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V-type proton ATPase subunit S1 (V-ATPase subunit S1) (Protein XAP-3) (V-ATPase Ac45 subunit) (V-ATPase S1 accessory protein) (Vacuolar proton pump subunit S1)

 VAS1_HUMAN              Reviewed;         470 AA.
Q15904; A6ZKI4; Q8NBT4; Q9H0C7;
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
11-JAN-2001, sequence version 2.
22-NOV-2017, entry version 174.
RecName: Full=V-type proton ATPase subunit S1;
Short=V-ATPase subunit S1;
AltName: Full=Protein XAP-3;
AltName: Full=V-ATPase Ac45 subunit;
AltName: Full=V-ATPase S1 accessory protein;
AltName: Full=Vacuolar proton pump subunit S1;
Flags: Precursor;
Name=ATP6AP1; Synonyms=ATP6IP1, ATP6S1, VATPS1, XAP3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
PubMed=8733135; DOI=10.1093/hmg/5.5.659;
Chen E.Y., Zollo M., Mazzarella R.A., Ciccodicola A., Chen C.-N.,
Zuo L., Heiner C., Burough F.W., Ripetto M., Schlessinger D.,
D'Urso M.;
"Long-range sequence analysis in Xq28: thirteen known and six
candidate genes in 219.4 kb of high GC DNA between the RCP/GCP and
G6PD loci.";
Hum. Mol. Genet. 5:659-668(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
PubMed=11230166; DOI=10.1101/gr.GR1547R;
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
Wambutt R., Korn B., Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and
analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=16303743; DOI=10.1093/dnares/12.2.117;
Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
Isogai T.;
"Signal sequence and keyword trap in silico for selection of full-
length human cDNAs encoding secretion or membrane proteins from oligo-
capped cDNA libraries.";
DNA Res. 12:117-126(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
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).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 97-470.
TISSUE=Brain;
PubMed=8034313; DOI=10.1006/geno.1994.1194;
Yokoi H., Hadano S., Kogi M., Kang X., Wakasa K., Ikeda J.;
"Isolation of expressed sequences encoded by the human Xq terminal
portion using microclone probes generated by laser microdissection.";
Genomics 20:404-411(1994).
[9]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-261 AND ASN-273.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-465, 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).
[12]
INVOLVEMENT IN IMD47, VARIANTS IMD47 PRO-144; CYS-313; LYS-346 AND
ILE-428, CHARACTERIZATION OF VARIANTS IMD47 CYS-313; LYS-346 AND
ILE-428, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION, AND
MUTAGENESIS OF VAL-470.
PubMed=27231034; DOI=10.1038/ncomms11600;
Jansen E.J., Timal S., Ryan M., Ashikov A., van Scherpenzeel M.,
Graham L.A., Mandel H., Hoischen A., Iancu T.C., Raymond K.,
Steenbergen G., Gilissen C., Huijben K., van Bakel N.H., Maeda Y.,
Rodenburg R.J., Adamowicz M., Crushell E., Koenen H., Adams D.,
Vodopiutz J., Greber-Platzer S., Mueller T., Dueckers G., Morava E.,
Sykut-Cegielska J., Martens G.J., Wevers R.A., Niehues T.,
Huynen M.A., Veltman J.A., Stevens T.H., Lefeber D.J.;
"ATP6AP1 deficiency causes an immunodeficiency with hepatopathy,
cognitive impairment and abnormal protein glycosylation.";
Nat. Commun. 7:11600-11600(2016).
[13]
FUNCTION.
PubMed=28296633; DOI=10.7554/eLife.22693;
Miles A.L., Burr S.P., Grice G.L., Nathan J.A.;
"The vacuolar-ATPase complex and assembly factors, TMEM199 and
CCDC115, control HIF1alpha prolyl hydroxylation by regulating cellular
iron levels.";
Elife 6:E22693-E22693(2017).
-!- FUNCTION: Accessory subunit of the proton-transporting vacuolar
(V)-ATPase protein pump, which is required for luminal
acidification of secretory vesicles. Guides the V-type ATPase into
specialized subcellular compartments, such as neuroendocrine
regulated secretory vesicles or the ruffled border of the
osteoclast, thereby regulating its activity. Involved in membrane
trafficking and Ca(2+)-dependent membrane fusion. May play a role
in the assembly of the V-type ATPase complex. In aerobic
conditions, involved in intracellular iron homeostasis, thus
triggering the activity of Fe(2+) prolyl hydroxylase (PHD)
enzymes, and leading to HIF1A hydroxylation and subsequent
proteasomal degradation (PubMed:28296633).
{ECO:0000269|PubMed:28296633, ECO:0000305|PubMed:27231034}.
-!- SUBUNIT: Accessory component of the multisubunit proton-
transporting vacuolar (V)-ATPase protein pump.
