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V-type proton ATPase 116 kDa subunit a isoform 4 (V-ATPase 116 kDa isoform a4) (Vacuolar proton translocating ATPase 116 kDa subunit a isoform 4) (Vacuolar proton translocating ATPase 116 kDa subunit a kidney isoform)

 VPP4_MOUSE              Reviewed;         833 AA.
Q920R6; Q8CJ79; Q920B5;
14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
23-MAY-2018, entry version 130.
RecName: Full=V-type proton ATPase 116 kDa subunit a isoform 4;
Short=V-ATPase 116 kDa isoform a4;
AltName: Full=Vacuolar proton translocating ATPase 116 kDa subunit a isoform 4;
AltName: Full=Vacuolar proton translocating ATPase 116 kDa subunit a kidney isoform;
Name=Atp6v0a4; Synonyms=Atp6n1b;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J; TISSUE=Kidney;
PubMed=11498539; DOI=10.1074/jbc.M106488200;
Oka T., Murata Y., Namba M., Yoshimizu T., Toyomura T., Yamamoto A.,
Sun-Wada G.-H., Hamasaki N., Wada Y., Futai M.;
"a4, a unique kidney-specific isoform of mouse vacuolar H+-ATPase
subunit a.";
J. Biol. Chem. 276:40050-40054(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=NOD; TISSUE=Kidney;
PubMed=11495928; DOI=10.1074/jbc.M107267200;
Smith A.N., Finberg K.E., Wagner C.A., Lifton R.P., Devonald M.A.,
Su Y., Karet F.E.;
"Molecular cloning and characterization of Atp6n1b: a novel fourth
murine vacuolar H+-ATPase a-subunit gene.";
J. Biol. Chem. 276:42382-42388(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J; TISSUE=Kidney;
Nishi T., Forgac M.;
"Interaction of the a and B subunit isoforms of the mouse vacuolar
proton translocating ATPase.";
Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Olfactory epithelium;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Part of the proton channel of the V-ATPase that is
involved in normal vectorial acid transport into the urine by the
kidney. {ECO:0000250}.
-!- SUBUNIT: The V-ATPase is a heteromultimeric enzyme composed of at
least thirteen different subunits. It has a membrane peripheral V1
sector for ATP hydrolysis and an integral V0 for proton
translocation. The V1 sector comprises subunits A-H, whereas V0
includes subunits a, d, c, c', and c''.
-!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
Note=Apical immunostaining present in male genital tissue.
According to PubMed:11498539, clearly detectable not only on the
apical surface of alpha-intercalated cells but also on the
basolateral surface of beta cells.
-!- TISSUE SPECIFICITY: Specifically expressed in kidney, but not in
the heart, brain, spleen, lung, liver, muscle, or testis.
Distribution within the kidney appears more widespread than that
seen in man. High intensity staining at the surface of
intercalated cells, with additional expression in the proximal
tubule.
-!- SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AB050903; BAB47243.1; -; mRNA.
EMBL; AF326316; AAL30435.1; -; mRNA.
EMBL; AF435090; AAN45855.1; -; mRNA.
EMBL; BC046979; AAH46979.1; -; mRNA.
CCDS; CCDS20010.1; -.
RefSeq; NP_536715.3; NM_080467.3.
UniGene; Mm.462308; -.
ProteinModelPortal; Q920R6; -.
BioGrid; 228267; 1.
IntAct; Q920R6; 2.
MINT; Q920R6; -.
STRING; 10090.ENSMUSP00000039381; -.
TCDB; 3.A.2.2.6; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
iPTMnet; Q920R6; -.
PhosphoSitePlus; Q920R6; -.
MaxQB; Q920R6; -.
PaxDb; Q920R6; -.
PeptideAtlas; Q920R6; -.
PRIDE; Q920R6; -.
Ensembl; ENSMUST00000040259; ENSMUSP00000039381; ENSMUSG00000038600.
Ensembl; ENSMUST00000114908; ENSMUSP00000110558; ENSMUSG00000038600.
GeneID; 140494; -.
KEGG; mmu:140494; -.
UCSC; uc009bjo.2; mouse.
CTD; 50617; -.
MGI; MGI:2153480; Atp6v0a4.
eggNOG; KOG2189; Eukaryota.
eggNOG; COG1269; LUCA.
