ID   VATF_MANSE              Reviewed;         124 AA.
AC   P31478;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   25-MAY-2022, entry version 92.
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;
OS   Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Sphingidae; Sphinginae; Sphingini; Manduca.
OX   NCBI_TaxID=7130;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   TISSUE=Midgut;
RX   PubMed=8106421; DOI=10.1016/s0021-9258(17)41926-0;
RA   Graef R., Lepier A., Harvey W.R., Wieczorek H.;
RT   "A novel 14-kDa V-ATPase subunit in the tobacco hornworm midgut.";
RL   J. Biol. Chem. 269:3767-3774(1994).
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; X67130; CAA47609.1; -; mRNA.
DR   PIR; A53055; A53055.
DR   AlphaFoldDB; P31478; -.
DR   SMR; P31478; -.
DR   DIP; DIP-61391N; -.
DR   IntAct; P31478; 1.
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; Transport.
FT   CHAIN           1..124
FT                   /note="V-type proton ATPase subunit F"
FT                   /id="PRO_0000144808"
SQ   SEQUENCE   124 AA;  13814 MW;  F519CD5B5E0ADCF1 CRC64;
     MALHAAVKGK LISVIGDEDT CVGFLLGGIG EINKNRHPNF MVVDKNTPVS EIEECFKRFV
     KRDDIDIILI NQNVAELVRH VIDAHTAPVP SVLEIPSKDH PYDASKDSIL RRAKGMFNPE
     DLVR