ID   VAS1_CAEEL              Reviewed;         451 AA.
AC   Q9TYW1;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=V-type proton ATPase subunit S1 {ECO:0000305};
DE            Short=V-ATPase subunit S1 {ECO:0000305};
DE   AltName: Full=V-ATPase Ac45 subunit {ECO:0000305};
DE   Flags: Precursor;
GN   Name=vha-19 {ECO:0000312|WormBase:Y55H10A.1};
GN   ORFNames=Y55H10A.1 {ECO:0000312|WormBase:Y55H10A.1};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN   [1] {ECO:0000312|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2] {ECO:0000305}
RP   FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=22768351; DOI=10.1371/journal.pone.0040317;
RA   Knight A.J., Johnson N.M., Behm C.A.;
RT   "VHA-19 is essential in Caenorhabditis elegans oocytes for embryogenesis
RT   and is involved in trafficking in oocytes.";
RL   PLoS ONE 7:e40317-e40317(2012).
CC   -!- FUNCTION: Accessory subunit of the proton-transporting vacuolar (V)-
CC       ATPase protein pump, which is required for luminal acidification of
CC       secretory vesicles (By similarity). In the germline, required for the
CC       trafficking of the receptor RME-2 to the oocyte cell membrane where it
CC       regulates the uptake of yolk proteins (PubMed:22768351). Also, plays an
CC       essential role in osmoregulation in the embryo, probably by regulating
CC       the proper formation of the eggshell (PubMed:22768351).
CC       {ECO:0000250|UniProtKB:Q15904, ECO:0000269|PubMed:22768351}.
CC   -!- SUBUNIT: Accessory component of the multisubunit proton-transporting
CC       vacuolar (V)-ATPase protein pump. {ECO:0000250|UniProtKB:Q15904}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Expressed in pharynx, hypodermis, intestine, vulval
CC       hypodermis and the H-shape excretory cell.
CC       {ECO:0000269|PubMed:22768351}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in larvae and adults.
CC       {ECO:0000269|PubMed:22768351}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown at the L1 larval stage
CC       causes arrest followed by death at the L3/L4 larval stages
CC       (PubMed:22768351). RNAi-mediated knockdown at the L4 larval stage does
CC       not affect development into adults (PubMed:22768351). However, only 26%
CC       of the progeny hatched into larvae which die at the L3 larval stage.
CC       RNAi-mediated knockdown at the L4 larval stage or in the germline
CC       causes egg compression in their uterus (PubMed:22768351). Fewer oocytes
CC       are produced in the oviduct and are endomitotic (PubMed:22768351). This
CC       results in a reduced rate of ovulation over time (PubMed:22768351).
CC       Oocytes fail to endocytose vitellogenin due to a failure to traffic
CC       receptor rme-2 to the cell membrane (PubMed:22768351). Also, embryos
CC       display osmotic sensitivity and defect in osmoregulation and
CC       cytokinesis probably due to an abnormal eggshell (PubMed:22768351).
CC       {ECO:0000269|PubMed:22768351}.
CC   -!- SIMILARITY: Belongs to the vacuolar ATPase subunit S1 family.
CC       {ECO:0000305}.
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DR   EMBL; BX284604; CCD62204.1; -; Genomic_DNA.
DR   PIR; T33763; T33763.
DR   RefSeq; NP_500332.1; NM_067931.4.
DR   AlphaFoldDB; Q9TYW1; -.
DR   STRING; 6239.Y55H10A.1; -.
DR   TCDB; 8.A.107.1.4; the v-type atpase assembly factor, atp6ap1 (atp6ap1) family.
DR   EPD; Q9TYW1; -.
DR   PaxDb; Q9TYW1; -.
DR   PeptideAtlas; Q9TYW1; -.
DR   EnsemblMetazoa; Y55H10A.1.1; Y55H10A.1.1; WBGene00021952.
DR   GeneID; 177103; -.
DR   KEGG; cel:CELE_Y55H10A.1; -.
DR   UCSC; Y55H10A.1; c. elegans.
DR   CTD; 177103; -.
DR   WormBase; Y55H10A.1; CE19628; WBGene00021952; vha-19.
DR   eggNOG; KOG3868; Eukaryota.
DR   GeneTree; ENSGT00940000170675; -.
DR   HOGENOM; CLU_627482_0_0_1; -.
DR   InParanoid; Q9TYW1; -.
DR   OMA; SVQTMDR; -.
DR   OrthoDB; 925129at2759; -.
DR   Reactome; R-CEL-77387; Insulin receptor recycling.
DR   Reactome; R-CEL-917977; Transferrin endocytosis and recycling.
DR   Reactome; R-CEL-983712; Ion channel transport.
DR   PRO; PR:Q9TYW1; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00021952; Expressed in larva and 4 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045121; C:membrane raft; HDA:WormBase.
DR   GO; GO:0033176; C:proton-transporting V-type ATPase complex; IBA:GO_Central.
DR   GO; GO:0009992; P:cellular water homeostasis; IMP:UniProtKB.
DR   GO; GO:0060282; P:positive regulation of oocyte development; IMP:UniProtKB.
DR   GO; GO:0090314; P:positive regulation of protein targeting to membrane; IMP:UniProtKB.
DR   GO; GO:0030641; P:regulation of cellular pH; IBA:GO_Central.
DR   InterPro; IPR008388; Ac45_acc_su.
DR   PANTHER; PTHR12471; PTHR12471; 1.
DR   Pfam; PF05827; ATP-synt_S1; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Membrane; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..451
FT                   /note="V-type proton ATPase subunit S1"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5004338122"
FT   PROPEP          17..?
FT                   /evidence="ECO:0000250|UniProtKB:Q9R1Q9"
FT                   /id="PRO_0000454047"
FT   TOPO_DOM        17..407
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        408..428
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        429..451
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   CARBOHYD        191
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        235
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        249
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        330
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   451 AA;  49609 MW;  A4B6A18903EBE0DE CRC64;
     MRVLFAVFSL IMACQAYDAV LFSNSREIGG TPAAKLVESA TAEEPVVFIV NPDFTLGQFS
     VKANAYTSEP SADYLAKSVK NSNFHESQYF SHQIEATQAQ WLSSADQYSA GSPIYIIYGE
     EWTSMEQLAE QLISKIDNSV GIITSTDAVA HEKSSRVKRV ATDEFNSDSE NSAAAEANGG
     FPFPLVIPPY NQTFYSVKPT NGHSCLFYLE GLTVVVEQKK EKVLYYANAY IPGSNFTWAY
     SETDVTCPNG TIGDFIFKIH LTLENDITGM QGTSKKAFTM KKGDKIDFDL TFTGDLFGYW
     ALNKASASNL AISGYDPYKS ASVDGSKVVN GSATQYTKLN SVAGWSLACG QSQAVFFPTN
     EQSVRIGVAL MNTQIQLFNY QNPEKWVESA HFTLQTEDCT GTFSSGSWMG IVSALVLIAG
     LMFGYVMLQS VQTMDRFDDP KQRQIVINVR E