ID   ATPG_VIGUN              Reviewed;         118 AA.
AC   Q2LGZ2;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 1.
DT   16-JUN-2009, entry version 18.
DE   RecName: Full=ATP synthase subunit gamma, chloroplastic;
DE   AltName: Full=F-ATPase gamma subunit;
DE   Contains:
DE     RecName: Full=Inceptin;
DE   Flags: Fragment;
OS   Vigna unguiculata (Cowpea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Phaseoleae;
OC   Vigna.
OX   NCBI_TaxID=3917;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 29-39, AND FUNCTION OF
RP   INCEPTIN.
RC   STRAIN=cv. California Blackeye no.5;
RX   PubMed=16720701; DOI=10.1073/pnas.0602328103;
RA   Schmelz E.A., Carroll M.J., Leclere S., Phipps S.M., Meredith J.,
RA   Chourey P.S., Alborn H.T., Teal P.E.;
RT   "Fragments of ATP synthase mediate plant perception of insect
RT   attack.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:8894-8899(2006).
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton
CC       gradient across the membrane. The gamma chain is believed to be
CC       important in regulating ATPase activity and the flow of protons
CC       through the CF(0) complex.
CC   -!- FUNCTION: Inceptin is a proteolytic fragment produced by insect
CC       larvae that previously ingested the protein. This peptide mediate
CC       plant perception of herbivory through the induction of volatile,
CC       phenylpropanoid and protease inhibitor defenses such as ethylene,
CC       jasmonic acid and salicylic acid for example.
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic
CC       core - and CF(0) - the membrane proton channel. CF(1) has five
CC       subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0)
CC       has three main subunits: a, b and c.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the ATPase gamma chain family.
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DR   EMBL; DQ312300; ABC42340.1; -; mRNA.
DR   BRENDA; 3.6.3.14; 2456.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045261; C:proton-transporting ATP synthase complex, c...; IEA:UniProtKB-KW.
DR   GO; GO:0046933; F:hydrogen ion transporting ATP synthase acti...; IEA:InterPro.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotati...; IEA:InterPro.
DR   GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro.
DR   InterPro; IPR000131; ATPase_F1-cplx_gsu.
DR   PANTHER; PTHR11693; ATPase_F1_gamma; 1.
DR   Pfam; PF00231; ATP-synt; 1.
PE   1: Evidence at protein level;
KW   ATP synthesis; CF(1); Chloroplast; Direct protein sequencing;
KW   Disulfide bond; Hydrogen ion transport; Ion transport; Membrane;
KW   Plastid; Thylakoid; Transport.
FT   CHAIN        <1   >118       ATP synthase subunit gamma,
FT                                chloroplastic.
FT                                /FTId=PRO_0000245320.
FT   PEPTIDE      29     39       Inceptin.
FT                                /FTId=PRO_0000245321.
FT   DISULFID     30     36
FT   NON_TER       1      1
FT   NON_TER     118    118
SQ   SEQUENCE   118 AA;  13024 MW;  4BA1985F83DD541E CRC64;
     DPLYTKFVSL VKSDPVIHTL LPLSPKGEIC DINGVCVDAA EDEFFRLTTK EGKLTVERDV
     VRTKTTDYSP ILQFEQDPVQ ILDALLPLYL NSQILRALQE SLASELAARM SAMSNAAA
//