ID A0A067E4V9_CITSI Unreviewed; 130 AA.
AC A0A067E4V9;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=V-type proton ATPase subunit F {ECO:0000256|PIRNR:PIRNR015945};
GN ORFNames=CISIN_1g037034mg {ECO:0000313|EMBL:KDO48920.1};
OS Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX NCBI_TaxID=2711 {ECO:0000313|EMBL:KDO48920.1, ECO:0000313|Proteomes:UP000027120};
RN [1] {ECO:0000313|EMBL:KDO48920.1, ECO:0000313|Proteomes:UP000027120}
RP NUCLEOTIDE SEQUENCE.
RG International Citrus Genome Consortium;
RA Gmitter F., Chen C., Farmerie W., Harkins T., Desany B., Mohiuddin M.,
RA Kodira C., Borodovsky M., Lomsadze A., Burns P., Jenkins J., Prochnik S.,
RA Shu S., Chapman J., Pitluck S., Schmutz J., Rokhsar D.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007829|PDB:7UW9, ECO:0007829|PDB:7UWA}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.90 ANGSTROMS).
RX PubMed=36041457; DOI=10.1016/j.str.2022.07.006;
RA Tan Y.Z., Keon K.A., Abdelaziz R., Imming P., Schulze W., Schumacher K.,
RA Rubinstein J.L.;
RT "Structure of V-ATPase from citrus fruit.";
RL Structure 30:1403-1410.e4(2022).
CC -!- FUNCTION: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase),
CC a multisubunit enzyme composed of a peripheral complex (V1) that
CC hydrolyzes ATP and a membrane integral complex (V0) that translocates
CC protons. V-ATPase is responsible for acidifying and maintaining the pH
CC of intracellular compartments. {ECO:0000256|PIRNR:PIRNR015945}.
CC -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme made up of two
CC complexes: the ATP-hydrolytic V1 complex and the proton translocation
CC V0 complex. {ECO:0000256|PIRNR:PIRNR015945}.
CC -!- SIMILARITY: Belongs to the V-ATPase F subunit family.
CC {ECO:0000256|ARBA:ARBA00010148, ECO:0000256|PIRNR:PIRNR015945}.
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DR EMBL; KK785127; KDO48920.1; -; Genomic_DNA.
DR RefSeq; XP_006471674.1; XM_006471611.2.
DR RefSeq; XP_006471675.1; XM_006471612.2.
DR RefSeq; XP_006471676.1; XM_006471613.2.
DR PDB; 7UW9; EM; 4.20 A; N=1-130.
DR PDB; 7UWA; EM; 4.30 A; N=1-130.
DR PDB; 7UWB; EM; 3.90 A; N=1-130.
DR PDB; 7UWC; EM; 4.00 A; N=1-130.
DR AlphaFoldDB; A0A067E4V9; -.
DR EMDB; EMD-26825; -.
DR EMDB; EMD-26826; -.
DR EMDB; EMD-26827; -.
DR EMDB; EMD-26828; -.
DR SMR; A0A067E4V9; -.
DR STRING; 2711.A0A067E4V9; -.
DR PaxDb; 2711-XP_006471675-1; -.
DR GeneID; 102614701; -.
DR KEGG; cit:102614701; -.
DR eggNOG; KOG3432; Eukaryota.
DR OrthoDB; 275186at2759; -.
DR Proteomes; UP000027120; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0033180; C:proton-transporting V-type ATPase, V1 domain; IEA:InterPro.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR Gene3D; 3.40.50.10580; ATPase, V1 complex, subunit F; 1.
DR InterPro; IPR008218; ATPase_V1-cplx_f_g_su.
DR InterPro; IPR005772; ATPase_V1-cplx_fsu_euk.
DR InterPro; IPR036906; ATPase_V1_fsu_sf.
DR NCBIfam; TIGR01101; V_ATP_synt_F; 1.
DR PANTHER; PTHR13861:SF2; V-TYPE PROTON ATPASE SUBUNIT F; 1.
DR PANTHER; PTHR13861; VACUOLAR ATP SYNTHASE SUBUNIT F; 1.
DR Pfam; PF01990; ATP-synt_F; 1.
DR PIRSF; PIRSF015945; ATPase_V1_F_euk; 1.
DR SUPFAM; SSF159468; AtpF-like; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:7UW9, ECO:0007829|PDB:7UWA};
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781,
KW ECO:0000256|PIRNR:PIRNR015945};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|PIRNR:PIRNR015945};
KW Reference proteome {ECO:0000313|Proteomes:UP000027120};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR015945}.
SQ SEQUENCE 130 AA; 14283 MW; 1AEC5E6A1800E3C0 CRC64;
MAGRAQIPTK SSALIAMIAD EDTVTGFLLA GVGNVDLRRK TNYLIVDSKT TVKAIEDAFK
EFTTKEDIAI VLISQYVANM IRFLVDSYNK PIPAILEIPS KDHPYDPAHD SVLSRVKNLF
SAESVASGRR
//
