VATF_ANOGA
ID VATF_ANOGA Reviewed; 127 AA.
AC Q17029; Q7QC67;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 25-MAY-2022, entry version 128.
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 Name=Vha14; ORFNames=AGAP002473;
OS Anopheles gambiae (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7165;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=G3; TISSUE=Midgut;
RX PubMed=8917545; DOI=10.1073/pnas.93.23.13066;
RA Dimopoulos G.M., Richman A.M., della Torre A., Kafatos F.C., Louis C.;
RT "Identification and characterization of differentially expressed cDNAs of
RT the vector mosquito, Anopheles gambiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:13066-13071(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEST;
RX PubMed=12364791; DOI=10.1126/science.1076181;
RA Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA Collins F.H., Hoffman S.L.;
RT "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL Science 298:129-149(2002).
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; Z69979; CAA93819.1; -; mRNA.
DR EMBL; AAAB01008859; EAA08191.2; -; Genomic_DNA.
DR RefSeq; XP_312465.2; XM_312465.4.
DR AlphaFoldDB; Q17029; -.
DR SMR; Q17029; -.
DR STRING; 7165.AGAP002473-PA; -.
DR PaxDb; Q17029; -.
DR GeneID; 1273486; -.
DR KEGG; aga:AgaP_AGAP002473; -.
DR CTD; 1273486; -.
DR VEuPathDB; VectorBase:AGAP002473; -.
DR eggNOG; KOG3432; Eukaryota.
DR HOGENOM; CLU_135754_0_0_1; -.
DR InParanoid; Q17029; -.
DR OMA; YTNAFPA; -.
DR OrthoDB; 1483558at2759; -.
DR PhylomeDB; Q17029; -.
DR Proteomes; UP000007062; Chromosome 2R.
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; -; 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_0000144803"
FT CONFLICT 17
FT /note="D -> H (in Ref. 1; CAA93819)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="L -> V (in Ref. 1; CAA93819)"
FT /evidence="ECO:0000305"
FT CONFLICT 92..93
FT /note="VL -> DV (in Ref. 1; CAA93819)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 127 AA; 14152 MW; 26AA3DE81BA31DA7 CRC64;
MALLSAMKGK LISVIGDEDT CVGFLLGGVG EINKNRHPNF MVVDKNTAVS EIEDCFKRFI
KRDDIDIILI NQNYAELIRH VIDSHTAPTP AVLEIPSKDH PYDASKDSIL RRAKGMFNPE
DMIANRG