{ECO:0000305|PubMed:27231034}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:27231034}; Single-pass membrane protein
{ECO:0000305}. Endoplasmic reticulum-Golgi intermediate
compartment membrane {ECO:0000269|PubMed:27231034}. Note=Not
detected in trans-Golgi network. {ECO:0000269|PubMed:27231034}.
-!- TISSUE SPECIFICITY: widely expressed, with highest levels in brain
and lowest in liver and duodenum. {ECO:0000269|PubMed:27231034}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:27231034}.
-!- DISEASE: Immunodeficiency 47 (IMD47) [MIM:300972]: A complex
immunodeficiency syndrome characterized by hypogammaglobulinemia,
recurrent bacterial infections, defective glycosylation of serum
proteins, and liver disease with neonatal jaundice and
hepatosplenomegaly. Some patients may also have neurologic
features, including seizures, mild intellectual disability, and
behavioral abnormalities. Inheritance is X-linked recessive.
{ECO:0000269|PubMed:27231034}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the vacuolar ATPase subunit S1 family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA03938.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAB66785.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; L44140; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL136851; CAB66785.1; ALT_INIT; mRNA.
EMBL; AK026519; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AK289452; BAF82141.1; -; mRNA.
EMBL; AK075284; BAC11520.1; -; mRNA.
EMBL; BX936347; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BX936385; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471172; EAW72715.1; -; Genomic_DNA.
EMBL; BC000724; AAH00724.1; -; mRNA.
EMBL; D16469; BAA03938.1; ALT_INIT; mRNA.
CCDS; CCDS35451.1; -.
RefSeq; NP_001174.2; NM_001183.5.
RefSeq; XP_011529481.1; XM_011531179.1.
UniGene; Hs.633817; -.
UniGene; Hs.6551; -.
ProteinModelPortal; Q15904; -.
SMR; Q15904; -.
BioGrid; 107019; 39.
IntAct; Q15904; 24.
MINT; MINT-4722342; -.
STRING; 9606.ENSP00000358777; -.
BindingDB; Q15904; -.
ChEMBL; CHEMBL4790; -.
iPTMnet; Q15904; -.
PhosphoSitePlus; Q15904; -.
BioMuta; ATP6AP1; -.
DMDM; 12230759; -.
EPD; Q15904; -.
MaxQB; Q15904; -.
PaxDb; Q15904; -.
PeptideAtlas; Q15904; -.
PRIDE; Q15904; -.
DNASU; 537; -.
Ensembl; ENST00000369762; ENSP00000358777; ENSG00000071553.
GeneID; 537; -.
KEGG; hsa:537; -.
UCSC; uc004flf.3; human.
CTD; 537; -.
DisGeNET; 537; -.
EuPathDB; HostDB:ENSG00000071553.16; -.
GeneCards; ATP6AP1; -.
HGNC; HGNC:868; ATP6AP1.
HPA; CAB015218; -.
MalaCards; ATP6AP1; -.
MIM; 300197; gene.
MIM; 300972; phenotype.
neXtProt; NX_Q15904; -.
OpenTargets; ENSG00000071553; -.
PharmGKB; PA25145; -.
eggNOG; KOG3868; Eukaryota.
eggNOG; ENOG410XTHY; LUCA.
GeneTree; ENSGT00530000063584; -.
HOGENOM; HOG000000706; -.
HOVERGEN; HBG001090; -.
InParanoid; Q15904; -.
KO; K03662; -.
OMA; HITSDMQ; -.
OrthoDB; EOG091G0772; -.
PhylomeDB; Q15904; -.
TreeFam; TF325819; -.
BioCyc; MetaCyc:HS01034-MONOMER; -.
Reactome; R-HSA-77387; Insulin receptor recycling.
Reactome; R-HSA-917977; Transferrin endocytosis and recycling.
Reactome; R-HSA-983712; Ion channel transport.
ChiTaRS; ATP6AP1; human.
GeneWiki; ATP6AP1; -.
GenomeRNAi; 537; -.
PRO; PR:Q15904; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000071553; -.
CleanEx; HS_ATP6AP1; -.
ExpressionAtlas; Q15904; baseline and differential.
Genevisible; Q15904; HS.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
GO; GO:0010008; C:endosome membrane; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016469; C:proton-transporting two-sector ATPase complex; TAS:ProtInc.
GO; GO:0033180; C:proton-transporting V-type ATPase, V1 domain; IEA:InterPro.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
GO; GO:0017137; F:Rab GTPase binding; ISS:UniProtKB.
GO; GO:0005215; F:transporter activity; TAS:ProtInc.
GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
GO; GO:0006879; P:cellular iron ion homeostasis; IMP:UniProtKB.
GO; GO:0036295; P:cellular response to increased oxygen levels; IMP:UniProtKB.
