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V-type proton ATPase 116 kDa subunit a isoform 1 (V-ATPase 116 kDa isoform a1) (Clathrin-coated vesicle/synaptic vesicle proton pump 116 kDa subunit) (Vacuolar adenosine triphosphatase subunit Ac116) (Vacuolar proton pump subunit 1) (Vacuolar proton translocating ATPase 116 kDa subunit a isoform 1)

 VPP1_HUMAN              Reviewed;         837 AA.
Q93050; B7Z3B7; Q8N5G7; Q9NSX0;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
15-FEB-2005, sequence version 3.
25-OCT-2017, entry version 161.
RecName: Full=V-type proton ATPase 116 kDa subunit a isoform 1;
Short=V-ATPase 116 kDa isoform a1;
AltName: Full=Clathrin-coated vesicle/synaptic vesicle proton pump 116 kDa subunit;
AltName: Full=Vacuolar adenosine triphosphatase subunit Ac116;
AltName: Full=Vacuolar proton pump subunit 1;
AltName: Full=Vacuolar proton translocating ATPase 116 kDa subunit a isoform 1;
Name=ATP6V0A1; Synonyms=ATP6N1, ATP6N1A, VPP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Pancreas;
Fehr C.N., Gillies R.J., Wang H.-Y., Ullrich A.;
"Sequence and alternative splicing in human 115 kDa subunit of
vacuolar-type H(+)-ATPase.";
Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Hippocampus, and Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 675-837 (ISOFORM 2).
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[7]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Melanoma;
PubMed=12643545; DOI=10.1021/pr025562r;
Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K.,
Valencia J., Muller J., Vieira W.D., Watabe H., Shabanowitz J.,
Hearing V.J., Hunt D.F., Appella E.;
"Proteomic analysis of early melanosomes: identification of novel
melanosomal proteins.";
J. Proteome Res. 2:69-79(2003).
[8]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Melanoma;
PubMed=17081065; DOI=10.1021/pr060363j;
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
Hunt D.F.;
"Proteomic and bioinformatic characterization of the biogenesis and
function of melanosomes.";
J. Proteome Res. 5:3135-3144(2006).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-360, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[11]
INTERACTION WITH SPAAR.
PubMed=28024296; DOI=10.1038/nature21034;
Matsumoto A., Pasut A., Matsumoto M., Yamashita R., Fung J.,
Monteleone E., Saghatelian A., Nakayama K.I., Clohessy J.G.,
Pandolfi P.P.;
"mTORC1 and muscle regeneration are regulated by the LINC00961-encoded
SPAR polypeptide.";
Nature 541:228-232(2017).
-!- FUNCTION: Required for assembly and activity of the vacuolar
ATPase. Potential role in differential targeting and regulation of
the enzyme for a specific organelle (By similarity).
{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''. Interacts with SPAAR
(PubMed:28024296). {ECO:0000269|PubMed:28024296}.
-!- INTERACTION:
P07195:LDHB; NbExp=2; IntAct=EBI-2891238, EBI-358748;
-!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Multi-pass
membrane protein. Melanosome. Note=Coated vesicle. Identified by
mass spectrometry in melanosome fractions from stage I to stage
IV.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=I;
IsoId=Q93050-2; Sequence=Displayed;
Name=2; Synonyms=II;
IsoId=Q93050-1; Sequence=VSP_012814;
Name=3;
IsoId=Q93050-3; Sequence=VSP_043532, VSP_012814;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family.
{ECO:0000305}.
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EMBL; Z71460; CAA96077.1; -; mRNA.
EMBL; AK295682; BAH12153.1; -; mRNA.
EMBL; AK316305; BAH14676.1; -; mRNA.
EMBL; AC067852; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC107993; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471152; EAW60830.1; -; Genomic_DNA.
EMBL; BC032398; AAH32398.1; -; mRNA.
EMBL; AL137683; CAB70874.1; -; mRNA.
