VATF_RAT
ID VATF_RAT Reviewed; 119 AA.
AC P50408;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 152.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Brain;
RX PubMed=8621738; DOI=10.1074/jbc.271.6.3324;
RA Peng S.B., Crider B.P., Tsai S.J., Xie X.S., Stone D.K.;
RT "Identification of a 14-kDa subunit associated with the catalytic sector of
RT clathrin-coated vesicle H+-ATPase.";
RL J. Biol. Chem. 271:3324-3327(1996).
RN [2]
RP PROTEIN SEQUENCE OF 31-41 AND 59-75, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Diao W.;
RL Submitted (APR-2007) to UniProtKB.
RN [3] {ECO:0007744|PDB:6VQ6, ECO:0007744|PDB:6VQ7, ECO:0007744|PDB:6VQ8, ECO:0007744|PDB:6VQC, ECO:0007744|PDB:6VQG, ECO:0007744|PDB:6VQH}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS), FUNCTION, IDENTIFICATION
RP IN THE V-ATPASE COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND TISSUE SPECIFICITY.
RX PubMed=32165585; DOI=10.1126/science.aaz2924;
RA Abbas Y.M., Wu D., Bueler S.A., Robinson C.V., Rubinstein J.L.;
RT "Structure of V-ATPase from the mammalian brain.";
RL Science 367:1240-1246(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:32165585). 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 (PubMed:32165585).
CC {ECO:0000269|PubMed:32165585}.
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:32165585). 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:32165585). 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:32165585).
CC {ECO:0000269|PubMed:32165585}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane {ECO:0000269|PubMed:32165585}; Peripheral membrane
CC protein {ECO:0000305}. Cytoplasmic vesicle, clathrin-coated vesicle
CC membrane {ECO:0000269|PubMed:32165585}; Peripheral membrane protein
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in brain (at protein level).
CC {ECO:0000269|PubMed:32165585}.
CC -!- SIMILARITY: Belongs to the V-ATPase F subunit family. {ECO:0000305}.
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DR EMBL; U43175; AAB03684.1; -; mRNA.
DR RefSeq; NP_446336.1; NM_053884.1.
DR PDB; 6VQ6; EM; 3.90 A; L=1-119.
DR PDB; 6VQ7; EM; 4.00 A; L=1-119.
DR PDB; 6VQ8; EM; 3.90 A; L=1-119.
DR PDB; 6VQC; EM; 3.80 A; L=1-119.
DR PDB; 6VQG; EM; 4.20 A; L=1-119.
DR PDB; 6VQH; EM; 4.40 A; L=1-119.
DR PDBsum; 6VQ6; -.
DR PDBsum; 6VQ7; -.
DR PDBsum; 6VQ8; -.
DR PDBsum; 6VQC; -.
DR PDBsum; 6VQG; -.
DR PDBsum; 6VQH; -.
DR AlphaFoldDB; P50408; -.
DR SMR; P50408; -.
DR IntAct; P50408; 4.
DR STRING; 10116.ENSRNOP00000009737; -.
DR jPOST; P50408; -.
DR PaxDb; P50408; -.
DR PRIDE; P50408; -.
DR GeneID; 116664; -.
DR KEGG; rno:116664; -.
DR UCSC; RGD:621552; rat.
DR CTD; 9296; -.
DR RGD; 621552; Atp6v1f.
DR eggNOG; KOG3432; Eukaryota.
DR HOGENOM; CLU_135754_0_0_1; -.
DR InParanoid; P50408; -.
DR OMA; YTNAFPA; -.
DR OrthoDB; 1483558at2759; -.
DR PhylomeDB; P50408; -.
DR TreeFam; TF300080; -.
DR Reactome; R-RNO-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-RNO-77387; Insulin receptor recycling.
DR Reactome; R-RNO-917977; Transferrin endocytosis and recycling.
DR Reactome; R-RNO-9639288; Amino acids regulate mTORC1.
DR Reactome; R-RNO-983712; Ion channel transport.
DR PRO; PR:P50408; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000007392; Expressed in cerebellum and 20 other tissues.
DR Genevisible; P50408; RN.
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:RGD.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; ISO:RGD.
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 3D-structure; Cytoplasmic vesicle; Direct protein sequencing;
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_0000144801"
SQ SEQUENCE 119 AA; 13370 MW; 9FFA95BD2667AA2A CRC64;
MAGRGKLIAV IGDEDTVTGF LLGGIGELNK NRHPNFLVVE KDTTINEIED TFRQFLNRDD
IGIILINQYI AEMVRHALDA HQRSIPAVLE IPSKEHPYDA AKDSILRRAK GMFTAEDLR
