VPP4_MOUSE
ID VPP4_MOUSE Reviewed; 833 AA.
AC Q920R6; Q8CJ79; Q920B5;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=V-type proton ATPase 116 kDa subunit a 4;
DE Short=V-ATPase 116 kDa isoform a 4;
DE AltName: Full=V-type proton ATPase 116 kDa subunit a isoform 4;
DE AltName: Full=Vacuolar proton translocating ATPase 116 kDa subunit a isoform 4;
DE AltName: Full=Vacuolar proton translocating ATPase 116 kDa subunit a kidney isoform;
GN Name=Atp6v0a4; Synonyms=Atp6n1b;
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 [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=11498539; DOI=10.1074/jbc.m106488200;
RA Oka T., Murata Y., Namba M., Yoshimizu T., Toyomura T., Yamamoto A.,
RA Sun-Wada G.-H., Hamasaki N., Wada Y., Futai M.;
RT "a4, a unique kidney-specific isoform of mouse vacuolar H+-ATPase subunit
RT a.";
RL J. Biol. Chem. 276:40050-40054(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH ATP6V1A AND ATP6V0C,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=NOD; TISSUE=Kidney;
RX PubMed=11495928; DOI=10.1074/jbc.m107267200;
RA Smith A.N., Finberg K.E., Wagner C.A., Lifton R.P., Devonald M.A., Su Y.,
RA Karet F.E.;
RT "Molecular cloning and characterization of Atp6n1b: a novel fourth murine
RT vacuolar H+-ATPase a-subunit gene.";
RL J. Biol. Chem. 276:42382-42388(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RA Nishi T., Forgac M.;
RT "Interaction of the a and B subunit isoforms of the mouse vacuolar proton
RT translocating ATPase.";
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Olfactory epithelium;
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].
RC TISSUE=Kidney;
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 V0 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). Involved in
CC normal vectorial acid transport into the urine by the kidney (By
CC similarity). {ECO:0000250|UniProtKB:Q29466,
CC ECO:0000250|UniProtKB:Q93050, ECO:0000250|UniProtKB:Q9HBG4}.
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 the V1 complex V-ATPase subunit A ATP6V1A
CC (PubMed:11498539). Interacts with the V0 complex V-ATPase subunit c
CC ATP6V0C (PubMed:11498539). {ECO:0000250|UniProtKB:Q93050,
CC ECO:0000269|PubMed:11498539}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:11495928, ECO:0000269|PubMed:11498539}; Multi-pass
CC membrane protein {ECO:0000255}. Basolateral cell membrane
CC {ECO:0000269|PubMed:11495928, ECO:0000269|PubMed:11498539}; Multi-pass
CC membrane protein {ECO:0000255}. Note=Localizes to the apical surface of
CC alpha-intercalated cells in the cortical collecting ducts of the distal
CC nephron (PubMed:11498539, PubMed:11495928). Localizes to the
CC basolateral surface of beta-intercalated cells in the cortical
CC collecting ducts of the distal nephron (PubMed:11498539,
CC PubMed:11495928). {ECO:0000269|PubMed:11495928,
CC ECO:0000269|PubMed:11498539}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in kidney, but not in the
CC heart, brain, spleen, lung, liver, muscle, or testis. Distribution
CC within the kidney appears more widespread than that seen in man. High
CC intensity staining at the surface of intercalated cells, with
CC additional expression in the proximal tubule.
CC -!- SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family.
CC {ECO:0000305}.
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DR EMBL; AB050903; BAB47243.1; -; mRNA.
DR EMBL; AF326316; AAL30435.1; -; mRNA.
DR EMBL; AF435090; AAN45855.1; -; mRNA.
DR EMBL; BC046979; AAH46979.1; -; mRNA.
DR CCDS; CCDS20010.1; -.
DR RefSeq; NP_536715.3; NM_080467.3.
DR AlphaFoldDB; Q920R6; -.
DR SMR; Q920R6; -.
DR BioGRID; 228267; 2.
DR STRING; 10090.ENSMUSP00000039381; -.
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; Q920R6; -.
DR PhosphoSitePlus; Q920R6; -.
DR jPOST; Q920R6; -.
DR MaxQB; Q920R6; -.
DR PaxDb; Q920R6; -.
DR PeptideAtlas; Q920R6; -.
DR PRIDE; Q920R6; -.
DR ProteomicsDB; 297931; -.
DR Antibodypedia; 3120; 126 antibodies from 23 providers.
DR DNASU; 140494; -.
DR Ensembl; ENSMUST00000040259; ENSMUSP00000039381; ENSMUSG00000038600.
DR Ensembl; ENSMUST00000114908; ENSMUSP00000110558; ENSMUSG00000038600.
DR GeneID; 140494; -.
DR KEGG; mmu:140494; -.
DR UCSC; uc009bjo.2; mouse.
DR CTD; 50617; -.
