VATF_HUMAN
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 03-AUG-2022, entry version 180.
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 PDBsum; 6WLZ; -.
DR PDBsum; 6WM2; -.
DR PDBsum; 6WM3; -.
DR PDBsum; 6WM4; -.
DR AlphaFoldDB; Q16864; -.
DR SMR; Q16864; -.
DR BioGRID; 114710; 105.
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; 23.
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 PRIDE; Q16864; -.
DR ProteomicsDB; 61111; -. [Q16864-1]
DR ProteomicsDB; 8219; -.
DR TopDownProteomics; Q16864-1; -. [Q16864-1]
DR TopDownProteomics; Q16864-2; -. [Q16864-2]
DR Antibodypedia; 4025; 209 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 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; YTNAFPA; -.
DR OrthoDB; 1483558at2759; -.
DR PhylomeDB; Q16864; -.
DR TreeFam; TF300080; -.
DR BioCyc; MetaCyc:HS05192-MON; -.
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; 635 hits in 1082 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 210 other tissues.
DR ExpressionAtlas; Q16864; baseline and differential.
DR Genevisible; Q16864; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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; IC:ComplexPortal.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IC:ComplexPortal.
DR GO; GO:0005765; C:lysosomal membrane; IC:ComplexPortal.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IC:ComplexPortal.
DR GO; GO:0033176; C:proton-transporting V-type ATPase complex; IC:ComplexPortal.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
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; IC:ComplexPortal.
DR GO; GO:0061795; P:Golgi lumen acidification; IC:ComplexPortal.
DR GO; GO:0051452; P:intracellular pH reduction; IC:ComplexPortal.
DR GO; GO:0007042; P:lysosomal lumen acidification; IC:ComplexPortal.
DR GO; GO:1902600; P:proton transmembrane transport; NAS:UniProtKB.
DR GO; GO:0007035; P:vacuolar acidification; IC:ComplexPortal.
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 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
