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ATP synthase subunit f, mitochondrial

 ATPK_HUMAN              Reviewed;          94 AA.
P56134; C9J8H9; F8W7V3; O76079; Q6IBB3; Q96L83; Q9BTI8;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
05-DEC-2018, entry version 170.
RecName: Full=ATP synthase subunit f, mitochondrial {ECO:0000305};
AltName: Full=ATP synthase membrane subunit f {ECO:0000305};
Name=ATP5MF {ECO:0000312|HGNC:HGNC:848}; Synonyms=ATP5J2, ATP5JL;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Thymus;
Lee H.C., Kang Y.J., Park D.S., Lee C.M., Cho W.K., Ahn H.J.,
Lee M.Y., Hwang M.Y., Jin S.W., Sohn U.I.K.;
"cDNA cloning, and chromosomal localization of a human F1F0-type
ATPase subunit f.";
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Umbilical cord blood;
PubMed=9653160; DOI=10.1073/pnas.95.14.8175;
Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H.,
He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H.,
Wang Y.-X., Chen S.-J., Chen Z.;
"Identification of genes expressed in human CD34(+) hematopoietic
stem/progenitor cells by expressed sequence tags and efficient full-
length cDNA cloning.";
Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Guo J.H., Yu L., Dai F.Y., She X.Y.;
"F1Fo-ATP synthase complex Fo membrane domain f subunit of Homo
sapiens.";
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12690205; DOI=10.1126/science.1083423;
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
Mural R.J., Adams M.D., Tsui L.-C.;
"Human chromosome 7: DNA sequence and biology.";
Science 300:767-772(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP
synthase or Complex V) produces ATP from ADP in the presence of a
proton gradient across the membrane which is generated by electron
transport complexes of the respiratory chain. F-type ATPases
consist of two structural domains, F(1) - containing the
extramembraneous catalytic core and F(0) - containing the membrane
proton channel, linked together by a central stalk and a
peripheral stalk. During catalysis, ATP synthesis in the catalytic
domain of F(1) is coupled via a rotary mechanism of the central
stalk subunits to proton translocation. Part of the complex F(0)
domain. Minor subunit located with subunit a in the membrane.
-!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic
core - and CF(0) - the membrane proton channel. CF(0) seems to
have nine subunits: a, b, c, d, e, f, g, F6 and 8 (or A6L).
Component of an ATP synthase complex composed of ATP5PB, ATP5MC1,
ATP5F1E, ATP5H, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A,
ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MD and MP68 (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane
{ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=P56134-1; Sequence=Displayed;
Name=2;
IsoId=P56134-2; Sequence=VSP_000437;
Note=No experimental confirmation available.;
Name=3;
IsoId=P56134-3; Sequence=VSP_046746;
Note=No experimental confirmation available. Gene prediction
based on EST data.;
Name=4;
IsoId=P56134-4; Sequence=VSP_000437, VSP_046746;
Note=No experimental confirmation available. Gene prediction
based on EST data.;
-!- SIMILARITY: Belongs to the ATPase F chain family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF088918; AAC34895.1; -; mRNA.
EMBL; AF047436; AAC39887.1; -; mRNA.
EMBL; AY046911; AAL06647.1; -; mRNA.
EMBL; CR456891; CAG33172.1; -; mRNA.
EMBL; CR542155; CAG46952.1; -; mRNA.
EMBL; AC073063; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH236956; EAL23877.1; -; Genomic_DNA.
EMBL; CH471091; EAW76661.1; -; Genomic_DNA.
EMBL; BC003678; AAH03678.1; -; mRNA.
CCDS; CCDS34692.1; -. [P56134-3]
CCDS; CCDS47653.1; -. [P56134-4]
CCDS; CCDS47654.1; -. [P56134-2]
CCDS; CCDS5665.1; -. [P56134-1]
RefSeq; NP_001003713.1; NM_001003713.2. [P56134-2]
RefSeq; NP_001003714.1; NM_001003714.2. [P56134-3]
RefSeq; NP_001034267.1; NM_001039178.2. [P56134-4]
RefSeq; NP_004880.1; NM_004889.3. [P56134-1]
UniGene; Hs.521056; -.
UniGene; Hs.656515; -.
ProteinModelPortal; P56134; -.
BioGrid; 114923; 49.
CORUM; P56134; -.
IntAct; P56134; 31.
STRING; 9606.ENSP00000292475; -.
iPTMnet; P56134; -.
PhosphoSitePlus; P56134; -.
SwissPalm; P56134; -.
BioMuta; ATP5J2; -.
