ID   VATF_HUMAN              Reviewed;         119 AA.
AC   Q16864; C9J2K4; Q6IBA8;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 2.
DT   27-MAR-2024, entry version 189.
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=ATP6V1F; Synonyms=ATP6S14, VATF;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Fetal brain;
RX   PubMed=8581736; DOI=10.1093/dnares/2.3.107;
RA   Fujiwara T., Kawai A., Shimizu F., Hirano H., Okuno S., Takeda S.,
RA   Ozaki K., Shimada Y., Nagata M., Watanabe T., Takaichi A., Nakamura Y.,
RA   Shin S.;
RT   "Cloning, sequencing and expression of a novel cDNA encoding human vacuolar
RT   ATPase (14-kDa subunit).";
RL   DNA Res. 2:107-111(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA   Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA   Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA   Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA   Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA   Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA   Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA   Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA   Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA   Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA   Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA   Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA   Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA   Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA   Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA   McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA   Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Brain, and Lung adenocarcinoma;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [7] {ECO:0007744|PDB:6WLZ, ECO:0007744|PDB:6WM2, ECO:0007744|PDB:6WM3, ECO:0007744|PDB:6WM4}
RP   STRUCTURE BY ELECTRON MICROSCOPY (2.90 ANGSTROMS), FUNCTION, AND
RP   IDENTIFICATION IN THE V-ATPASE COMPLEX.
RX   PubMed=33065002; DOI=10.1016/j.molcel.2020.09.029;
RA   Wang L., Wu D., Robinson C.V., Wu H., Fu T.M.;
RT   "Structures of a Complete Human V-ATPase Reveal Mechanisms of Its
RT   Assembly.";
RL   Mol. Cell 80:501-511.e3(2020).
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 (PubMed:33065002). 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:Q28029, ECO:0000269|PubMed:33065002}.
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 (PubMed:33065002). The V1 complex consists of three
CC       catalytic AB heterodimers that form a heterohexamer, three peripheral
CC       stalks each consisting of EG heterodimers, one central rotor including
CC       subunits D and F, and the regulatory subunits C and H
CC       (PubMed:33065002). The proton translocation complex V0 consists of the
CC       proton transport subunit a, a ring of proteolipid subunits c9c'',
CC       rotary subunit d, subunits e and f, and the accessory subunits
CC       ATP6AP1/Ac45 and ATP6AP2/PRR (PubMed:33065002).
CC       {ECO:0000269|PubMed:33065002}.
CC   -!- INTERACTION:
CC       Q16864; Q9Y5K8: ATP6V1D; NbExp=3; IntAct=EBI-714690, EBI-2684998;
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC       vesicle membrane {ECO:0000250|UniProtKB:P50408}; Peripheral membrane
CC       protein {ECO:0000305}. Cytoplasmic vesicle, clathrin-coated vesicle
CC       membrane {ECO:0000250|UniProtKB:P50408}; Peripheral membrane protein
CC       {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q16864-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q16864-2; Sequence=VSP_045952;
CC   -!- SIMILARITY: Belongs to the V-ATPase F subunit family. {ECO:0000305}.
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DR   EMBL; D49400; BAA08392.1; -; mRNA.
DR   EMBL; CR456896; CAG33177.1; -; mRNA.
DR   EMBL; AC025594; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC104230; AAI04231.1; -; mRNA.
DR   EMBL; BC104231; AAI04232.1; -; mRNA.
DR   EMBL; BC107854; AAI07855.1; -; mRNA.
DR   EMBL; BU956696; -; NOT_ANNOTATED_CDS; mRNA.
DR   CCDS; CCDS56511.1; -. [Q16864-2]
DR   CCDS; CCDS5807.1; -. [Q16864-1]
DR   PIR; JC4193; JC4193.
DR   RefSeq; NP_001185838.1; NM_001198909.1. [Q16864-2]
DR   RefSeq; NP_004222.2; NM_004231.3. [Q16864-1]
DR   PDB; 6WLZ; EM; 2.90 A; N=1-119.
DR   PDB; 6WM2; EM; 3.10 A; N=1-119.
DR   PDB; 6WM3; EM; 3.40 A; N=1-119.
DR   PDB; 6WM4; EM; 3.60 A; N=1-119.
DR   PDB; 7U4T; EM; 3.60 A; N=1-119.
