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   27-MAR-2024, entry version 154.
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 subunit 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}.
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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; 10090-ENSMUSP00000047682; -.
DR   Antibodypedia; 32422; 89 antibodies from 19 providers.
DR   DNASU; 114143; -.
DR   Ensembl; ENSMUST00000036380.14; ENSMUSP00000047682.8; ENSMUSG00000033379.14.
DR   GeneID; 114143; -.
DR   KEGG; mmu:114143; -.
DR   UCSC; uc008ujc.1; mouse.
DR   AGR; MGI:1890510; -.
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; GWFLENT; -.
DR   OrthoDB; 1112183at2759; -.
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 80 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 270 other cell types or tissues.
DR   ExpressionAtlas; Q91V37; baseline and differential.
DR   GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005768; C:endosome; IDA:MGI.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0033176; C:proton-transporting V-type ATPase complex; IDA:MGI.
DR   GO; GO:0033179; C:proton-transporting V-type ATPase, V0 domain; ISA:MGI.
DR   GO; GO:1902495; C:transmembrane transporter complex; IDA: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   CDD; cd18177; ATP-synt_Vo_c_ATP6F_rpt1; 1.
DR   CDD; cd18178; ATP-synt_Vo_c_ATP6F_rpt2; 1.
DR   Gene3D; 1.20.120.610; lithium bound rotor ring of v- atpase; 1.
DR   InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
DR   InterPro; IPR000245; ATPase_proteolipid_csu.
DR   InterPro; IPR035921; F/V-ATP_Csub_sf.
DR   PANTHER; PTHR10263:SF18; V-TYPE PROTON ATPASE 21 KDA PROTEOLIPID SUBUNIT C; 1.
DR   PANTHER; PTHR10263; V-TYPE PROTON ATPASE PROTEOLIPID SUBUNIT; 1.
DR   Pfam; PF00137; ATP-synt_C; 2.
DR   PRINTS; PR00122; VACATPASE.
DR   SUPFAM; SSF81333; F1F0 ATP synthase subunit C; 2.
DR   Genevisible; Q91V37; MM.
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
//