ID   VATF_MOUSE              Reviewed;         119 AA.
AC   Q9D1K2; Q3U6X0;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 2.
DT   03-AUG-2022, entry version 148.
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   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, Embryo, and Pancreas;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Mammary tumor;
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   [3]
RP   PROTEIN SEQUENCE OF 42-53, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Kidney, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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 ATP6AP1/Ac45 and ATP6AP2/PRR (By
CC       similarity). {ECO:0000250|UniProtKB:Q16864}.
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   -!- SIMILARITY: Belongs to the V-ATPase F subunit family. {ECO:0000305}.
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DR   EMBL; AK003419; BAB22780.1; -; mRNA.
DR   EMBL; AK007327; BAB24962.1; -; mRNA.
DR   EMBL; AK152153; BAE30988.1; -; mRNA.
DR   EMBL; AK152929; BAE31604.1; -; mRNA.
DR   EMBL; AK152959; BAE31622.1; -; mRNA.
DR   EMBL; BC016553; AAH16553.1; -; mRNA.
DR   CCDS; CCDS19960.1; -.
DR   RefSeq; NP_079657.1; NM_025381.2.
DR   AlphaFoldDB; Q9D1K2; -.
DR   SMR; Q9D1K2; -.
DR   BioGRID; 211247; 12.
DR   IntAct; Q9D1K2; 1.
DR   STRING; 10090.ENSMUSP00000004396; -.
DR   TCDB; 3.A.2.2.6; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR   iPTMnet; Q9D1K2; -.
DR   PhosphoSitePlus; Q9D1K2; -.
DR   REPRODUCTION-2DPAGE; Q9D1K2; -.
DR   EPD; Q9D1K2; -.
DR   jPOST; Q9D1K2; -.
DR   MaxQB; Q9D1K2; -.
DR   PaxDb; Q9D1K2; -.
DR   PeptideAtlas; Q9D1K2; -.
DR   PRIDE; Q9D1K2; -.
DR   ProteomicsDB; 297874; -.
DR   TopDownProteomics; Q9D1K2; -.
DR   Antibodypedia; 4025; 209 antibodies from 25 providers.
DR   DNASU; 66144; -.
DR   Ensembl; ENSMUST00000004396; ENSMUSP00000004396; ENSMUSG00000004285.
DR   GeneID; 66144; -.
DR   KEGG; mmu:66144; -.
DR   UCSC; uc009bdp.1; mouse.
DR   CTD; 9296; -.
DR   MGI; MGI:1913394; Atp6v1f.
DR   VEuPathDB; HostDB:ENSMUSG00000004285; -.
DR   eggNOG; KOG3432; Eukaryota.
DR   GeneTree; ENSGT00390000013208; -.
DR   HOGENOM; CLU_135754_0_0_1; -.
DR   InParanoid; Q9D1K2; -.
DR   OMA; YTNAFPA; -.
DR   OrthoDB; 1483558at2759; -.
DR   PhylomeDB; Q9D1K2; -.
DR   TreeFam; TF300080; -.
DR   Reactome; R-MMU-1222556; ROS and RNS production in phagocytes.
DR   Reactome; R-MMU-77387; Insulin receptor recycling.
DR   Reactome; R-MMU-917977; Transferrin endocytosis and recycling.
DR   Reactome; R-MMU-9639288; Amino acids regulate mTORC1.
DR   Reactome; R-MMU-983712; Ion channel transport.
DR   BioGRID-ORCS; 66144; 26 hits in 72 CRISPR screens.
DR   ChiTaRS; Atp6v1f; mouse.
DR   PRO; PR:Q9D1K2; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; Q9D1K2; protein.
DR   Bgee; ENSMUSG00000004285; Expressed in embryonic brain and 85 other tissues.
DR   ExpressionAtlas; Q9D1K2; baseline and differential.
DR   Genevisible; Q9D1K2; MM.
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:0016020; C:membrane; ISO:MGI.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; ISO:MGI.
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   1: Evidence at protein level;
KW   Cytoplasmic vesicle; Direct protein sequencing; Hydrogen ion transport;
KW   Ion transport; Membrane; Reference proteome; Synapse; Transport.
FT   CHAIN           1..119
FT                   /note="V-type proton ATPase subunit F"
FT                   /id="PRO_0000144800"
FT   CONFLICT        35
FT                   /note="N -> D (in Ref. 1; BAB22780)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   119 AA;  13370 MW;  9FFA95BD2667AA2A CRC64;
     MAGRGKLIAV IGDEDTVTGF LLGGIGELNK NRHPNFLVVE KDTTINEIED TFRQFLNRDD
     IGIILINQYI AEMVRHALDA HQRSIPAVLE IPSKEHPYDA AKDSILRRAK GMFTAEDLR