VPP4_CAEEL
ID VPP4_CAEEL Reviewed; 1210 AA.
AC B2MZD0; A0A0K3AXB9; G5EDH1;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=V-type proton ATPase 116 kDa subunit a 4 {ECO:0000305};
DE Short=V-ATPase 116 kDa isoform a 4 {ECO:0000305};
GN Name=vha-7 {ECO:0000303|PubMed:11441002, ECO:0000312|WormBase:C26H9A.1b};
GN ORFNames=C26H9A.1 {ECO:0000312|WormBase:C26H9A.1b};
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|EMBL:BAB62293.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=11441002; DOI=10.1074/jbc.m101652200;
RA Oka T., Toyomura T., Honjo K., Wada Y., Futai M.;
RT "Four subunit a isoforms of Caenorhabditis elegans vacuolar H+-ATPase.
RT Cell-specific expression during development.";
RL J. Biol. Chem. 276:33079-33085(2001).
RN [2] {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).
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).
CC {ECO:0000250|UniProtKB:G5EGP4, ECO:0000250|UniProtKB:Q29466}.
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 vah-19/Ac45 and vah-20/PRR (By similarity).
CC {ECO:0000250|UniProtKB:Q29466}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=b {ECO:0000312|WormBase:C26H9A.1b};
CC IsoId=B2MZD0-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:C26H9A.1a};
CC IsoId=B2MZD0-2; Sequence=VSP_061243;
CC Name=c {ECO:0000312|WormBase:C26H9A.1c};
CC IsoId=B2MZD0-3; Sequence=VSP_061244, VSP_061245;
CC -!- TISSUE SPECIFICITY: Expressed in uterus. {ECO:0000269|PubMed:11441002}.
CC -!- DEVELOPMENTAL STAGE: Expressed in hypodermal cells in L1 larvae
CC (PubMed:11441002). No expressed in embryos (PubMed:11441002).
CC {ECO:0000269|PubMed:11441002}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown does not affect embryonic
CC or larval development. {ECO:0000269|PubMed:11441002}.
CC -!- SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family.
CC {ECO:0000305}.
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DR EMBL; AB055112; BAB62293.1; -; mRNA.
DR EMBL; BX284604; CAB16306.2; -; Genomic_DNA.
DR EMBL; BX284604; CAQ48388.2; -; Genomic_DNA.
DR EMBL; BX284604; CTQ86638.1; -; Genomic_DNA.
DR PIR; T19492; T19492.
DR RefSeq; NP_001129847.2; NM_001136375.2.
DR AlphaFoldDB; B2MZD0; -.
DR SMR; B2MZD0; -.
DR STRING; 6239.C26H9A.1b; -.
DR TCDB; 3.A.2.2.7; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR PaxDb; B2MZD0; -.
DR PeptideAtlas; B2MZD0; -.
DR EnsemblMetazoa; C26H9A.1a.1; C26H9A.1a.1; WBGene00006916. [B2MZD0-2]
DR EnsemblMetazoa; C26H9A.1b.1; C26H9A.1b.1; WBGene00006916. [B2MZD0-1]
DR EnsemblMetazoa; C26H9A.1c.1; C26H9A.1c.1; WBGene00006916. [B2MZD0-3]
DR GeneID; 178219; -.
DR CTD; 178219; -.
DR WormBase; C26H9A.1a; CE30882; WBGene00006916; vha-7.
DR WormBase; C26H9A.1b; CE43617; WBGene00006916; vha-7.
DR WormBase; C26H9A.1c; CE50146; WBGene00006916; vha-7.
DR eggNOG; KOG2189; Eukaryota.
DR GeneTree; ENSGT00950000182881; -.
DR HOGENOM; CLU_005230_0_0_1; -.
DR InParanoid; B2MZD0; -.
DR OMA; IMMLMGI; -.
DR OrthoDB; 181796at2759; -.
DR PhylomeDB; B2MZD0; -.
DR Reactome; R-CEL-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR Reactome; R-CEL-77387; Insulin receptor recycling.
DR Reactome; R-CEL-917977; Transferrin endocytosis and recycling.
DR Reactome; R-CEL-9639288; Amino acids regulate mTORC1.
