VATB2_CAEEL
ID VATB2_CAEEL Reviewed; 501 AA.
AC Q9N5A0;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=V-type proton ATPase subunit B 2 {ECO:0000305};
DE Short=V-ATPase subunit B 2 {ECO:0000305};
DE AltName: Full=Defective spermatogenesis protein 5 {ECO:0000303|PubMed:9178007};
DE AltName: Full=Vacuolar proton pump subunit B 2 {ECO:0000305};
GN Name=spe-5 {ECO:0000303|PubMed:9178007, ECO:0000312|WormBase:Y110A7A.12};
GN ORFNames=Y110A7A.12 {ECO:0000312|WormBase:Y110A7A.12};
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, AND MUTAGENESIS OF GLY-110; ASP-172; PRO-382 AND
RP 473-TRP--GLN-501.
RX PubMed=9178007; DOI=10.1093/genetics/146.2.567;
RA Machaca K., L'Hernault S.W.;
RT "The Caenorhabditis elegans spe-5 gene is required for morphogenesis of a
RT sperm-specific organelle and is associated with an inherent cold-sensitive
RT phenotype.";
RL Genetics 146:567-581(1997).
RN [3] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF 473-TRP--GLN-501.
RX PubMed=16005300; DOI=10.1016/j.cub.2005.05.057;
RA Syntichaki P., Samara C., Tavernarakis N.;
RT "The vacuolar H+ -ATPase mediates intracellular acidification required for
RT neurodegeneration in C. elegans.";
RL Curr. Biol. 15:1249-1254(2005).
RN [4] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=22446317; DOI=10.1534/genetics.112.139618;
RA Gleason E.J., Hartley P.D., Henderson M., Hill-Harfe K.L., Price P.W.,
RA Weimer R.M., Kroft T.L., Zhu G.D., Cordovado S., L'Hernault S.W.;
RT "Developmental genetics of secretory vesicle acidification during
RT Caenorhabditis elegans spermatogenesis.";
RL Genetics 191:477-491(2012).
CC -!- FUNCTION: Non-catalytic subunit of the V1 complex of vacuolar(H+)-
CC ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral
CC complex (V1) that hydrolyzes ATP and a membrane integral complex (V0)
CC that translocates protons (By similarity). V-ATPase is responsible for
CC acidifying and maintaining the pH of intracellular compartments and in
CC some cell types, is targeted to the plasma membrane, where it is
CC responsible for acidifying the extracellular environment (Probable). In
CC neurons, required for necrotic cell death probably by promoting
CC intracellular acidification (PubMed:16005300). Required for
CC spermatogenesis where it regulates the fibrous body-membranous
CC organelle (FBMO) morphology in spermatocytes and the acidification of
CC FBMO-derived secretory membranous organelles (MOs) as spermatids mature
CC (PubMed:9178007, PubMed:22446317). {ECO:0000250|UniProtKB:P31408,
CC ECO:0000269|PubMed:16005300, ECO:0000269|PubMed:22446317,
CC ECO:0000269|PubMed:9178007, ECO:0000305|PubMed:22446317}.
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:P31408}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22446317}. Note=In
CC spermatocytes at the meiotic I stage, localizes to the cytoplasm and to
CC discrete dots (PubMed:22446317). In spermatids and the residual body,
CC localizes to discrete dots in the cytoplasm (PubMed:22446317). In
CC budded spermatids, localizes near the cell membrane as discrete dots
CC that are adjacent to secretory membranous organelles (MOs)
CC (PubMed:22446317). {ECO:0000269|PubMed:22446317}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in male and hermaphrodite
CC testis (at protein level). {ECO:0000269|PubMed:22446317}.
CC -!- DISRUPTION PHENOTYPE: Spermatogenesis is arrested at the primary
CC spermatocyte stage. {ECO:0000269|PubMed:22446317}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000255|RuleBase:RU366021}.
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DR EMBL; BX284601; CCD66203.1; -; Genomic_DNA.
DR RefSeq; NP_491518.1; NM_059117.1.
DR AlphaFoldDB; Q9N5A0; -.
DR SMR; Q9N5A0; -.
DR STRING; 6239.Y110A7A.12; -.
DR TCDB; 3.A.2.2.7; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR EPD; Q9N5A0; -.
DR PaxDb; Q9N5A0; -.
DR PeptideAtlas; Q9N5A0; -.
