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ATP synthase-coupling factor 6, mitochondrial (ATPase subunit F6)

 ATP5J_HUMAN             Reviewed;         108 AA.
P18859; J3KQ83;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
01-NOV-1990, sequence version 1.
20-JUN-2018, entry version 181.
RecName: Full=ATP synthase-coupling factor 6, mitochondrial;
Short=ATPase subunit F6;
Flags: Precursor;
Name=ATP5J; Synonyms=ATP5A, ATPM;
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).
PubMed=1825642; DOI=10.1016/0378-1119(91)90068-M;
Javed A.A., Ogata K., Sanadi D.R.;
"Human mitochondrial ATP synthase: cloning cDNA for the nuclear-
encoded precursor of coupling factor 6.";
Gene 97:307-310(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1830479; DOI=10.1016/0006-291X(91)90178-A;
Higuti T., Tsurumi C., Kawamura Y., Tsujita H., Osaka F.,
Yoshihara Y., Tani I., Tanaka K., Ichihara A.;
"Molecular cloning of cDNA for the import precursor of human coupling
factor 6 of H(+)-ATP synthase in mitochondria.";
Biochem. Biophys. Res. Commun. 178:793-799(1991).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Kidney;
PubMed=11230166; DOI=10.1101/gr.GR1547R;
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
Wambutt R., Korn B., Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and
analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
PubMed=17213182; DOI=10.1093/dnares/dsl016;
Kim J.M., Lee K.H., Jeon Y.J., Oh J.H., Jeong S.Y., Song I.S.,
Kim J.M., Lee D.S., Kim N.S.;
"Identification of genes related to Parkinson's disease using
expressed sequence tags.";
DNA Res. 13:275-286(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10830953; DOI=10.1038/35012518;
Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T.,
Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y.,
Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K.,
Polley A., Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D.,
Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W.,
Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S.,
Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E.,
Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P.,
Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H.,
Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E.,
Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F.,
Lehrach H., Reinhardt R., Yaspo M.-L.;
"The DNA sequence of human chromosome 21.";
Nature 405:311-319(2000).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Eye;
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).
[8]
PROTEIN SEQUENCE OF 33-43.
TISSUE=Liver;
PubMed=1286669; DOI=10.1002/elps.11501301201;
Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F.,
Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R.,
Appel R.D., Hughes G.J.;
"Human liver protein map: a reference database established by
microsequencing and gel comparison.";
Electrophoresis 13:992-1001(1992).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-41; LYS-46; LYS-99 AND
LYS-105, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[13]
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 and the peripheric stalk, which acts as a stator to hold
the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static
relative to the rotary elements. Also involved in the restoration
of oligomycin-sensitive ATPase activity to depleted F1-F0
complexes.
-!- 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 ATP5F1, ATP5MC1,
ATP5F1E, ATP5H, ATP5I, ATP5J, ATP5J2, MT-ATP6, MT-ATP8, ATP5F1A,
ATP5F1B, ATP5F1D, ATP5F1C, ATP5O, ATP5L, USMG5 and MP68 (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P18859-1; Sequence=Displayed;
Name=2;
IsoId=P18859-2; Sequence=VSP_046187;
-!- SIMILARITY: Belongs to the eukaryotic ATPase subunit F6 family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M37104; AAA51807.1; -; mRNA.
EMBL; M73031; AAA58630.1; -; mRNA.
EMBL; AL110183; CAB53667.1; -; mRNA.
EMBL; BT007244; AAP35908.1; -; mRNA.
EMBL; DT217787; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AP001694; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC001178; AAH01178.1; -; mRNA.
CCDS; CCDS13574.1; -. [P18859-1]
CCDS; CCDS46637.1; -. [P18859-2]
PIR; JT0563; JT0563.
RefSeq; NP_001003696.1; NM_001003696.1. [P18859-1]
RefSeq; NP_001003697.1; NM_001003697.1. [P18859-1]
RefSeq; NP_001003701.1; NM_001003701.1. [P18859-2]
RefSeq; NP_001003703.1; NM_001003703.1. [P18859-1]
RefSeq; NP_001307195.1; NM_001320266.1. [P18859-1]
RefSeq; NP_001307196.1; NM_001320267.1. [P18859-1]
RefSeq; NP_001676.2; NM_001685.4. [P18859-1]
UniGene; Hs.246310; -.
ProteinModelPortal; P18859; -.
SMR; P18859; -.
BioGrid; 107006; 49.
CORUM; P18859; -.
IntAct; P18859; 39.
MINT; P18859; -.
STRING; 9606.ENSP00000389649; -.
iPTMnet; P18859; -.