GO; GO:0051656; P:establishment of organelle localization; ISS:UniProtKB.
GO; GO:0008286; P:insulin receptor signaling pathway; TAS:Reactome.
GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
GO; GO:0045851; P:pH reduction; ISS:UniProtKB.
GO; GO:0045780; P:positive regulation of bone resorption; ISS:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
GO; GO:0045921; P:positive regulation of exocytosis; ISS:UniProtKB.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISS:UniProtKB.
GO; GO:2001206; P:positive regulation of osteoclast development; ISS:UniProtKB.
GO; GO:0015992; P:proton transport; TAS:ProtInc.
GO; GO:0033572; P:transferrin transport; TAS:Reactome.
InterPro; IPR008388; ATPase_V1-cplx_s1su.
PANTHER; PTHR12471; PTHR12471; 1.
Pfam; PF05827; ATP-synt_S1; 1.
1: Evidence at protein level;
ATP-binding; Complete proteome; Disease mutation;
Endoplasmic reticulum; Glycoprotein; Hydrogen ion transport;
Ion transport; Membrane; Nucleotide-binding; Phosphoprotein;
Reference proteome; Signal; Transmembrane; Transmembrane helix;
Transport.
SIGNAL 1 41 {ECO:0000255}.
CHAIN 42 470 V-type proton ATPase subunit S1.
/FTId=PRO_0000002543.
TOPO_DOM 42 419 Vacuolar. {ECO:0000255}.
TRANSMEM 420 440 Helical. {ECO:0000255}.
TOPO_DOM 441 470 Cytoplasmic. {ECO:0000255}.
MOD_RES 465 465 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CARBOHYD 170 170 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 261 261 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 273 273 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 296 296 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 303 303 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 350 350 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 357 357 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VARIANT 144 144 L -> P (in IMD47; dbSNP:rs878853276).
{ECO:0000269|PubMed:27231034}.
/FTId=VAR_077021.
VARIANT 313 313 Y -> C (in IMD47; probable loss of
proton-transporting V-type ATPase complex
assembly in yeast; unable to restore V-
ATPase-dependent growth in Voa1 mutant
yeast; dbSNP:rs878853278).
{ECO:0000269|PubMed:27231034}.
/FTId=VAR_077022.
VARIANT 346 346 E -> K (in IMD47; probable loss of
proton-transporting V-type ATPase complex
assembly in yeast; unable to restore V-
ATPase-dependent growth in Voa1 mutant
yeast; dbSNP:rs878853277).
{ECO:0000269|PubMed:27231034}.
/FTId=VAR_077023.
VARIANT 428 428 M -> I (in IMD47; restores V-ATPase-
dependent growth in Voa1 mutant yeast;
dbSNP:rs878853275).
{ECO:0000269|PubMed:27231034}.
/FTId=VAR_077024.
MUTAGEN 470 470 V->VKKNN: Retained in the endoplasmic
reticulum when transfected into yeast
cells. Restores V-ATPase-dependent growth
in Voa1 mutant yeast.
{ECO:0000269|PubMed:27231034}.
CONFLICT 68 68 I -> V (in Ref. 4; BAC11520).
{ECO:0000305}.
CONFLICT 74 74 L -> P (in Ref. 4; BAC11520).
{ECO:0000305}.
CONFLICT 229 229 V -> A (in Ref. 3; AK026519).
{ECO:0000305}.
CONFLICT 307 307 A -> T (in Ref. 3; AK026519).
{ECO:0000305}.
CONFLICT 335 335 S -> F (in Ref. 3; AK026519).
{ECO:0000305}.
SEQUENCE 470 AA; 52026 MW; A71C7EF0E90D0652 CRC64;
MMAAMATARV RMGPRCAQAL WRMPWLPVFL SLAAAAAAAA AEQQVPLVLW SSDRDLWAPA
ADTHEGHITS DLQLSTYLDP ALELGPRNVL LFLQDKLSIE DFTAYGGVFG NKQDSAFSNL
ENALDLAPSS LVLPAVDWYA VSTLTTYLQE KLGASPLHVD LATLRELKLN ASLPALLLIR
LPYTASSGLM APREVLTGND EVIGQVLSTL KSEDVPYTAA LTAVRPSRVA RDVAVVAGGL
GRQLLQKQPV SPVIHPPVSY NDTAPRILFW AQNFSVAYKD QWEDLTPLTF GVQELNLTGS
FWNDSFARLS LTYERLFGTT VTFKFILANR LYPVSARHWF TMERLEVHSN GSVAYFNASQ
VTGPSIYSFH CEYVSSLSKK GSLLVARTQP SPWQMMLQDF QIQAFNVMGE QFSYASDCAS
FFSPGIWMGL LTSLFMLFIF TYGLHMILSL KTMDRFDDHK GPTISLTQIV


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