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 27-MAR-2024, entry version 59. 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; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade; OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; 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 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 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. {ECO:0000269|PubMed:16720701}. CC -!- FUNCTION: Inceptin is a proteolytic fragment produced by insect larvae CC that previously ingested the protein. This peptide mediate plant CC 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 {ECO:0000269|PubMed:16720701}. 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). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ATPase gamma chain family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; DQ312300; ABC42340.1; -; mRNA. DR AlphaFoldDB; Q2LGZ2; -. DR SMR; Q2LGZ2; -. DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell. DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW. DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro. DR Gene3D; 3.40.1380.10; -; 1. DR InterPro; IPR035968; ATP_synth_F1_ATPase_gsu. DR InterPro; IPR000131; ATP_synth_F1_gsu. DR PANTHER; PTHR11693; ATP SYNTHASE GAMMA CHAIN; 1. DR PANTHER; PTHR11693:SF41; ATP SYNTHASE GAMMA CHAIN 1, CHLOROPLASTIC; 1. DR Pfam; PF00231; ATP-synt; 1. DR SUPFAM; SSF52943; ATP synthase (F1-ATPase), gamma subunit; 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; Plastid; KW Thylakoid; Transport. FT CHAIN <1..>118 FT /note="ATP synthase subunit gamma, chloroplastic" FT /id="PRO_0000245320" FT PEPTIDE 29..39 FT /note="Inceptin" FT /id="PRO_0000245321" FT DISULFID 30..36 FT NON_TER 1 FT NON_TER 118 SQ SEQUENCE 118 AA; 13024 MW; 4BA1985F83DD541E CRC64; DPLYTKFVSL VKSDPVIHTL LPLSPKGEIC DINGVCVDAA EDEFFRLTTK EGKLTVERDV VRTKTTDYSP ILQFEQDPVQ ILDALLPLYL NSQILRALQE SLASELAARM SAMSNAAA //