Full text data of ATP5J2
ATP5J2
(ATP5JL)
[Confidence: low (only semi-automatic identification from reviews)]
ATP synthase subunit f, mitochondrial
ATP synthase subunit f, mitochondrial
UniProt
P56134
ID ATPK_HUMAN Reviewed; 94 AA.
AC P56134; C9J8H9; F8W7V3; O76079; Q6IBB3; Q96L83; Q9BTI8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 123.
DE RecName: Full=ATP synthase subunit f, mitochondrial;
GN Name=ATP5J2; Synonyms=ATP5JL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Lee M.Y., Hwang M.Y., Jin S.W., Sohn U.I.K.;
RT "cDNA cloning, and chromosomal localization of a human F1F0-type
RT ATPase 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-
RT length 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
RT 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.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA 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.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., 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.,
RA Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
RA Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
RA Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
RA Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
RA Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
RA Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
RA Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
RA Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
RA Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
RA Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
RA Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
RA 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.,
RA Mural R.J., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
CC -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP
CC synthase or Complex V) produces ATP from ADP in the presence of a
CC proton gradient across the membrane which is generated by electron
CC transport complexes of the respiratory chain. F-type ATPases
CC consist of two structural domains, F(1) - containing the
CC extramembraneous catalytic core and F(0) - containing the membrane
CC proton channel, linked together by a central stalk and a
CC peripheral stalk. During catalysis, ATP synthesis in the catalytic
CC domain of F(1) is coupled via a rotary mechanism of the central
CC stalk subunits to proton translocation. Part of the complex F(0)
CC domain. Minor subunit located with subunit a in the membrane.
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic
CC core - and CF(0) - the membrane proton channel. CF(0) seems to
CC have nine subunits: a, b, c, d, e, f, g, F6 and 8 (or A6L).
CC Component of an ATP synthase complex composed of ATP5F1, ATP5G1,
CC ATP5E, ATP5H, ATP5I, ATP5J, ATP5J2, MT-ATP6, MT-ATP8, ATP5A1,
CC ATP5B, ATP5D, ATP5C1, ATP5O, ATP5L, USMG5 and MP68 (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane;
CC Single-pass membrane protein (Potential).
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 Note=No experimental confirmation available;
CC Name=3;
CC IsoId=P56134-3; Sequence=VSP_046746;
CC Note=No experimental confirmation available. Gene prediction
CC based on EST data;
CC Name=4;
CC IsoId=P56134-4; Sequence=VSP_000437, VSP_046746;
CC Note=No experimental confirmation available. Gene prediction
CC based on EST data;
CC -!- SIMILARITY: Belongs to the ATPase F chain family.
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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 RefSeq; NP_001003713.1; NM_001003713.2.
DR RefSeq; NP_001003714.1; NM_001003714.2.
DR RefSeq; NP_001034267.1; NM_001039178.2.
DR RefSeq; NP_004880.1; NM_004889.3.
DR UniGene; Hs.521056; -.
DR UniGene; Hs.656515; -.
DR ProteinModelPortal; P56134; -.
DR IntAct; P56134; 17.
DR MINT; MINT-1370314; -.
DR STRING; 9606.ENSP00000292475; -.
DR PhosphoSite; P56134; -.
DR DMDM; 7404340; -.
DR PaxDb; P56134; -.
DR PRIDE; P56134; -.
DR Ensembl; ENST00000292475; ENSP00000292475; ENSG00000241468.
DR Ensembl; ENST00000359832; ENSP00000352890; ENSG00000241468.
DR Ensembl; ENST00000394186; ENSP00000377740; ENSG00000241468.
DR Ensembl; ENST00000414062; ENSP00000412149; ENSG00000241468.
DR Ensembl; ENST00000488775; ENSP00000418197; ENSG00000241468.
DR GeneID; 9551; -.
DR KEGG; hsa:9551; -.
DR UCSC; uc003uqn.3; human.
DR CTD; 9551; -.
DR GeneCards; GC07M099046; -.
DR HGNC; HGNC:848; ATP5J2.
DR neXtProt; NX_P56134; -.
DR PharmGKB; PA25138; -.
DR eggNOG; NOG292892; -.
DR HOGENOM; HOG000034215; -.
DR HOVERGEN; HBG002418; -.
