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Database: UniProt
Entry: G5EEK9_CAEEL
LinkDB: G5EEK9_CAEEL
Original site: G5EEK9_CAEEL 
ID   G5EEK9_CAEEL            Unreviewed;       873 AA.
AC   G5EEK9;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-SEP-2017, entry version 58.
DE   RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
GN   Name=vha-5 {ECO:0000313|EMBL:CCD69637.1,
GN   ECO:0000313|WormBase:F35H10.4};
GN   ORFNames=CELE_F35H10.4 {ECO:0000313|EMBL:CCD69637.1}, F35H10.4
GN   {ECO:0000313|WormBase:F35H10.4};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000313|EMBL:CCD69637.1, ECO:0000313|Proteomes:UP000001940};
RN   [1] {ECO:0000313|EMBL:CCD69637.1, ECO:0000313|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000313|EMBL:CCD69637.1,
RC   ECO:0000313|Proteomes:UP000001940};
RX   PubMed=9851916; DOI=https://doi.org/10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RA   Sulson J.E., Waterston R.;
RT   "Genome sequence of the nematode C. elegans: a platform for
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
RN   [2] {ECO:0000313|EMBL:BAB62291.1}
RP   NUCLEOTIDE SEQUENCE.
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   [3] {ECO:0000313|EMBL:CCD69637.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Bristol N2 {ECO:0000313|EMBL:CCD69637.1};
RA   Alber B.E., Fuchs G.;
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:CCD69637.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Bristol N2 {ECO:0000313|EMBL:CCD69637.1};
RG   WormBase Consortium;
RA   WormBase;
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Essential component of the vacuolar proton pump (V-
CC       ATPase), a multimeric enzyme that catalyzes the translocation of
CC       protons across the membranes. Required for assembly and activity
CC       of the V-ATPase. {ECO:0000256|RuleBase:RU361189}.
CC   -!- SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family.
CC       {ECO:0000256|RuleBase:RU361189}.
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DR   EMBL; AB055110; BAB62291.1; -; mRNA.
DR   EMBL; BX284604; CCD69637.1; -; Genomic_DNA.
DR   PIR; T16282; T16282.
DR   RefSeq; NP_501399.1; NM_068998.7.
DR   UniGene; Cel.8895; -.
DR   STRING; 6239.F35H10.4.1; -.
DR   TCDB; 3.A.2.2.7; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR   EnsemblMetazoa; F35H10.4.1; F35H10.4.1; WBGene00006914.
DR   EnsemblMetazoa; F35H10.4.2; F35H10.4.2; WBGene00006914.
DR   GeneID; 177626; -.
DR   KEGG; cel:CELE_F35H10.4; -.
DR   CTD; 177626; -.
DR   WormBase; F35H10.4; CE04504; WBGene00006914; vha-5.
DR   eggNOG; KOG2189; Eukaryota.
DR   eggNOG; COG1269; LUCA.
DR   GeneTree; ENSGT00390000004941; -.
DR   KO; K02154; -.
DR   OMA; CYLSQWY; -.
DR   OrthoDB; EOG091G01BI; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00006914; -.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:WormBase.
DR   GO; GO:0044298; C:cell body membrane; IDA:WormBase.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IDA:WormBase.
DR   GO; GO:0070382; C:exocytic vesicle; IDA:WormBase.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005771; C:multivesicular body; IDA:WormBase.
DR   GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IPI:WormBase.
DR   GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR   GO; GO:0051117; F:ATPase binding; IBA:GO_Central.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IBA:GO_Central.
DR   GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
DR   GO; GO:0015986; P:ATP synthesis coupled proton transport; IBA:GO_Central.
DR   GO; GO:0040002; P:collagen and cuticulin-based cuticle development; IMP:WormBase.
DR   GO; GO:1990182; P:exosomal secretion; IDA:WormBase.
DR   GO; GO:0050891; P:multicellular organismal water homeostasis; IMP:WormBase.
DR   GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR   GO; GO:0051046; P:regulation of secretion; IMP:WormBase.
DR   GO; GO:0007035; P:vacuolar acidification; IBA:GO_Central.
DR   GO; GO:0070072; P:vacuolar proton-transporting V-type ATPase complex assembly; IBA:GO_Central.
DR   GO; GO:0030104; P:water homeostasis; IMP:WormBase.
DR   InterPro; IPR002490; V-ATPase_116kDa_su.
DR   InterPro; IPR026028; V-type_ATPase_116kDa_su_euka.
DR   PANTHER; PTHR11629; PTHR11629; 1.
DR   Pfam; PF01496; V_ATPase_I; 1.
DR   PIRSF; PIRSF001293; ATP6V0A1; 1.
PE   1: Evidence at protein level;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001940};
KW   Hydrogen ion transport {ECO:0000256|RuleBase:RU361189};
KW   Ion transport {ECO:0000256|RuleBase:RU361189};
KW   Membrane {ECO:0000256|RuleBase:RU361189};
KW   Proteomics identification {ECO:0000213|EPD:G5EEK9,
KW   ECO:0000213|PeptideAtlas:G5EEK9};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001940};
KW   Transmembrane {ECO:0000256|RuleBase:RU361189};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU361189};
KW   Transport {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    449    467       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    546    564       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    576    599       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    670    689       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    789    809       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    815    839       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   COILED       96    123       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   873 AA;  99313 MW;  930CD7223847E2A4 CRC64;
     MGSLSRSEEM RFCQLIVEKD AAFNIVAEIG KQPYVQFKDL NPNVNSFQRT FVKDIRRYDE
     MERKLRFLES QIVKDEIVIP GRVDTGDYTI LPTSELNTLE GTLTELEKDV KSMNDSDSQL
     KANFMDLKEW DAVLDKTDEF FQGGVDDQAQ EELENLDEEG AVPRVEKGPV NYLVGIIRRE
     RLNGFERVLW RACHHTAYIR SSDIEEELED PGTGEKVHKS VFIIFLKGDR MRSIVEKVCD
     GFKAKLFKNC PKTFKERQSA RNDVRARIQD LQTVLGQTRE HRFRVLQAAA NNHHQWLKQV
     RMIKTVFHML NLFTFDGIGR FFVGECWIPL KHVEDVRKAI EVGAERSGSS VKPVLNILET
     SVTPPTYNET NKFTAVFQGI VDSYGIATYR ELNPAPYTII TFPFLFSCMF GDLGHGCIML
     MAGLWFVLRE KNLQARNIKD EIFNMFFGGR YIILLMGLFS IHAGIIYNDM FAKSFNIFGS
     GWKNPYNASE IEGWINRTEH GKEMLVELAP EDAYDHAGGP YSFGVDPIWN IAENKLNFLN
     SMKMKLSVIL GISQMTFGVI LSFFNHTYNK SKIDIFTVFI PQMLFMGCIF MYLCLQIILK
     WLFFWTKEAT VFGQIYPGSH CAPSLLIGLI NMFMMKDRNA GFVVDGGKVN GEYREVETCY
     LSQWYPGQSV IEMILVVIAV ICVPVMLFGK PIHHVMQQKK KAKELHGNAT VRANVVSDSS
     EIVLNGGSKK EGAAHEEHGH GGHEDESFGD IMVHQAIHTI EYVLGCVSHT ASYLRLWALS
     LAHAQLSEVL WHMVFVTGGL GISGTAGFIA VYVVFFIFFV LTISILVLME GLSAFLHTLR
     LHWVEFQSKF YLGLGYPFVP YSFKTALQEA EAA
//
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