ID   A0A1J1HNB5_9DIPT        Unreviewed;       128 AA.
AC   A0A1J1HNB5;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=V-type proton ATPase subunit F {ECO:0000256|PIRNR:PIRNR015945};
GN   ORFNames=CLUMA_CG003189 {ECO:0000313|EMBL:CRK89443.1};
OS   Clunio marinus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Chironomoidea; Chironomidae;
OC   Clunio.
OX   NCBI_TaxID=568069 {ECO:0000313|EMBL:CRK89443.1, ECO:0000313|Proteomes:UP000183832};
RN   [1] {ECO:0000313|EMBL:CRK89443.1, ECO:0000313|Proteomes:UP000183832}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Syromyatnikov M.Y., Popov V.N.;
RL   Submitted (APR-2015) 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 (By similarity). V-ATPase is responsible for acidifying and
CC       maintaining the pH of intracellular compartments and in some cell
CC       types, is targeted to the plasma membrane, where it is responsible for
CC       acidifying the extracellular environment.
CC       {ECO:0000256|ARBA:ARBA00029379}.
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 (By similarity). The V1 complex consists of three catalytic
CC       AB heterodimers that form a heterohexamer, three peripheral stalks each
CC       consisting of EG heterodimers, one central rotor including subunits D
CC       and F, and the regulatory subunits C and H (By similarity). The proton
CC       translocation complex V0 consists of the proton transport subunit a, a
CC       ring of proteolipid subunits c9c'', rotary subunit d, subunits e and f,
CC       and the accessory subunits VhaAC45 and ATP6AP2.
CC       {ECO:0000256|ARBA:ARBA00029469}.
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; CVRI01000012; CRK89443.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J1HNB5; -.
DR   STRING; 568069.A0A1J1HNB5; -.
DR   OrthoDB; 275186at2759; -.
DR   Proteomes; UP000183832; Unassembled WGS sequence.
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   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:UP000183832};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR015945}.
SQ   SEQUENCE   128 AA;  14180 MW;  445ED090A2C45CC8 CRC64;
     MALHSAIKGK LISVIGDEDT CVGFLLGGVG EINKNRHPNF MVVDKNTPIS ELEDCFKRFV
     KRDDIDIILI NQNYAELIRH VIDAHTAPIP AVLEIPSKDH PYDATKDSIL RRAKGMFSAD
     DLVGVNRG
//