CCDS; CCDS11426.1; -. [Q93050-1]
CCDS; CCDS45683.1; -. [Q93050-3]
CCDS; CCDS45684.1; -. [Q93050-2]
PIR; T46449; T46449.
RefSeq; NP_001123492.1; NM_001130020.1. [Q93050-3]
RefSeq; NP_001123493.1; NM_001130021.1. [Q93050-2]
RefSeq; NP_005168.2; NM_005177.3. [Q93050-1]
UniGene; Hs.463074; -.
ProteinModelPortal; Q93050; -.
BioGrid; 107018; 84.
IntAct; Q93050; 31.
MINT; MINT-3049850; -.
STRING; 9606.ENSP00000264649; -.
TCDB; 3.A.2.2.4; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
iPTMnet; Q93050; -.
PhosphoSitePlus; Q93050; -.
SwissPalm; Q93050; -.
BioMuta; ATP6V0A1; -.
DMDM; 59803038; -.
PaxDb; Q93050; -.
PeptideAtlas; Q93050; -.
PRIDE; Q93050; -.
Ensembl; ENST00000264649; ENSP00000264649; ENSG00000033627. [Q93050-3]
Ensembl; ENST00000343619; ENSP00000342951; ENSG00000033627. [Q93050-2]
Ensembl; ENST00000393829; ENSP00000377415; ENSG00000033627. [Q93050-1]
GeneID; 535; -.
KEGG; hsa:535; -.
UCSC; uc002hzq.4; human. [Q93050-2]
CTD; 535; -.
DisGeNET; 535; -.
EuPathDB; HostDB:ENSG00000033627.14; -.
GeneCards; ATP6V0A1; -.
H-InvDB; HIX0013842; -.
HGNC; HGNC:865; ATP6V0A1.
HPA; HPA022144; -.
MIM; 192130; gene.
neXtProt; NX_Q93050; -.
OpenTargets; ENSG00000033627; -.
PharmGKB; PA25146; -.
eggNOG; KOG2189; Eukaryota.
eggNOG; COG1269; LUCA.
GeneTree; ENSGT00390000004941; -.
HOGENOM; HOG000037059; -.
HOVERGEN; HBG014606; -.
InParanoid; Q93050; -.
KO; K02154; -.
OMA; WTAYDAH; -.
OrthoDB; EOG091G01BI; -.
PhylomeDB; Q93050; -.
TreeFam; TF300346; -.
BioCyc; MetaCyc:ENSG00000033627-MONOMER; -.
Reactome; R-HSA-1222556; ROS, RNS production in phagocytes.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-77387; Insulin receptor recycling.
Reactome; R-HSA-917977; Transferrin endocytosis and recycling.
Reactome; R-HSA-983712; Ion channel transport.
ChiTaRS; ATP6V0A1; human.
GeneWiki; ATPase,_H%2B_transporting,_lysosomal_V0_subunit_a1; -.
GenomeRNAi; 535; -.
PRO; PR:Q93050; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000033627; -.
CleanEx; HS_ATP6V0A1; -.
ExpressionAtlas; Q93050; baseline and differential.
Genevisible; Q93050; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0010008; C:endosome membrane; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005765; C:lysosomal membrane; TAS:ParkinsonsUK-UCL.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0016607; C:nuclear speck; IDA:HPA.
GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IBA:GO_Central.
GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
GO; GO:0051117; F:ATPase binding; IPI:UniProtKB.
GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IBA:GO_Central.
GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
GO; GO:0015986; P:ATP synthesis coupled proton transport; IBA:GO_Central.
GO; GO:0008286; P:insulin receptor signaling pathway; TAS:Reactome.
GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0090383; P:phagosome acidification; TAS:Reactome.
GO; GO:0016241; P:regulation of macroautophagy; IMP:ParkinsonsUK-UCL.
GO; GO:1901998; P:toxin transport; IEA:Ensembl.
GO; GO:0033572; P:transferrin transport; TAS:Reactome.
