ID C3Y468_BRAFL Unreviewed; 508 AA.
AC C3Y468;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=Vacuolar proton pump subunit B {ECO:0000256|RuleBase:RU366021};
DE Short=V-ATPase subunit B {ECO:0000256|RuleBase:RU366021};
DE AltName: Full=Vacuolar proton pump subunit B {ECO:0000256|RuleBase:RU366021};
GN Name=LOC118412860 {ECO:0000313|RefSeq:XP_035671795.1};
GN ORFNames=BRAFLDRAFT_126123 {ECO:0000313|EMBL:EEN65094.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1] {ECO:0000313|EMBL:EEN65094.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN65094.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN65094.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
RN [2] {ECO:0000313|RefSeq:XP_035671795.1}
RP IDENTIFICATION.
RC STRAIN=S238N-H82 {ECO:0000313|RefSeq:XP_035671795.1};
RC TISSUE=Testes {ECO:0000313|RefSeq:XP_035671795.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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. 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.
CC {ECO:0000256|RuleBase:RU366021}.
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. The V1 complex consists of three catalytic AB heterodimers
CC that form a heterohexamer, three peripheral stalks each consisting of
CC EG heterodimers, one central rotor including subunits D and F, and the
CC regulatory subunits C and H. The proton translocation complex V0
CC consists of the proton transport subunit a, a ring of proteolipid
CC subunits c9c'', rotary subunit d, subunits e and f, and the accessory
CC subunits. {ECO:0000256|RuleBase:RU366021}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000256|ARBA:ARBA00008936, ECO:0000256|RuleBase:RU366021}.
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DR EMBL; GG666484; EEN65094.1; -; Genomic_DNA.
DR RefSeq; XP_002609084.1; XM_002609038.1.
DR RefSeq; XP_035671795.1; XM_035815902.1.
DR STRING; 7739.C3Y468; -.
DR KEGG; bfo:118412860; -.
DR eggNOG; KOG1351; Eukaryota.
DR InParanoid; C3Y468; -.
DR OMA; GFKIKPR; -.
DR OrthoDB; 5473721at2759; -.
DR Proteomes; UP000001554; Chromosome 4.
DR GO; GO:0033180; C:proton-transporting V-type ATPase, V1 domain; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:0007035; P:vacuolar acidification; IBA:GO_Central.
DR CDD; cd18112; ATP-synt_V_A-type_beta_C; 1.
DR CDD; cd18118; ATP-synt_V_A-type_beta_N; 1.
DR CDD; cd01135; V_A-ATPase_B; 1.
DR Gene3D; 3.40.50.12240; -; 1.
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 NCBIfam; TIGR01040; V-ATPase_V1_B; 1.
DR PANTHER; PTHR43389; V-TYPE PROTON ATPASE SUBUNIT B; 1.
DR PANTHER; PTHR43389:SF4; V-TYPE PROTON ATPASE SUBUNIT B; 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; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 3: Inferred from homology;
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781,
KW ECO:0000256|RuleBase:RU366021};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU366021};
KW Reference proteome {ECO:0000313|Proteomes:UP000001554};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366021}.
FT DOMAIN 44..110
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02874"
FT DOMAIN 167..394
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF00006"
SQ SEQUENCE 508 AA; 56628 MW; 810CEB4B5ED00455 CRC64;
MSAMGDLMDL GSTPPTNDIR MAREHTLAIT RNYHSQPRLT YKTVTGVNGP LVILDDVKFP
KYAEIVHLTL NDGSIRSGQV LEVSGSKAVV QVFEGTSGID AKHTTCEFTG DILRTPVSED
MLGRVFNGSG KPIDKGPNIL AEDYLDIQGQ PINPQSRIYP EEMIQTGISA IDCMNSIARG
QKIPIFSAAG LPHNEIAAQI CRQGGLVKKQ GKSIVDDHDD NFAIVFAAMG VNMETARFFK
MDFEENGSME NVCLFLNLAN DPTIERIITP RLALTTAEFL AYQCEKHVLV ILTDMSSYAE
ALREVSAARE EVPGRRGFPG YMYTDLATIY ERAGRVDGRN GSITQIPILT MPNDDITHPI
PDLTGYITEG QIYVERQLHN RQIYPPINVL PSLSRLMKSA IGEGMTRKDH ADVSNQLYAC
YAIGKDVQAM KAVVGEEALT PDDLLYLEFL SKFEKNFINQ GPYDNRSIYE SLDIGWSLLR
IFPKQMLKRI PEKTLNEFYP RESRTTTK
//