DR   PDB; 7UNF; EM; 4.08 A; F=1-119.
DR   PDBsum; 6WLZ; -.
DR   PDBsum; 6WM2; -.
DR   PDBsum; 6WM3; -.
DR   PDBsum; 6WM4; -.
DR   PDBsum; 7U4T; -.
DR   PDBsum; 7UNF; -.
DR   AlphaFoldDB; Q16864; -.
DR   EMDB; EMD-21845; -.
DR   EMDB; EMD-21847; -.
DR   EMDB; EMD-21848; -.
DR   EMDB; EMD-21849; -.
DR   EMDB; EMD-26334; -.
DR   EMDB; EMD-26623; -.
DR   SMR; Q16864; -.
DR   BioGRID; 114710; 134.
DR   ComplexPortal; CPX-2470; Vacuolar proton translocating ATPase complex, ATP6V0A1 variant.
DR   ComplexPortal; CPX-6904; Vacuolar proton translocating ATPase complex, ATP6V0A2 variant.
DR   ComplexPortal; CPX-6905; Vacuolar proton translocating ATPase complex, ATP6V0A3 variant.
DR   ComplexPortal; CPX-6912; Vacuolar proton translocating ATPase complex, ATP6V0A4 variant.
DR   IntAct; Q16864; 29.
DR   STRING; 9606.ENSP00000417378; -.
DR   DrugBank; DB01133; Tiludronic acid.
DR   TCDB; 3.A.2.2.4; the h+- or na+-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR   iPTMnet; Q16864; -.
DR   MetOSite; Q16864; -.
DR   PhosphoSitePlus; Q16864; -.
DR   BioMuta; ATP6V1F; -.
DR   DMDM; 126302612; -.
DR   EPD; Q16864; -.
DR   jPOST; Q16864; -.
DR   MassIVE; Q16864; -.
DR   MaxQB; Q16864; -.
DR   PeptideAtlas; Q16864; -.
DR   ProteomicsDB; 61111; -. [Q16864-1]
DR   ProteomicsDB; 8219; -.
DR   Pumba; Q16864; -.
DR   TopDownProteomics; Q16864-1; -. [Q16864-1]
DR   TopDownProteomics; Q16864-2; -. [Q16864-2]
DR   Antibodypedia; 4025; 228 antibodies from 25 providers.
DR   DNASU; 9296; -.
DR   Ensembl; ENST00000249289.5; ENSP00000249289.4; ENSG00000128524.5. [Q16864-1]
DR   Ensembl; ENST00000492758.1; ENSP00000417378.1; ENSG00000128524.5. [Q16864-2]
DR   GeneID; 9296; -.
DR   KEGG; hsa:9296; -.
DR   MANE-Select; ENST00000249289.5; ENSP00000249289.4; NM_004231.4; NP_004222.2.
DR   UCSC; uc003voc.3; human. [Q16864-1]
DR   AGR; HGNC:16832; -.
DR   CTD; 9296; -.
DR   DisGeNET; 9296; -.
DR   GeneCards; ATP6V1F; -.
DR   HGNC; HGNC:16832; ATP6V1F.
DR   HPA; ENSG00000128524; Low tissue specificity.
DR   MIM; 607160; gene.
DR   neXtProt; NX_Q16864; -.
DR   OpenTargets; ENSG00000128524; -.
DR   PharmGKB; PA38421; -.
DR   VEuPathDB; HostDB:ENSG00000128524; -.
DR   GeneTree; ENSGT00390000013208; -.
DR   HOGENOM; CLU_135754_0_0_1; -.
DR   InParanoid; Q16864; -.
DR   OMA; FTEERKD; -.
DR   OrthoDB; 275186at2759; -.
DR   PhylomeDB; Q16864; -.
DR   TreeFam; TF300080; -.
DR   BioCyc; MetaCyc:HS05192-MONOMER; -.
DR   PathwayCommons; Q16864; -.
DR   Reactome; R-HSA-1222556; ROS and RNS production in phagocytes.
DR   Reactome; R-HSA-77387; Insulin receptor recycling.
DR   Reactome; R-HSA-917977; Transferrin endocytosis and recycling.
DR   Reactome; R-HSA-9639288; Amino acids regulate mTORC1.
DR   Reactome; R-HSA-983712; Ion channel transport.
