ATPG1_ARATH
ID ATPG1_ARATH Reviewed; 373 AA.
AC Q01908;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=ATP synthase gamma chain 1, chloroplastic;
DE AltName: Full=F-ATPase gamma subunit 1;
DE Flags: Precursor;
GN Name=ATPC1; OrderedLocusNames=At4g04640; ORFNames=T19J18.4;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1826905; DOI=10.1016/s0021-9258(20)89450-2;
RA Inohara N., Iwamoto A., Moriyama Y., Shimomura S., Maeda M., Futai M.;
RT "Two genes, atpC1 and atpC2, for the gamma subunit of Arabidopsis thaliana
RT chloroplast ATP synthase.";
RL J. Biol. Chem. 266:7333-7338(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [7]
RP INTERACTION WITH PAB.
RX PubMed=25775508; DOI=10.1073/pnas.1413392111;
RA Mao J., Chi W., Ouyang M., He B., Chen F., Zhang L.;
RT "PAB is an assembly chaperone that functions downstream of chaperonin 60 in
RT the assembly of chloroplast ATP synthase coupling factor 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:4152-4157(2015).
CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC across the membrane. The gamma chain is believed to be important in
CC regulating ATPase activity and the flow of protons through the CF(0)
CC complex.
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has four main
CC subunits: a, b, b' and c (By similarity). Interacts with PAB
CC (PubMed:25775508). {ECO:0000250|UniProtKB:P12113,
CC ECO:0000269|PubMed:25775508}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC -!- INDUCTION: By light.
CC -!- SIMILARITY: Belongs to the ATPase gamma chain family. {ECO:0000305}.
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DR EMBL; M61741; AAA32753.1; -; Genomic_DNA.
DR EMBL; AF149414; AAD48955.1; -; Genomic_DNA.
DR EMBL; AL161501; CAB80829.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82408.1; -; Genomic_DNA.
DR EMBL; AF428422; AAL16191.1; -; mRNA.
DR EMBL; AY065199; AAL38375.1; -; mRNA.
DR EMBL; AY081505; AAM10067.1; -; mRNA.
DR EMBL; AY088438; AAM65974.1; -; mRNA.
DR PIR; B39732; B39732.
DR RefSeq; NP_567265.1; NM_116702.2.
DR AlphaFoldDB; Q01908; -.
DR SMR; Q01908; -.
DR BioGRID; 11108; 9.
DR IntAct; Q01908; 2.
DR MINT; Q01908; -.
DR STRING; 3702.AT4G04640.1; -.
DR iPTMnet; Q01908; -.
DR MetOSite; Q01908; -.
DR PaxDb; Q01908; -.
DR PRIDE; Q01908; -.
DR ProteomicsDB; 241134; -.
DR EnsemblPlants; AT4G04640.1; AT4G04640.1; AT4G04640.
DR GeneID; 825797; -.
DR Gramene; AT4G04640.1; AT4G04640.1; AT4G04640.
DR KEGG; ath:AT4G04640; -.
DR Araport; AT4G04640; -.
DR TAIR; locus:2135054; AT4G04640.
DR eggNOG; KOG1531; Eukaryota.
DR HOGENOM; CLU_050669_0_0_1; -.
DR InParanoid; Q01908; -.
DR OMA; CGGYNNF; -.
DR OrthoDB; 841252at2759; -.
DR PhylomeDB; Q01908; -.
DR BioCyc; ARA:AT4G04640-MON; -.
DR PRO; PR:Q01908; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q01908; baseline and differential.
DR Genevisible; Q01908; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009544; C:chloroplast ATP synthase complex; TAS:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0000275; C:mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1); IBA:GO_Central.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0030234; F:enzyme regulator activity; TAS:TAIR.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0006754; P:ATP biosynthetic process; IMP:TAIR.
DR GO; GO:0009772; P:photosynthetic electron transport in photosystem II; IMP:TAIR.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
DR CDD; cd12151; F1-ATPase_gamma; 1.
DR HAMAP; MF_00815; ATP_synth_gamma_bact; 1.
DR InterPro; IPR035968; ATP_synth_F1_ATPase_gsu.
DR InterPro; IPR000131; ATP_synth_F1_gsu.
DR InterPro; IPR023632; ATP_synth_F1_gsu_CS.
DR PANTHER; PTHR11693; PTHR11693; 1.
DR Pfam; PF00231; ATP-synt; 1.
DR PRINTS; PR00126; ATPASEGAMMA.
DR SUPFAM; SSF52943; SSF52943; 1.
DR TIGRFAMs; TIGR01146; ATPsyn_F1gamma; 1.
DR PROSITE; PS00153; ATPASE_GAMMA; 1.
PE 1: Evidence at protein level;
KW ATP synthesis; CF(1); Chloroplast; Disulfide bond; Hydrogen ion transport;
KW Ion transport; Membrane; Phosphoprotein; Plastid; Reference proteome;
KW Thylakoid; Transit peptide; Transport.
FT TRANSIT 1..50
FT /note="Chloroplast"
FT /evidence="ECO:0000250"
FT CHAIN 51..373
FT /note="ATP synthase gamma chain 1, chloroplastic"
FT /id="PRO_0000002674"
FT ACT_SITE 139
FT /evidence="ECO:0000250"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT DISULFID 249..255
FT /evidence="ECO:0000250"
SQ SEQUENCE 373 AA; 40911 MW; 116FFC6F75BA96DE CRC64;
MACSNLTTMW VSSKPSLSAD SSSLSFRSVL KCPTNTSSPP SRASSVSPLQ ASLRELRDRI
DSVKNTQKIT EAMKLVAAAK VRRAQEAVVN GRPFSETLVE VLYNINEQLQ TDDVDVPLTK
VRPVKKVALV VVTGDRGLCG GFNNFIIKKA EARIKELKGL GLEYTVISVG KKGNSYFLRR
PYIPVDKYLE AGTLPTAKEA QAVADDVFSL FISEEVDKVE LLYTKFVSLV KSEPVIHTLL
PLSPKGEICD INGTCVDAAE DEFFRLTTKE GKLTVERETF RTPTADFSPI LQFEQDPVQI
LDALLPLYLN SQILRALQES LASELAARMS AMSSASDNAS DLKKSLSMVY NRKRQAKITG
EILEIVAGAN AQV
