VATO_MOUSE
ID VATO_MOUSE Reviewed; 205 AA.
AC Q91V37;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=V-type proton ATPase 21 kDa proteolipid subunit c'' {ECO:0000305};
DE Short=V-ATPase 21 kDa proteolipid subunit c'' {ECO:0000305};
DE AltName: Full=23 kDa subunit of V-ATPase;
DE AltName: Full=Vacuolar proton pump 21 kDa proteolipid subunit c'' {ECO:0000305};
GN Name=Atp6v0b; Synonyms=Atp6f;
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 [GENOMIC DNA / MRNA].
RC STRAIN=129/Sv, and C57BL/6J;
RX PubMed=11675001; DOI=10.1016/s0378-1119(01)00603-5;
RA Sun-Wada G.H., Murakami H., Nakai H., Wada Y., Futai M.;
RT "Mouse Atp6f, the gene encoding the 23-kDa proteolipid of vacuolar proton
RT translocating ATPase.";
RL Gene 274:93-99(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ, and C57BL/6J;
RX PubMed=11441017; DOI=10.1074/jbc.m104682200;
RA Nishi T., Kawasaki-Nishi S., Forgac M.;
RT "Expression and localization of the mouse homolog of the yeast V-ATPase 21-
RT kDa subunit c' (Vma16p).";
RL J. Biol. Chem. 276:34122-34130(2001).
RN [3]
RP INTERACTION WITH IFITM3.
RX PubMed=22467717; DOI=10.1177/1753425912443392;
RA Wee Y.S., Roundy K.M., Weis J.J., Weis J.H.;
RT "Interferon-inducible transmembrane proteins of the innate immune response
RT act as membrane organizers by influencing clathrin and v-ATPase
RT localization and function.";
RL Inn. Immun. 18:834-845(2012).
CC -!- FUNCTION: Proton-conducting pore forming of the V0 complex of
CC vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a
CC peripheral complex (V1) that hydrolyzes ATP and a membrane integral
CC complex (V0) that translocates protons (By similarity). V-ATPase is
CC responsible for acidifying and maintaining the pH of intracellular
CC compartments and in some cell types, is targeted to the plasma
CC membrane, where it is responsible for acidifying the extracellular
CC environment (By similarity). {ECO:0000250|UniProtKB:Q2TA24,
CC ECO:0000250|UniProtKB:Q99437}.
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). Interacts with IFITM3 (PubMed:22467717).
CC {ECO:0000250|UniProtKB:Q99437, ECO:0000269|PubMed:22467717}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle
CC membrane {ECO:0000250|UniProtKB:Q2TA24}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11441017}.
CC -!- SIMILARITY: Belongs to the V-ATPase proteolipid subunit family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB060654; BAB61954.1; -; mRNA.
DR EMBL; AB060655; BAB61955.1; -; Genomic_DNA.
DR EMBL; AF356006; AAL02096.1; -; mRNA.
DR EMBL; AF356007; AAL02097.1; -; Genomic_DNA.
DR CCDS; CCDS18540.1; -.
DR RefSeq; NP_291095.1; NM_033617.3.
DR AlphaFoldDB; Q91V37; -.
DR SMR; Q91V37; -.
DR BioGRID; 227579; 1.
DR STRING; 10090.ENSMUSP00000047682; -.
DR TCDB; 3.A.2.2.6; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR PhosphoSitePlus; Q91V37; -.
DR PaxDb; Q91V37; -.
DR PRIDE; Q91V37; -.
DR Antibodypedia; 32422; 86 antibodies from 18 providers.
DR DNASU; 114143; -.
DR Ensembl; ENSMUST00000036380; ENSMUSP00000047682; ENSMUSG00000033379.
DR GeneID; 114143; -.
DR KEGG; mmu:114143; -.
DR UCSC; uc008ujc.1; mouse.
DR CTD; 533; -.
DR MGI; MGI:1890510; Atp6v0b.
DR VEuPathDB; HostDB:ENSMUSG00000033379; -.
DR eggNOG; KOG0233; Eukaryota.
DR GeneTree; ENSGT00550000075120; -.
DR HOGENOM; CLU_085752_0_0_1; -.
DR InParanoid; Q91V37; -.
DR OMA; PYAWAST; -.
DR OrthoDB; 1408246at2759; -.
DR PhylomeDB; Q91V37; -.
DR TreeFam; TF314946; -.
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; 114143; 24 hits in 76 CRISPR screens.
DR ChiTaRS; Atp6v0b; mouse.
DR PRO; PR:Q91V37; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q91V37; protein.
DR Bgee; ENSMUSG00000033379; Expressed in facial nucleus and 268 other tissues.
DR ExpressionAtlas; Q91V37; baseline and differential.
DR Genevisible; Q91V37; MM.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IDA:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; ISA:MGI.
DR GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; ISS:UniProtKB.
DR GO; GO:0008553; F:P-type proton-exporting transporter activity; ISA:MGI.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:1902600; P:proton transmembrane transport; ISA:MGI.
DR Gene3D; 1.20.120.610; -; 1.
DR InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
DR InterPro; IPR000245; ATPase_proteolipid_csu.
DR InterPro; IPR035921; F/V-ATP_Csub_sf.
DR Pfam; PF00137; ATP-synt_C; 2.
DR PRINTS; PR00122; VACATPASE.
DR SUPFAM; SSF81333; SSF81333; 2.
PE 1: Evidence at protein level;
KW Cytoplasmic vesicle; Hydrogen ion transport; Ion transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..205
FT /note="V-type proton ATPase 21 kDa proteolipid subunit c''"
FT /id="PRO_0000071778"
FT TOPO_DOM 1..3
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..51
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 73..90
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 112..137
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..175
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 197..205
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT SITE 98
FT /note="Essential for proton translocation"
FT /evidence="ECO:0000250|UniProtKB:Q2TA24"
SQ SEQUENCE 205 AA; 21607 MW; C1B05E87B53C076E CRC64;
MTGLELLYLG IFVAFWACMV VVGICYTIFD LGFRFDVAWF LTETSPFMWS NLGIGLAISL
SVVGAAWGIY ITGSSIIGGG VKAPRIKTKN LVSIIFCEAV AIYGIIMAIV ISNMAEPFSA
TEPKAIGHRN YHAGYSMFGA GLTVGLSNLF CGVCVGIVGS GAALADAQNP SLFVKILIVE
IFGSAIGLFG VIVAILQTSR VKMGD