DR InParanoid; P56134; -.
DR KO; K02130; -.
DR OrthoDB; EOG73JKZ1; -.
DR PhylomeDB; P56134; -.
DR Reactome; REACT_111217; Metabolism.
DR GeneWiki; ATP5J2; -.
DR GenomeRNAi; 9551; -.
DR NextBio; 35811; -.
DR PRO; PR:P56134; -.
DR ArrayExpress; P56134; -.
DR Bgee; P56134; -.
DR CleanEx; HS_ATP5J2; -.
DR Genevestigator; P56134; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IDA:UniProtKB.
DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR GO; GO:0022857; F:transmembrane transporter activity; IC:UniProtKB.
DR GO; GO:0006200; P:ATP catabolic process; IDA:GOC.
DR GO; GO:0042776; P:mitochondrial ATP synthesis coupled proton transport; IC:UniProtKB.
DR GO; GO:0022904; P:respiratory electron transport chain; TAS:Reactome.
DR InterPro; IPR019344; F1F0-ATPsyn_F_prd.
DR PANTHER; PTHR13080; PTHR13080; 1.
DR Pfam; PF10206; WRW; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP synthesis; CF(0);
KW Complete proteome; Hydrogen ion transport; Ion transport; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 94 ATP synthase subunit f, mitochondrial.
FT /FTId=PRO_0000194824.
FT TRANSMEM 63 82 Helical; (Potential).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 22 22 N6-acetyllysine (By similarity).
FT VAR_SEQ 5 10 Missing (in isoform 2 and isoform 4).
FT /FTId=VSP_000437.
FT VAR_SEQ 47 86 GYYRYYNKYINVKKGSISGITMVLACYVLFSYSFSYKHLK
FT -> E (in isoform 3 and isoform 4).
FT /FTId=VSP_046746.
FT CONFLICT 24 24 G -> L (in Ref. 8; AAH03678).
SQ SEQUENCE 94 AA; 10918 MW; D5F0D94273DEF880 CRC64;
MASVGECPAP VPVKDKKLLE VKLGELPSWI LMRDFSPSGI FGAFQRGYYR YYNKYINVKK
GSISGITMVL ACYVLFSYSF SYKHLKHERL RKYH
//
ID ATPK_HUMAN Reviewed; 94 AA.
AC P56134; C9J8H9; F8W7V3; O76079; Q6IBB3; Q96L83; Q9BTI8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 123.
DE RecName: Full=ATP synthase subunit f, mitochondrial;
GN Name=ATP5J2; Synonyms=ATP5JL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Lee M.Y., Hwang M.Y., Jin S.W., Sohn U.I.K.;
RT "cDNA cloning, and chromosomal localization of a human F1F0-type
RT ATPase 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-
RT length 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
RT 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.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA 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.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., 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.,
RA Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
RA Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
RA Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
RA Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
RA Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
RA Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
RA Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
RA Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
RA Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
RA Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
RA Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
RA 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.,
RA Mural R.J., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
CC -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP
CC synthase or Complex V) produces ATP from ADP in the presence of a
CC proton gradient across the membrane which is generated by electron
CC transport complexes of the respiratory chain. F-type ATPases
CC consist of two structural domains, F(1) - containing the
CC extramembraneous catalytic core and F(0) - containing the membrane
CC proton channel, linked together by a central stalk and a
CC peripheral stalk. During catalysis, ATP synthesis in the catalytic
CC domain of F(1) is coupled via a rotary mechanism of the central
CC stalk subunits to proton translocation. Part of the complex F(0)
CC domain. Minor subunit located with subunit a in the membrane.
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic
CC core - and CF(0) - the membrane proton channel. CF(0) seems to
CC have nine subunits: a, b, c, d, e, f, g, F6 and 8 (or A6L).
CC Component of an ATP synthase complex composed of ATP5F1, ATP5G1,
CC ATP5E, ATP5H, ATP5I, ATP5J, ATP5J2, MT-ATP6, MT-ATP8, ATP5A1,
CC ATP5B, ATP5D, ATP5C1, ATP5O, ATP5L, USMG5 and MP68 (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane;
CC Single-pass membrane protein (Potential).