DR EnsemblMetazoa; Y110A7A.12.1; Y110A7A.12.1; WBGene00004959.
DR GeneID; 172137; -.
DR KEGG; cel:CELE_Y110A7A.12; -.
DR UCSC; Y110A7A.12; c. elegans.
DR CTD; 172137; -.
DR WormBase; Y110A7A.12; CE23245; WBGene00004959; spe-5.
DR eggNOG; KOG1351; Eukaryota.
DR GeneTree; ENSGT00970000196287; -.
DR HOGENOM; CLU_022916_3_0_1; -.
DR InParanoid; Q9N5A0; -.
DR OMA; DFEECGS; -.
DR OrthoDB; 541116at2759; -.
DR PhylomeDB; Q9N5A0; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00004959; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IBA:GO_Central.
DR GO; GO:0046034; P:ATP metabolic process; IEA:InterPro.
DR GO; GO:0051452; P:intracellular pH reduction; IMP:UniProtKB.
DR GO; GO:0043068; P:positive regulation of programmed cell death; IGI:WormBase.
DR GO; GO:0048137; P:spermatocyte division; IMP:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
DR GO; GO:0007035; P:vacuolar acidification; IBA:GO_Central.
DR HAMAP; MF_00310; ATP_synth_B_arch; 1.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR005723; ATPase_V1-cplx_bsu.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR022879; V-ATPase_su_B/beta.
DR PANTHER; PTHR43389; PTHR43389; 1.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR PIRSF; PIRSF039114; V-ATPsynth_beta/V-ATPase_B; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01040; V-ATPase_V1_B; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Hydrogen ion transport; Ion transport;
KW Nucleotide-binding; Reference proteome; Transport.
FT CHAIN 1..501
FT /note="V-type proton ATPase subunit B 2"
FT /id="PRO_0000454048"
FT BINDING 392
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P21281"
FT MUTAGEN 110
FT /note="G->R: In hc110; reduces self-fertility at 25 degrees
FT Celsius which is almost abolished at 18 degrees Celsius.
FT Spermatogenesis arrest at the spermatocyte stage.
FT Spermatocytes have defective fibrous body-membranous
FT organelle complexes (FBMOs) causing vacuolation of the
FT cytoplasm. The few produced spermatids exhibit an
FT incomplete penetrance for tubulin mis-segregation during
FT the second meiotic division."
FT /evidence="ECO:0000269|PubMed:9178007"
FT MUTAGEN 172
FT /note="D->N: In eb30; reduces self-fertility at 25 degrees
FT Celsius which is almost abolished at 18 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:9178007"
FT MUTAGEN 382
FT /note="P->S: In eb29; reduces self-fertility at 25 degrees
FT Celsius which is almost abolished at 18 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:9178007"
FT MUTAGEN 473..501
FT /note="Missing: In hc93; reduces self-fertility at 25
FT degrees Celsius which is almost abolished at 18 degrees
FT Celsius. Suppresses neurodegeneration of touch-receptor
FT neurons in a mec-4 (u231) mutant background."
FT /evidence="ECO:0000269|PubMed:16005300,
FT ECO:0000269|PubMed:9178007"
SQ SEQUENCE 501 AA; 56035 MW; 6A05E67A54E28D8A CRC64;
MTEASEINLS DIKGPIDVNT PITNHRTALI QNYSTKPKLT YQTVFGVNGP LVIVHNVKFP
MFNEIVKITL PNGQIRMGQV LESSKNKAVV QVFEGTTGVD AKFTTCEFTG DIFRSPVSLD
MLGRIFNGSG KPIDKGPPVL PEDYLDINGQ PINPFNRIYP EEMIQTGISA IDVMNSIARG
QKIPIFSAAG LPHNEIAAQI VRQGGLVQLP GRNNETVNFA IVFAAMGVNM ETARFFKQDF
EECGSMDNVC LFLNLANDPT IERIITPRIA LTAAEFFAYH CGKHVLVVLT DMSSYAEALR
EISAAREEVP GRRGFPGYMY TDLATIYERA GRVKGREGSI TQIPILTMPN NDITHPIPDL
TGYITEGQIY IDKQLHKRLI YPPIDVLPSL SRLMKSAVGE GMTREDHSDL SNQLYACYAM
GKDVQAMKAV VGVEALSPDD LLYLEFLAKF EKNFIAQGRY ENRTIVESLN IGWELLRIFP
REMLKRIPET LLEKYYKRKK Q
