134; -.
DR   IntAct; P56134; 60.
DR   MINT; P56134; -.
DR   STRING; 9606.ENSP00000292475; -.
DR   TCDB; 3.A.2.1.15; the h+- or na+-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR   GlyGen; P56134; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P56134; -.
DR   PhosphoSitePlus; P56134; -.
DR   SwissPalm; P56134; -.
DR   BioMuta; ATP5J2; -.
DR   DMDM; 7404340; -.
DR   EPD; P56134; -.
DR   jPOST; P56134; -.
DR   MassIVE; P56134; -.
DR   MaxQB; P56134; -.
DR   PaxDb; 9606-ENSP00000292475; -.
DR   PeptideAtlas; P56134; -.
DR   PRIDE; P56134; -.
DR   ProteomicsDB; 30017; -.
DR   ProteomicsDB; 56886; -. [P56134-1]
DR   ProteomicsDB; 56887; -. [P56134-2]
DR   ProteomicsDB; 9047; -.
DR   Pumba; P56134; -.
DR   TopDownProteomics; P56134-1; -. [P56134-1]
DR   TopDownProteomics; P56134-2; -. [P56134-2]
DR   Antibodypedia; 56015; 130 antibodies from 19 providers.
DR   DNASU; 9551; -.
DR   Ensembl; ENST00000292475.8; ENSP00000292475.4; ENSG00000241468.8. [P56134-1]
DR   Ensembl; ENST00000359832.8; ENSP00000352890.4; ENSG00000241468.8. [P56134-3]
DR   Ensembl; ENST00000394186.3; ENSP00000377740.3; ENSG00000241468.8. [P56134-2]
DR   Ensembl; ENST00000414062.5; ENSP00000412149.1; ENSG00000241468.8. [P56134-4]
DR   Ensembl; ENST00000488775.5; ENSP00000418197.1; ENSG00000241468.8. [P56134-4]
DR   GeneID; 9551; -.
DR   KEGG; hsa:9551; -.
DR   MANE-Select; ENST00000292475.8; ENSP00000292475.4; NM_004889.5; NP_004880.1.
DR   UCSC; uc003uql.4; human. [P56134-1]
DR   AGR; HGNC:848; -.
DR   CTD; 9551; -.
DR   DisGeNET; 9551; -.
DR   GeneCards; ATP5MF; -.
DR   HGNC; HGNC:848; ATP5MF.
DR   HPA; ENSG00000241468; Low tissue specificity.
DR   MIM; 619792; gene.
DR   neXtProt; NX_P56134; -.
DR   OpenTargets; ENSG00000241468; -.
DR   PharmGKB; PA25138; -.
DR   VEuPathDB; HostDB:ENSG00000241468; -.
DR   eggNOG; KOG4092; Eukaryota.
DR   GeneTree; ENSGT00510000046986; -.
DR   HOGENOM; CLU_3227123_0_0_1; -.
DR   InParanoid; P56134; -.
DR   OMA; HKYVQPK; -.
DR   OrthoDB; 2872009at2759; -.
DR   PhylomeDB; P56134; -.
DR   TreeFam; TF342865; -.
DR   BioCyc; MetaCyc:HS08550-MONOMER; -.
DR   PathwayCommons; P56134; -.
DR   Reactome; R-HSA-163210; Formation of ATP by chemiosmotic coupling.
DR   Reactome; R-HSA-8949613; Cristae formation.
DR   SignaLink; P56134; -.
DR   BioGRID-ORCS; 9551; 449 hits in 1117 CRISPR screens.
DR   GeneWiki; ATP5J2; -.
DR   GenomeRNAi; 9551; -.
DR   Pharos; P56134; Tbio.
DR   PRO; PR:P56134; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; P56134; Protein.
DR   Bgee; ENSG00000241468; Expressed in apex of heart and 212 other cell types or tissues.
DR   ExpressionAtlas; P56134; baseline and differential.
DR   GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR   GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR   GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR   GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR   GO; GO:0015986; P:proton motive force-driven ATP synthesis; NAS:ComplexPortal.
DR   GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IDA:UniProtKB.
DR   GO; GO:1902600; P:proton transmembrane transport; NAS:UniProtKB.
DR   InterPro; IPR019344; F1F0-ATPsyn_F_prd.
DR   PANTHER; PTHR13080; ATP SYNTHASE F CHAIN, MITOCHONDRIAL-RELATED; 1.
DR   PANTHER; PTHR13080:SF16; ATP SYNTHASE SUBUNIT F, MITOCHONDRIAL; 1.
DR   Pfam; PF10206; WRW; 1.
DR   Genevisible; P56134; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; ATP synthesis; CF(0);
KW   Hydrogen ion transport; Ion transport; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Phosphoprotein; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:25944712"
FT   CHAIN           2..94
FT                   /note="ATP synthase subunit f, mitochondrial"
FT                   /id="PRO_0000194824"
FT   TRANSMEM        63..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:25944712"
FT   MOD_RES         3
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:D3ZAF6"
FT   MOD_RES         22
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P56135"
FT   VAR_SEQ         5..10
FT                   /note="Missing (in isoform 2 and isoform 4)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_000437"
FT   VAR_SEQ         47..86
FT                   /note="GYYRYYNKYINVKKGSISGITMVLACYVLFSYSFSYKHLK -> E (in
FT                   isoform 3 and isoform 4)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_046746"
FT   CONFLICT        24
FT                   /note="G -> L (in Ref. 8; AAH03678)"
FT                   /evidence="ECO:0000305"
FT   TURN            21..23
FT                   /evidence="ECO:0007829|PDB:8H9M"
FT   HELIX           28..32
FT                   /evidence="ECO:0007829|PDB:8H9M"
FT   HELIX           37..55
FT                   /evidence="ECO:0007829|PDB:8H9M"
FT   HELIX           64..85
FT                   /evidence="ECO:0007829|PDB:8H9M"
FT   HELIX           86..88
FT                   /evidence="ECO:0007829|PDB:8H9V"
SQ   SEQUENCE   94 AA;  10918 MW;  D5F0D94273DEF880 CRC64;
     MASVGECPAP VPVKDKKLLE VKLGELPSWI LMRDFSPSGI FGAFQRGYYR YYNKYINVKK
     GSISGITMVL ACYVLFSYSF SYKHLKHERL RKYH
//