DR MGI; MGI:2153480; Atp6v0a4.
DR VEuPathDB; HostDB:ENSMUSG00000038600; -.
DR eggNOG; KOG2189; Eukaryota.
DR GeneTree; ENSGT00950000182881; -.
DR HOGENOM; CLU_005230_0_0_1; -.
DR InParanoid; Q920R6; -.
DR OMA; GCKEFMF; -.
DR OrthoDB; 181796at2759; -.
DR PhylomeDB; Q920R6; -.
DR TreeFam; TF300346; -.
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-983712; Ion channel transport.
DR BioGRID-ORCS; 140494; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Atp6v0a4; mouse.
DR PRO; PR:Q920R6; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q920R6; protein.
DR Bgee; ENSMUSG00000038600; Expressed in right kidney and 57 other tissues.
DR Genevisible; Q920R6; MM.
DR GO; GO:0045177; C:apical part of cell; IDA:UniProtKB.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005903; C:brush border; IDA:MGI.
DR GO; GO:0031526; C:brush border membrane; ISO:MGI.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IPI:MGI.
DR GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR GO; GO:0051117; F:ATPase binding; ISO:MGI.
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:0001503; P:ossification; ISO:MGI.
DR GO; GO:1902600; P:proton transmembrane transport; IPI:MGI.
DR GO; GO:0006885; P:regulation of pH; ISO:MGI.
DR GO; GO:0097254; P:renal tubular secretion; ISO:MGI.
DR GO; GO:0007605; P:sensory perception of sound; ISO:MGI.
DR GO; GO:0007035; P:vacuolar acidification; IBA:GO_Central.
DR InterPro; IPR002490; V-ATPase_116kDa_su.
DR InterPro; IPR026028; V-type_ATPase_116kDa_su_euka.
DR PANTHER; PTHR11629; PTHR11629; 1.
DR Pfam; PF01496; V_ATPase_I; 1.
DR PIRSF; PIRSF001293; ATP6V0A1; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Hydrogen ion transport; Ion transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..833
FT /note="V-type proton ATPase 116 kDa subunit a 4"
FT /id="PRO_0000119220"
FT TOPO_DOM 1..390
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 391..409
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 410..411
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 412..428
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 429..443
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 444..473
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 474..538
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 539..558
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 559..576
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 577..597
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 598..642
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 643..662
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 663..720
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 721..745
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 746..766
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 767..805
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 806..833
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 681..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 4
FT /note="V -> A (in Ref. 3; AAN45855)"
FT /evidence="ECO:0000305"
FT CONFLICT 161
FT /note="T -> A (in Ref. 2; AAL30435)"
FT /evidence="ECO:0000305"
FT CONFLICT 625
FT /note="D -> N (in Ref. 3; AAN45855)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 833 AA; 95605 MW; BADEE53790C83B45 CRC64;
MASVFRSEEM CLSQVFLQVE AAYCCVAELG ELGLVQFKDL NANVNSFQRK FVNEVRRCES
LERILRFLED EMQNEILIQV PEKDAETPLP REMITLETTL EKLEGELQEA NQSHQALKKS
FLELTELKYL LKKTQDFFET ETNLGEDFFV EDTSGLLELR TIPAFMTGKL GFTAGVINRE
RMASFERLLW RVCRGNVYLK FSEMDTLLED PVTKEEIKKN IFIIFYQGEQ LRLKIKKICD
GFRATIYPCP EHAAERREML TSVNVRLEDL ITVITQTESH RQRLLQEAAA NWHSWVIKVQ
KMKAVYHVLN MCNIDVTQQC IIAEIWFPVA DTRHIKKALE QGMELSGSSM IPIMTEVETK
TDPPTFNRTN KFTAGFQNIV DAYGVGSYRE INPAPYTIIT FPFLFAVMFG DCGHGMVMLM
AALWMVLNER HLLAQKSTNE MWNIFFNGRY LILLMGIFSI YTGLIYNDCF SKSFNIFGSS
WSVQPMFRNG TWNTHIVENS PYLQLDPAIP GVYSGNPYPF GIDPIWNLAS NKLTFLNSYK
MKMSVILGIA HMIFGVILSL FNHIYFRRTL NIILQFIPEM IFMLSLFGYL VFMIIFKWCR
YDAHTSRKAP SILIHFIGMF LFDYDDSSNA PLYGHQQEVQ TFFVIIALVS VPWMLLIKPF
VLRAKHQKSQ LQSFTIHEDA VEGDHSGHSS KKTAGAHGMK DGHEEEFNFG DIFVHQAIHT
IEYCLGCISN TASYLRLWAL SLAHAELSEV LWTMVMSIGL RLQGWAGLVG VFIIFAVFAV
LTVAILLVME GLSAFLHALR LHWVEFQNKF YEGAGSKFSP FSFKHVLEGT AEE
