ID   VATF_AEDAE              Reviewed;         127 AA.
AC   Q1HQK8;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=V-type proton ATPase subunit F;
DE            Short=V-ATPase subunit F;
DE   AltName: Full=V-ATPase 14 kDa subunit;
DE   AltName: Full=Vacuolar proton pump subunit F;
GN   ORFNames=AAEL002464;
OS   Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Culicinae; Aedini; Aedes; Stegomyia.
OX   NCBI_TaxID=7159;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Black-eyed Liverpool; TISSUE=Salivary gland;
RX   PubMed=17204158; DOI=10.1186/1471-2164-8-6;
RA   Ribeiro J.M.C., Arca B., Lombardo F., Calvo E., Phan V.M., Chandra P.K.,
RA   Wikel S.K.;
RT   "An annotated catalogue of salivary gland transcripts in the adult female
RT   mosquito, Aedes aegypti.";
RL   BMC Genomics 8:6-6(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LVPib12;
RX   PubMed=17510324; DOI=10.1126/science.1138878;
RA   Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA   Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA   Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA   Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA   Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA   Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA   El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA   Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA   Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA   Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA   Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA   Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA   Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA   Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA   Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA   Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA   Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT   "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL   Science 316:1718-1723(2007).
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 (By similarity).
CC       {ECO:0000250|UniProtKB:Q16864, ECO:0000250|UniProtKB:Q28029}.
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 (By similarity).
CC       {ECO:0000250|UniProtKB:Q16864}.
CC   -!- SIMILARITY: Belongs to the V-ATPase F subunit family. {ECO:0000305}.
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DR   EMBL; DQ440436; ABF18469.1; -; mRNA.
DR   EMBL; CH477243; EAT46336.1; -; Genomic_DNA.
DR   RefSeq; XP_001655376.1; XM_001655326.1.
DR   AlphaFoldDB; Q1HQK8; -.
DR   SMR; Q1HQK8; -.
DR   STRING; 7159.AAEL002464-PA; -.
DR   GeneID; 5574816; -.
DR   KEGG; aag:5574816; -.
DR   VEuPathDB; VectorBase:AAEL002464; -.
DR   eggNOG; KOG3432; Eukaryota.
DR   HOGENOM; CLU_135754_0_0_1; -.
DR   InParanoid; Q1HQK8; -.
DR   OMA; YTNAFPA; -.
DR   OrthoDB; 1483558at2759; -.
DR   PhylomeDB; Q1HQK8; -.
DR   Proteomes; UP000008820; Chromosome 3.
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; -; 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   Pfam; PF01990; ATP-synt_F; 1.
DR   PIRSF; PIRSF015945; ATPase_V1_F_euk; 1.
DR   SUPFAM; SSF159468; SSF159468; 1.
DR   TIGRFAMs; TIGR01101; V_ATP_synt_F; 1.
PE   2: Evidence at transcript level;
KW   Hydrogen ion transport; Ion transport; Reference proteome; Transport.
FT   CHAIN           1..127
FT                   /note="V-type proton ATPase subunit F"
FT                   /id="PRO_0000406048"
SQ   SEQUENCE   127 AA;  14124 MW;  2ADFEFE8E73C3725 CRC64;
     MALLSAVKGK LISVIGDEDT CVGFLLGGIG EINKNRHPNF MVVDKNTAVS EIEDCFKRFI
     KRDDIDIILI NQNYAEMIRH VIDAHTSPTP AVLEIPSKDH PYDASKDSIL RRAKGMFNPD
     DMVANRG