GeneTree; ENSGT00390000004941; -.
HOGENOM; HOG000037059; -.
HOVERGEN; HBG014606; -.
InParanoid; Q920R6; -.
KO; K02154; -.
OMA; FILRANH; -.
OrthoDB; EOG091G01BI; -.
PhylomeDB; Q920R6; -.
TreeFam; TF300346; -.
Reactome; R-MMU-1222556; ROS, RNS production in phagocytes.
Reactome; R-MMU-77387; Insulin receptor recycling.
Reactome; R-MMU-917977; Transferrin endocytosis and recycling.
Reactome; R-MMU-983712; Ion channel transport.
PRO; PR:Q920R6; -.
Proteomes; UP000000589; Chromosome 6.
Bgee; ENSMUSG00000038600; -.
CleanEx; MM_ATP6V0A4; -.
Genevisible; Q920R6; MM.
GO; GO:0045177; C:apical part of cell; IDA:UniProtKB.
GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
GO; GO:0005903; C:brush border; IDA:MGI.
GO; GO:0031526; C:brush border membrane; ISO:MGI.
GO; GO:0005768; C:endosome; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IPI:MGI.
GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
GO; GO:0051117; F:ATPase binding; ISO:MGI.
GO; GO:0008553; F:proton-exporting ATPase activity, phosphorylative mechanism; ISA:MGI.
GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IBA:GO_Central.
GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IPI:MGI.
GO; GO:0015986; P:ATP synthesis coupled proton transport; IBA:GO_Central.
GO; GO:0007588; P:excretion; ISO:MGI.
GO; GO:0001503; P:ossification; ISO:MGI.
GO; GO:1902600; P:proton transmembrane transport; ISO:MGI.
GO; GO:0006885; P:regulation of pH; ISO:MGI.
GO; GO:0007605; P:sensory perception of sound; ISO:MGI.
GO; GO:0007035; P:vacuolar acidification; IBA:GO_Central.
GO; GO:0070072; P:vacuolar proton-transporting V-type ATPase complex assembly; IBA:GO_Central.
InterPro; IPR002490; V-ATPase_116kDa_su.
InterPro; IPR026028; V-type_ATPase_116kDa_su_euka.
PANTHER; PTHR11629; PTHR11629; 1.
Pfam; PF01496; V_ATPase_I; 1.
PIRSF; PIRSF001293; ATP6V0A1; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Hydrogen ion transport;
Ion transport; Membrane; Reference proteome; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 833 V-type proton ATPase 116 kDa subunit a
isoform 4.
/FTId=PRO_0000119220.
TOPO_DOM 1 390 Cytoplasmic. {ECO:0000255}.
TRANSMEM 391 409 Helical. {ECO:0000255}.
TOPO_DOM 410 411 Vacuolar. {ECO:0000255}.
TRANSMEM 412 428 Helical. {ECO:0000255}.
TOPO_DOM 429 443 Cytoplasmic. {ECO:0000255}.
TRANSMEM 444 473 Helical. {ECO:0000255}.
TOPO_DOM 474 538 Vacuolar. {ECO:0000255}.
TRANSMEM 539 558 Helical. {ECO:0000255}.
TOPO_DOM 559 576 Cytoplasmic. {ECO:0000255}.
TRANSMEM 577 597 Helical. {ECO:0000255}.
TOPO_DOM 598 642 Vacuolar. {ECO:0000255}.
TRANSMEM 643 662 Helical. {ECO:0000255}.
TOPO_DOM 663 720 Cytoplasmic. {ECO:0000255}.
TRANSMEM 721 745 Helical. {ECO:0000255}.
TOPO_DOM 746 766 Vacuolar. {ECO:0000255}.
TRANSMEM 767 805 Helical. {ECO:0000255}.
TOPO_DOM 806 833 Cytoplasmic. {ECO:0000255}.
CONFLICT 4 4 V -> A (in Ref. 3; AAN45855).
{ECO:0000305}.
CONFLICT 161 161 T -> A (in Ref. 2; AAL30435).
{ECO:0000305}.
CONFLICT 625 625 D -> N (in Ref. 3; AAN45855).
{ECO:0000305}.
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


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