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 Note=No experimental confirmation available;
CC Name=3;
CC IsoId=P56134-3; Sequence=VSP_046746;
CC Note=No experimental confirmation available. Gene prediction
CC based on EST data;
CC Name=4;
CC IsoId=P56134-4; Sequence=VSP_000437, VSP_046746;
CC Note=No experimental confirmation available. Gene prediction
CC based on EST data;
CC -!- SIMILARITY: Belongs to the ATPase F chain family.
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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 RefSeq; NP_001003713.1; NM_001003713.2.
DR RefSeq; NP_001003714.1; NM_001003714.2.
DR RefSeq; NP_001034267.1; NM_001039178.2.
DR RefSeq; NP_004880.1; NM_004889.3.
DR UniGene; Hs.521056; -.
DR UniGene; Hs.656515; -.
DR ProteinModelPortal; P56134; -.
DR IntAct; P56134; 17.
DR MINT; MINT-1370314; -.
DR STRING; 9606.ENSP00000292475; -.
DR PhosphoSite; P56134; -.
DR DMDM; 7404340; -.
DR PaxDb; P56134; -.
DR PRIDE; P56134; -.
DR Ensembl; ENST00000292475; ENSP00000292475; ENSG00000241468.
DR Ensembl; ENST00000359832; ENSP00000352890; ENSG00000241468.
DR Ensembl; ENST00000394186; ENSP00000377740; ENSG00000241468.
DR Ensembl; ENST00000414062; ENSP00000412149; ENSG00000241468.
DR Ensembl; ENST00000488775; ENSP00000418197; ENSG00000241468.
DR GeneID; 9551; -.
DR KEGG; hsa:9551; -.
DR UCSC; uc003uqn.3; human.
DR CTD; 9551; -.
DR GeneCards; GC07M099046; -.
DR HGNC; HGNC:848; ATP5J2.
DR neXtProt; NX_P56134; -.
DR PharmGKB; PA25138; -.
DR eggNOG; NOG292892; -.
DR HOGENOM; HOG000034215; -.
DR HOVERGEN; HBG002418; -.
DR InParanoid; P56134; -.
DR KO; K02130; -.
DR OrthoDB; EOG73JKZ1; -.
DR PhylomeDB; P56134; -.
DR Reactome; REACT_111217; Metabolism.
DR GeneWiki; ATP5J2; -.
DR GenomeRNAi; 9551; -.
DR NextBio; 35811; -.
DR PRO; PR:P56134; -.
DR ArrayExpress; P56134; -.
DR Bgee; P56134; -.
DR CleanEx; HS_ATP5J2; -.
DR Genevestigator; P56134; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IDA:UniProtKB.
DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR GO; GO:0022857; F:transmembrane transporter activity; IC:UniProtKB.
DR GO; GO:0006200; P:ATP catabolic process; IDA:GOC.
DR GO; GO:0042776; P:mitochondrial ATP synthesis coupled proton transport; IC:UniProtKB.
DR GO; GO:0022904; P:respiratory electron transport chain; TAS:Reactome.
DR InterPro; IPR019344; F1F0-ATPsyn_F_prd.
DR PANTHER; PTHR13080; PTHR13080; 1.
DR Pfam; PF10206; WRW; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP synthesis; CF(0);
KW Complete proteome; Hydrogen ion transport; Ion transport; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 94 ATP synthase subunit f, mitochondrial.
FT /FTId=PRO_0000194824.
FT TRANSMEM 63 82 Helical; (Potential).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 22 22 N6-acetyllysine (By similarity).
FT VAR_SEQ 5 10 Missing (in isoform 2 and isoform 4).
FT /FTId=VSP_000437.
FT VAR_SEQ 47 86 GYYRYYNKYINVKKGSISGITMVLACYVLFSYSFSYKHLK
FT -> E (in isoform 3 and isoform 4).
FT /FTId=VSP_046746.
FT CONFLICT 24 24 G -> L (in Ref. 8; AAH03678).
SQ SEQUENCE 94 AA; 10918 MW; D5F0D94273DEF880 CRC64;
MASVGECPAP VPVKDKKLLE VKLGELPSWI LMRDFSPSGI FGAFQRGYYR YYNKYINVKK
GSISGITMVL ACYVLFSYSF SYKHLKHERL RKYH
//