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Database: UniProt
Entry: A0A6I9I4L0_VICPA
LinkDB: A0A6I9I4L0_VICPA
Original site: A0A6I9I4L0_VICPA 
ID   A0A6I9I4L0_VICPA        Unreviewed;       119 AA.
AC   A0A6I9I4L0;
DT   07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT   07-OCT-2020, sequence version 1.
DT   18-JUN-2025, entry version 24.
DE   RecName: Full=V-type proton ATPase subunit F {ECO:0000256|ARBA:ARBA00013430, ECO:0000256|PIRNR:PIRNR015945};
GN   Name=ATP6V1F {ECO:0000313|RefSeq:XP_006202337.1};
OS   Vicugna pacos (Alpaca) (Lama pacos).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Tylopoda; Camelidae; Vicugna.
OX   NCBI_TaxID=30538 {ECO:0000313|Proteomes:UP000504605, ECO:0000313|RefSeq:XP_006202337.1};
RN   [1] {ECO:0000313|RefSeq:XP_006202337.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_006202337.1};
RG   RefSeq;
RL   Submitted (MAR-2025) to UniProtKB.
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 and in some cell types, is targeted to
CC       the plasma membrane, where it is responsible for acidifying the
CC       extracellular environment. {ECO:0000256|ARBA:ARBA00045737}.
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. {ECO:0000256|PIRNR:PIRNR015945}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC       vesicle membrane {ECO:0000256|ARBA:ARBA00037827}; Peripheral membrane
CC       protein {ECO:0000256|ARBA:ARBA00037827}.
CC   -!- SIMILARITY: Belongs to the V-ATPase F subunit family.
CC       {ECO:0000256|ARBA:ARBA00010148, ECO:0000256|PIRNR:PIRNR015945}.
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DR   RefSeq; XP_006202337.1; XM_006202275.3.
DR   AlphaFoldDB; A0A6I9I4L0; -.
DR   SMR; A0A6I9I4L0; -.
DR   FunCoup; A0A6I9I4L0; 2079.
DR   GeneID; 102540127; -.
DR   KEGG; vpc:102540127; -.
DR   CTD; 9296; -.
DR   InParanoid; A0A6I9I4L0; -.
DR   OrthoDB; 2812at91561; -.
DR   Proteomes; UP000504605; Unplaced.
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   FunFam; 3.40.50.10580:FF:000001; V-type proton ATPase subunit F; 1.
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:UP000504605};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR015945}.
SQ   SEQUENCE   119 AA;  13398 MW;  9FE5A8BD2667AA2A CRC64;
     MAGRGKLIAV IGDEDTVTGF LLGGIGELNK NRHPNFLVVE KDTTINEIED TFRQFLNRDD
     IGIILINQYI AEMVRHALDA HQRSIPAVLE IPSKEHPYDA AKDSILRRAR GMFTAEDLR
//
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