DR Reactome; R-CEL-983712; Ion channel transport.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00006916; Expressed in reproductive system and 9 other tissues.
DR ExpressionAtlas; B2MZD0; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0033179; C:proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IBA:GO_Central.
DR GO; GO:0051117; F:ATPase binding; IBA:GO_Central.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0007035; P:vacuolar acidification; IBA:GO_Central.
DR InterPro; IPR002490; V-ATPase_116kDa_su.
DR PANTHER; PTHR11629; PTHR11629; 1.
DR Pfam; PF01496; V_ATPase_I; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Coiled coil; Glycoprotein; Ion transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1210
FT /note="V-type proton ATPase 116 kDa subunit a 4"
FT /id="PRO_0000454083"
FT TOPO_DOM 1..715
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 716..736
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 737..760
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 761..781
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 782..855
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 856..876
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 877..892
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 893..913
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 914..976
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 977..997
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 998..1127
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1128..1148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1149..1210
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 259..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 339..405
FT /evidence="ECO:0000255"
FT COMPBIAS 259..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 1010
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1019
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 1..244
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_061243"
FT VAR_SEQ 328..336
FT /note="LNAKMSLYS -> VEFITGFLF (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_061244"
FT VAR_SEQ 337..1210
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_061245"
SQ SEQUENCE 1210 AA; 138510 MW; A53407025413A298 CRC64;
MSSFSNVGFV PHDGENEEDA INLAPKSSES FPAEDSIFAD GSPRHRTLFD SKKRFKLRPP
LLASTPRVIC RFQQASSGSS APYFTREPTF QPIQEFIEMS EHFHDITENS QGYRFLNTKE
PFSRHHSALH HPRLSFDVLP KVIDFSRRWI GRARDTLYRL SVAYSGQEEL GIERARDELD
DRREHINLSE IFGGSHSQEN SCSSGGVFNL NFDKSIEDRQ LSFENIDLDS TSPQSTNDVI
WLRDMTTVST ISEPILHPSS KISFTSSSPS PQRNPKNEAQ KNSSSKREET SMFRSDPMKL
YQMILVKEAA FECVAEIGKH GNVQFVDLNA KMSLYSRTFV KQMRRCEEME RKLRFLEKQV
ITCKPGLDPK SIDYTDLSAP TQAEMIQLEH KLDQLEREFL DLNNNDYALR KNLNSSKEFL
QVMRLVDEFF QVHKEEEAKA RFERSATTDD IEMFSKSFGF GGLPSSNEMP LTPLLGSDDN
AWFVAGVLPL DKKESFERVL WRACRRTAFV RTSDASFTVN DPVTLEPLQK CVFIVFFKGE
SLRLIVEKVC DGFNATQYPC PKSSKDRKMK MSETEGRMND LTVVIDTTQT HRYTILKDMS
FEIPIWLKNI QIQKSVFAVM NMFTVDTNGF LAGECWIPAA EEDDVRQALH DGFKASGTEV
EPILNELWTN APPPTFHRTN KFTNVFQSIV DSYGVSQYCE VNPAPYTIIT FPFLFAVMFG
DAAHGAILLL AALFFIRNER KIESKKIRDE IFNTFYGGRY IMMLMGIFSI YTGFLYNDAF
AKSFNVFGSG WSNSYNETQL DWWIARSYRK HREYSLELVP EKSFDIEKTY PFGVDPIWNI
ADNRLSFLNS MKMKASVIIG ITQMTFGVFL SVLNHIHFKS YIDIISNFIP QVIFLSCIFI
YLCIQIIVKW IFFSVNAENV FGFEYPGSHC APSLLIGLIN MFMFKKRNEG YLNENGEVYS
NCHLGYWYPN QRLVETILIS ISLACIPIML FGKPLWVRFV TSKRHKLQEN KSLKSLRRNG
TTVSAPTSPV VDAGPPRFED AELLLADELD IGEDIHHSLS DIFVHQAIHT IEFVLGCVSH
TASYLRLWAL SLAHAQLSEV MWHMVLIQGI HTVDHIENET IAMCLKPVVA CVAFFIFASL
SLSILIMMEG LSAFLHALRL HWVEFQSKFY LGTGHPFHAF YLKESLENAQ LITEETDRLA
DISSGQHLHI