DMDM; 7404340; -.
EPD; P56134; -.
PaxDb; P56134; -.
PeptideAtlas; P56134; -.
PRIDE; P56134; -.
ProteomicsDB; 56886; -.
ProteomicsDB; 56887; -. [P56134-2]
TopDownProteomics; P56134-1; -. [P56134-1]
TopDownProteomics; P56134-2; -. [P56134-2]
Ensembl; ENST00000292475; ENSP00000292475; ENSG00000241468. [P56134-1]
Ensembl; ENST00000359832; ENSP00000352890; ENSG00000241468. [P56134-3]
Ensembl; ENST00000394186; ENSP00000377740; ENSG00000241468. [P56134-2]
Ensembl; ENST00000414062; ENSP00000412149; ENSG00000241468. [P56134-4]
Ensembl; ENST00000488775; ENSP00000418197; ENSG00000241468. [P56134-4]
GeneID; 9551; -.
KEGG; hsa:9551; -.
UCSC; uc003uql.4; human. [P56134-1]
CTD; 9551; -.
DisGeNET; 9551; -.
EuPathDB; HostDB:ENSG00000241468.7; -.
GeneCards; ATP5MF; -.
HGNC; HGNC:848; ATP5MF.
HPA; HPA067267; -.
HPA; HPA070412; -.
neXtProt; NX_P56134; -.
OpenTargets; ENSG00000241468; -.
PharmGKB; PA25138; -.
eggNOG; KOG4092; Eukaryota.
eggNOG; ENOG4111PBN; LUCA.
GeneTree; ENSGT00510000046986; -.
HOGENOM; HOG000034215; -.
HOVERGEN; HBG002418; -.
InParanoid; P56134; -.
KO; K02130; -.
PhylomeDB; P56134; -.
TreeFam; TF342865; -.
Reactome; R-HSA-163210; Formation of ATP by chemiosmotic coupling.
Reactome; R-HSA-8949613; Cristae formation.
GeneWiki; ATP5J2; -.
GenomeRNAi; 9551; -.
PRO; PR:P56134; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000241468; Expressed in 234 organ(s), highest expression level in anterior cingulate cortex.
CleanEx; HS_ATP5J2; -.
ExpressionAtlas; P56134; baseline and differential.
Genevisible; P56134; HS.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IDA:UniProtKB.
GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IEA:Ensembl.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0005634; C:nucleus; HDA:UniProtKB.
GO; GO:0022857; F:transmembrane transporter activity; IC:UniProtKB.
GO; GO:0006754; P:ATP biosynthetic process; TAS:Reactome.
GO; GO:0042407; P:cristae formation; TAS:Reactome.
GO; GO:0042776; P:mitochondrial ATP synthesis coupled proton transport; IC:UniProtKB.
GO; GO:1902600; P:proton transmembrane transport; NAS:UniProtKB.
InterPro; IPR019344; F1F0-ATPsyn_F_prd.
PANTHER; PTHR13080; PTHR13080; 1.
Pfam; PF10206; WRW; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; ATP synthesis; CF(0);
Complete proteome; Hydrogen ion transport; Ion transport; Membrane;
Mitochondrion; Mitochondrion inner membrane; Phosphoprotein;
Reference proteome; Transmembrane; Transmembrane helix; Transport.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:25944712}.
CHAIN 2 94 ATP synthase subunit f, mitochondrial.
/FTId=PRO_0000194824.
TRANSMEM 63 82 Helical. {ECO:0000255}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:25944712}.
MOD_RES 3 3 Phosphoserine.
{ECO:0000250|UniProtKB:D3ZAF6}.
MOD_RES 22 22 N6-acetyllysine.
{ECO:0000250|UniProtKB:P56135}.
VAR_SEQ 5 10 Missing (in isoform 2 and isoform 4).
{ECO:0000303|Ref.3}.
/FTId=VSP_000437.
VAR_SEQ 47 86 GYYRYYNKYINVKKGSISGITMVLACYVLFSYSFSYKHLK
-> E (in isoform 3 and isoform 4).
{ECO:0000305}.
/FTId=VSP_046746.
CONFLICT 24 24 G -> L (in Ref. 8; AAH03678).
{ECO:0000305}.
SEQUENCE 94 AA; 10918 MW; D5F0D94273DEF880 CRC64;
MASVGECPAP VPVKDKKLLE VKLGELPSWI LMRDFSPSGI FGAFQRGYYR YYNKYINVKK
GSISGITMVL ACYVLFSYSF SYKHLKHERL RKYH


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