ID A0A5C6NA74_9TELE Unreviewed; 119 AA.
AC A0A5C6NA74;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 18-JUN-2025, entry version 16.
DE RecName: Full=V-type proton ATPase subunit F {ECO:0000256|ARBA:ARBA00013430, ECO:0000256|PIRNR:PIRNR015945};
GN ORFNames=D4764_22G0000390 {ECO:0000313|EMBL:TWW64392.1};
OS Takifugu flavidus (sansaifugu).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=433684 {ECO:0000313|EMBL:TWW64392.1, ECO:0000313|Proteomes:UP000324091};
RN [1] {ECO:0000313|EMBL:TWW64392.1, ECO:0000313|Proteomes:UP000324091}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTHZ2018 {ECO:0000313|EMBL:TWW64392.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:TWW64392.1};
RA Xiao S.;
RT "Chromosome genome assembly for Takifugu flavidus.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
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 and in some cell types, is targeted to
CC the plasma membrane, where it is responsible for acidifying the
CC extracellular environment. {ECO:0000256|ARBA:ARBA00045737}.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TWW64392.1}.
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DR EMBL; RHFK02000015; TWW64392.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5C6NA74; -.
DR Proteomes; UP000324091; Chromosome 22.
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 FunFam; 3.40.50.10580:FF:000001; V-type proton ATPase subunit F; 1.
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 3: Inferred from homology;
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:UP000324091};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR015945}.
SQ SEQUENCE 119 AA; 13221 MW; 4F021DC62F713ACD CRC64;
MAGRGKLIAV IGDEDTCTGF LLGGIGELNK NRKPNFLVVE KDTSITEIEE TFKSFLARSD
IGIILINQFI AEMIRHAIDA HMQSIPAVLE IPSKEHPYDA SKDSILRRAK GMFSAEDFR
//