GO; GO:0007035; P:vacuolar acidification; TAS:ParkinsonsUK-UCL.
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;
Alternative splicing; Complete proteome; Cytoplasmic vesicle;
Hydrogen ion transport; Ion transport; Membrane; Phosphoprotein;
Reference proteome; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 837 V-type proton ATPase 116 kDa subunit a
isoform 1.
/FTId=PRO_0000119211.
TOPO_DOM 1 388 Cytoplasmic. {ECO:0000255}.
TRANSMEM 389 407 Helical. {ECO:0000255}.
TOPO_DOM 408 409 Vacuolar. {ECO:0000255}.
TRANSMEM 410 426 Helical. {ECO:0000255}.
TOPO_DOM 427 441 Cytoplasmic. {ECO:0000255}.
TRANSMEM 442 471 Helical. {ECO:0000255}.
TOPO_DOM 472 534 Vacuolar. {ECO:0000255}.
TRANSMEM 535 554 Helical. {ECO:0000255}.
TOPO_DOM 555 572 Cytoplasmic. {ECO:0000255}.
TRANSMEM 573 593 Helical. {ECO:0000255}.
TOPO_DOM 594 638 Vacuolar. {ECO:0000255}.
TRANSMEM 639 658 Helical. {ECO:0000255}.
TOPO_DOM 659 724 Cytoplasmic. {ECO:0000255}.
TRANSMEM 725 749 Helical. {ECO:0000255}.
TOPO_DOM 750 770 Vacuolar. {ECO:0000255}.
TRANSMEM 771 809 Helical. {ECO:0000255}.
TOPO_DOM 810 837 Cytoplasmic. {ECO:0000255}.
MOD_RES 250 250 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9Z1G4}.
MOD_RES 360 360 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 364 364 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9Z1G4}.
VAR_SEQ 141 141 E -> EAELHHQQ (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043532.
VAR_SEQ 705 710 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:17974005,
ECO:0000303|Ref.1}.
/FTId=VSP_012814.
CONFLICT 750 751 QL -> HV (in Ref. 1; CAA96077).
{ECO:0000305}.
SEQUENCE 837 AA; 96413 MW; 80E4842CF6ADEE44 CRC64;
MGELFRSEEM TLAQLFLQSE AAYCCVSELG ELGKVQFRDL NPDVNVFQRK FVNEVRRCEE
MDRKLRFVEK EIRKANIPIM DTGENPEVPF PRDMIDLEAN FEKIENELKE INTNQEALKR
NFLELTELKF ILRKTQQFFD EMADPDLLEE SSSLLEPSEM GRGTPLRLGF VAGVINRERI
PTFERMLWRV CRGNVFLRQA EIENPLEDPV TGDYVHKSVF IIFFQGDQLK NRVKKICEGF
RASLYPCPET PQERKEMASG VNTRIDDLQM VLNQTEDHRQ RVLQAAAKNI RVWFIKVRKM
KAIYHTLNLC NIDVTQKCLI AEVWCPVTDL DSIQFALRRG TEHSGSTVPS ILNRMQTNQT
PPTYNKTNKF TYGFQNIVDA YGIGTYREIN PAPYTIITFP FLFAVMFGDF GHGILMTLFA
VWMVLRESRI LSQKNENEMF STVFSGRYII LLMGVFSMYT GLIYNDCFSK SLNIFGSSWS
VRPMFTYNWT EETLRGNPVL QLNPALPGVF GGPYPFGIDP IWNIATNKLT FLNSFKMKMS
VILGIIHMLF GVSLSLFNHI YFKKPLNIYF GFIPEIIFMT SLFGYLVILI FYKWTAYDAH
TSENAPSLLI HFINMFLFSY PESGYSMLYS GQKGIQCFLV VVALLCVPWM LLFKPLVLRR
QYLRRKHLGT LNFGGIRVGN GPTEEDAEII QHDQLSTHSE DADEPSEDEV FDFGDTMVHQ
AIHTIEYCLG CISNTASYLR LWALSLAHAQ LSEVLWTMVI HIGLSVKSLA GGLVLFFFFT