DR   SignaLink; Q16864; -.
DR   BioGRID-ORCS; 9296; 664 hits in 1160 CRISPR screens.
DR   ChiTaRS; ATP6V1F; human.
DR   GeneWiki; ATP6V1F; -.
DR   GenomeRNAi; 9296; -.
DR   Pharos; Q16864; Tbio.
DR   PRO; PR:Q16864; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; Q16864; Protein.
DR   Bgee; ENSG00000128524; Expressed in prefrontal cortex and 212 other cell types or tissues.
DR   ExpressionAtlas; Q16864; baseline and differential.
DR   GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0010008; C:endosome membrane; NAS:ComplexPortal.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; NAS:ComplexPortal.
DR   GO; GO:0005765; C:lysosomal membrane; NAS:ComplexPortal.
DR   GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; NAS:ComplexPortal.
DR   GO; GO:0033176; C:proton-transporting V-type ATPase complex; NAS:ComplexPortal.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:1902495; C:transmembrane transporter complex; IEA:Ensembl.
DR   GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IDA:UniProtKB.
DR   GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; ISS:UniProtKB.
DR   GO; GO:0042625; F:ATPase-coupled ion transmembrane transporter activity; NAS:UniProtKB.
DR   GO; GO:0015078; F:proton transmembrane transporter activity; NAS:UniProtKB.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0048388; P:endosomal lumen acidification; NAS:ComplexPortal.
DR   GO; GO:0061795; P:Golgi lumen acidification; NAS:ComplexPortal.
DR   GO; GO:0051452; P:intracellular pH reduction; NAS:ComplexPortal.
DR   GO; GO:0007042; P:lysosomal lumen acidification; NAS:ComplexPortal.
DR   GO; GO:1902600; P:proton transmembrane transport; NAS:UniProtKB.
DR   GO; GO:0097401; P:synaptic vesicle lumen acidification; IEA:Ensembl.
DR   GO; GO:0007035; P:vacuolar acidification; NAS:ComplexPortal.
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.
DR   Genevisible; Q16864; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cytoplasmic vesicle;
KW   Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW   Synapse; Transport.
FT   CHAIN           1..119
FT                   /note="V-type proton ATPase subunit F"
FT                   /id="PRO_0000144799"
FT   VAR_SEQ         52
FT                   /note="F -> FRSLGSLPGSVVEANPNQRDPPLWDEIDS (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_045952"
FT   VARIANT         24
FT                   /note="G -> V (in dbSNP:rs10958)"
FT                   /id="VAR_048348"
FT   CONFLICT        8
FT                   /note="I -> T (in Ref. 1; BAA08392)"
FT                   /evidence="ECO:0000305"
FT   STRAND          6..12
FT                   /evidence="ECO:0007829|PDB:6WLZ"
FT   HELIX           14..23
FT                   /evidence="ECO:0007829|PDB:6WLZ"
FT   STRAND          34..36
FT                   /evidence="ECO:0007829|PDB:6WM2"
FT   HELIX           45..57
FT                   /evidence="ECO:0007829|PDB:6WLZ"
FT   STRAND          61..67
FT                   /evidence="ECO:0007829|PDB:6WLZ"
FT   HELIX           68..71
FT                   /evidence="ECO:0007829|PDB:6WLZ"
FT   HELIX           75..79
FT                   /evidence="ECO:0007829|PDB:6WLZ"
FT   STRAND          84..91
FT                   /evidence="ECO:0007829|PDB:6WLZ"
FT   STRAND          94..96
FT                   /evidence="ECO:0007829|PDB:6WLZ"
FT   STRAND          100..102
FT                   /evidence="ECO:0007829|PDB:6WLZ"
FT   STRAND          104..106
FT                   /evidence="ECO:0007829|PDB:6WLZ"
FT   TURN            108..111
FT                   /evidence="ECO:0007829|PDB:6WM3"
SQ   SEQUENCE   119 AA;  13370 MW;  9FE5A8BD249A85FA CRC64;
     MAGRGKLIAV IGDEDTVTGF LLGGIGELNK NRHPNFLVVE KDTTINEIED TFRQFLNRDD
     IGIILINQYI AEMVRHALDA HQQSIPAVLE IPSKEHPYDA AKDSILRRAR GMFTAEDLR
//