VATF_VANPO
ID VATF_VANPO Reviewed; 119 AA.
AC A7TMI5;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 62.
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=VMA7; ORFNames=Kpol_1064p61;
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC Y-8283 / UCD 57-17;
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(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 (By similarity).
CC {ECO:0000250|UniProtKB:P39111}.
CC -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a peripheral
CC catalytic V1 complex (components A to H) attached to an integral
CC membrane V0 proton pore complex (components: a, c, c', c'', d, e, f and
CC VOA1). {ECO:0000250|UniProtKB:P39111}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250|UniProtKB:P39111};
CC Peripheral membrane protein {ECO:0000305}; Cytoplasmic side
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the V-ATPase F subunit family. {ECO:0000305}.
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DR EMBL; DS480422; EDO16579.1; -; Genomic_DNA.
DR RefSeq; XP_001644437.1; XM_001644387.1.
DR AlphaFoldDB; A7TMI5; -.
DR SMR; A7TMI5; -.
DR STRING; 436907.A7TMI5; -.
DR EnsemblFungi; EDO16579; EDO16579; Kpol_1064p61.
DR GeneID; 5544739; -.
DR KEGG; vpo:Kpol_1064p61; -.
DR eggNOG; KOG3432; Eukaryota.
DR HOGENOM; CLU_135754_0_0_1; -.
DR InParanoid; A7TMI5; -.
DR OMA; YTNAFPA; -.
DR OrthoDB; 1483558at2759; -.
DR PhylomeDB; A7TMI5; -.
DR Proteomes; UP000000267; Unassembled WGS sequence.
DR GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; ISS:UniProtKB.
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 3: Inferred from homology;
KW Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW Transport; Vacuole.
FT CHAIN 1..119
FT /note="V-type proton ATPase subunit F"
FT /id="PRO_0000406051"
SQ SEQUENCE 119 AA; 13640 MW; 1CE0390316E11F44 CRC64;
MSVDKRTLIA VIGDEDTTTG LLLAGIGQIT KETNEKNFFI YEDGKTTKEQ ILNNFINYTQ
ERQDIAILLI NQHIAEKIRS DIDNYTNAFP AILEIPSKDH PYDPEKDSVL KRVRRLFGE