AFATLTVAIL LIMEGLSAFL HALRLHWVEF QNKFYSGTGF KFLPFSFEHI REGKFEE


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EIAAB45913 ATP6N1B,ATP6N2,ATP6V0A4,Homo sapiens,Human,Vacuolar proton translocating ATPase 116 kDa subunit a isoform 4,Vacuolar proton translocating ATPase 116 kDa subunit a kidney isoform,V-ATPase 116 kDa isofo
EIAAB45692 ATP6V1H,Bos taurus,Bovine,Vacuolar proton pump subunit H,Vacuolar proton pump subunit SFD,V-ATPase 50_57 kDa subunits,V-ATPase subunit H,V-type proton ATPase subunit H
EIAAB45909 ATP6V0A2,Homo sapiens,Human,Lysosomal H(+)-transporting ATPase V0 subunit a2,TJ6,Vacuolar proton translocating ATPase 116 kDa subunit a isoform 2,V-ATPase 116 kDa isoform a2,V-type proton ATPase 116 k
EIAAB45693 ATP6V1H,Pig,Sus scrofa,Vacuolar proton pump subunit H,Vacuolar proton pump subunit SFD,V-ATPase 50_57 kDa subunits,V-ATPase subunit H,V-type proton ATPase subunit H
EIAAB45914 Atp6n1b,Atp6v0a4,Mouse,Mus musculus,Vacuolar proton translocating ATPase 116 kDa subunit a isoform 4,Vacuolar proton translocating ATPase 116 kDa subunit a kidney isoform,V-ATPase 116 kDa isoform a4,V
15-288-22820 Vacuolar ATP synthase catalytic subunit A. ubiquitous isoform - EC 3.6.3.14; V-ATPase subunit A 1; Vacuolar proton pump alpha subunit 1; V-ATPase 69 kDa subunit 1; Isoform VA68 Polyclonal 0.05 mg
15-288-22820 Vacuolar ATP synthase catalytic subunit A. ubiquitous isoform - EC 3.6.3.14; V-ATPase subunit A 1; Vacuolar proton pump alpha subunit 1; V-ATPase 69 kDa subunit 1; Isoform VA68 Polyclonal 0.1 mg
EIAAB45911 ATP6N1B,ATP6V0A2,Bos taurus,Bovine,Vacuolar proton translocating ATPase 116 kDa subunit a isoform 2,V-ATPase 116 kDa isoform a2,V-type proton ATPase 116 kDa subunit a isoform 2
EIAAB45573 ATP6H,ATP6V0E,ATP6V0E1,Homo sapiens,Human,Vacuolar proton pump subunit e 1,V-ATPase 9.2 kDa membrane accessory protein,V-ATPase M9.2 subunit,V-ATPase subunit e 1,V-type proton ATPase subunit e 1
EIAAB45570 ATP6H,ATP6V0E,ATP6V0E1,Bos taurus,Bovine,Vacuolar proton pump subunit e 1,V-ATPase 9.2 kDa membrane accessory protein,V-ATPase M9.2 subunit,V-ATPase subunit e 1,V-type proton ATPase subunit e 1
EIAAB45629 ATP6AP1,ATP6IP1,ATP6S1,Bos taurus,Bovine,Vacuolar proton pump subunit S1,V-ATPase Ac45 subunit,V-ATPase S1 accessory protein,V-ATPase subunit S1,V-type proton ATPase subunit S1
EIAAB45562 Atp6d,Atp6v0d1,Mouse,Mus musculus,P39,Physophilin,Vacuolar proton pump subunit d 1,V-ATPase 40 kDa accessory protein,V-ATPase AC39 subunit,V-ATPase subunit d 1,V-type proton ATPase subunit d 1


 

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