PhosphoSitePlus; P18859; -.
BioMuta; ATP5J; -.
DMDM; 114688; -.
SWISS-2DPAGE; P18859; -.
EPD; P18859; -.
PaxDb; P18859; -.
PeptideAtlas; P18859; -.
PRIDE; P18859; -.
ProteomicsDB; 53618; -.
TopDownProteomics; P18859-1; -. [P18859-1]
DNASU; 522; -.
Ensembl; ENST00000284971; ENSP00000284971; ENSG00000154723. [P18859-1]
Ensembl; ENST00000400087; ENSP00000382959; ENSG00000154723. [P18859-1]
Ensembl; ENST00000400090; ENSP00000382962; ENSG00000154723. [P18859-1]
Ensembl; ENST00000400093; ENSP00000382965; ENSG00000154723. [P18859-1]
Ensembl; ENST00000400094; ENSP00000382966; ENSG00000154723. [P18859-1]
Ensembl; ENST00000457143; ENSP00000389649; ENSG00000154723. [P18859-2]
GeneID; 522; -.
KEGG; hsa:522; -.
UCSC; uc002ylv.4; human. [P18859-1]
CTD; 522; -.
DisGeNET; 522; -.
EuPathDB; HostDB:ENSG00000154723.12; -.
GeneCards; ATP5PF; -.
HGNC; HGNC:847; ATP5J.
HPA; HPA031069; -.
MIM; 603152; gene.
neXtProt; NX_P18859; -.
OpenTargets; ENSG00000154723; -.
PharmGKB; PA25137; -.
eggNOG; KOG4634; Eukaryota.
eggNOG; ENOG41122G1; LUCA.
GeneTree; ENSGT00390000008902; -.
HOGENOM; HOG000261672; -.
HOVERGEN; HBG062261; -.
InParanoid; P18859; -.
KO; K02131; -.
OMA; YKQKSSG; -.
PhylomeDB; P18859; -.
TreeFam; TF318998; -.
Reactome; R-HSA-163210; Formation of ATP by chemiosmotic coupling.
Reactome; R-HSA-8949613; Cristae formation.
ChiTaRS; ATP5J; human.
GeneWiki; ATP5J; -.
GenomeRNAi; 522; -.
PRO; PR:P18859; -.
Proteomes; UP000005640; Chromosome 21.
Bgee; ENSG00000154723; -.
CleanEx; HS_ATP5J; -.
ExpressionAtlas; P18859; baseline and differential.
Genevisible; P18859; HS.
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:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
GO; GO:0022857; F:transmembrane transporter activity; IC:UniProtKB.
GO; GO:0005215; F:transporter activity; NAS:ProtInc.
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:0021762; P:substantia nigra development; HEP:UniProtKB.
InterPro; IPR008387; ATP_synth_f6_mt.
InterPro; IPR036204; ATP_synth_f6_sf_mt.
PANTHER; PTHR12441; PTHR12441; 1.
Pfam; PF05511; ATP-synt_F6; 1.
PIRSF; PIRSF002455; ATP_synthase_coupling_factor_6; 1.
SUPFAM; SSF111357; SSF111357; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; CF(0); Complete proteome;
Direct protein sequencing; Hydrogen ion transport; Ion transport;
Membrane; Mitochondrion; Mitochondrion inner membrane; Phosphoprotein;
Reference proteome; Transit peptide; Transport.
TRANSIT 1 32 Mitochondrion.
{ECO:0000269|PubMed:1286669}.
CHAIN 33 108 ATP synthase-coupling factor 6,
mitochondrial.
/FTId=PRO_0000002527.
MOD_RES 41 41 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 46 46 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 65 65 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 79 79 N6-acetyllysine.
{ECO:0000250|UniProtKB:P97450}.
MOD_RES 94 94 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P97450}.
MOD_RES 94 94 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P97450}.
MOD_RES 99 99 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 99 99 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P97450}.
MOD_RES 105 105 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
VAR_SEQ 1 1 M -> MHCDGGISM (in isoform 2).
{ECO:0000303|PubMed:17213182}.
/FTId=VSP_046187.
CONFLICT 68 68 Q -> H (in Ref. 2; AAA58630).
{ECO:0000305}.
SEQUENCE 108 AA; 12588 MW; EDC1A14F01A10F17 CRC64;
MILQRLFRFS SVIRSAVSVH LRRNIGVTAV AFNKELDPIQ KLFVDKIREY KSKRQTSGGP
VDASSEYQQE LERELFKLKQ MFGNADMNTF PTFKFEDPKF EVIEKPQA


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