ATPB_CAEEL
ID ATPB_CAEEL Reviewed; 538 AA.
AC P46561;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=ATP synthase subunit beta, mitochondrial;
DE EC=7.1.2.2;
DE Flags: Precursor;
GN Name=atp-2 {ECO:0000312|WormBase:C34E10.6};
GN ORFNames=C34E10.6 {ECO:0000312|WormBase:C34E10.6};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
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]
RP FUNCTION, INTERACTION WITH LOV-1, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=15563610; DOI=10.1091/mbc.e04-09-0851;
RA Hu J., Barr M.M.;
RT "ATP-2 interacts with the PLAT domain of LOV-1 and is involved in
RT Caenorhabditis elegans polycystin signaling.";
RL Mol. Biol. Cell 16:458-469(2005).
CC -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or
CC Complex V) produces ATP from ADP in the presence of a proton gradient
CC across the membrane which is generated by electron transport complexes
CC of the respiratory chain. F-type ATPases consist of two structural
CC domains, F(1) - containing the extramembraneous catalytic core, and
CC F(0) - containing the membrane proton channel, linked together by a
CC central stalk and a peripheral stalk. During catalysis, ATP synthesis
CC in the catalytic domain of F(1) is coupled via a rotary mechanism of
CC the central stalk subunits to proton translocation. Subunits alpha and
CC beta form the catalytic core in F(1). Rotation of the central stalk
CC against the surrounding subunits leads to hydrolysis of ATP in three
CC separate catalytic sites on the beta subunits (Probable). Required
CC during male mating behavior for the response to hermaphrodite contact,
CC acting with lov-1 and pkd-2. May be involved in polycystin signaling.
CC {ECO:0000269|PubMed:15563610, ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate;
CC Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2;
CC -!- SUBUNIT: Subunit of the F-type ATPase which has 2 components, CF(1)
CC - the catalytic core - and CF(0) - the membrane proton channel
CC (Probable). Interacts (via N-terminus) with lov-1 (via PLAT domain).
CC {ECO:0000269|PubMed:15563610, ECO:0000305}.
CC -!- INTERACTION:
CC P46561; P50488: daf-4; NbExp=2; IntAct=EBI-316294, EBI-296172;
CC P46561; Q09624: lov-1; NbExp=4; IntAct=EBI-316294, EBI-2529627;
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC {ECO:0000269|PubMed:15563610}. Mitochondrion
CC {ECO:0000269|PubMed:15563610}. Mitochondrion inner membrane
CC {ECO:0000269|PubMed:15563610}. Note=Peripheral membrane protein.
CC Localizes to the cilium only in male-specific sensory neurons.
CC -!- TISSUE SPECIFICITY: Expressed in three categories of adult male sensory
CC neurons: tail ray B neurons, HOB hook neuron and head cephalic (CEM)
CC neurons. {ECO:0000269|PubMed:15563610}.
CC -!- DEVELOPMENTAL STAGE: Widely expressed throughout development in both
CC males and hermaphrodites.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000305}.
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DR EMBL; BX284603; CCD66650.1; -; Genomic_DNA.
DR PIR; T15763; T15763.
DR RefSeq; NP_498111.2; NM_065710.5.
DR AlphaFoldDB; P46561; -.
DR SMR; P46561; -.
DR BioGRID; 40947; 78.
DR DIP; DIP-24363N; -.
DR IntAct; P46561; 15.
DR STRING; 6239.C34E10.6.1; -.
DR EPD; P46561; -.
DR PaxDb; P46561; -.
DR PeptideAtlas; P46561; -.
DR PRIDE; P46561; -.
DR EnsemblMetazoa; C34E10.6.1; C34E10.6.1; WBGene00000229.
DR EnsemblMetazoa; C34E10.6.2; C34E10.6.2; WBGene00000229.
DR GeneID; 175716; -.
DR KEGG; cel:CELE_C34E10.6; -.
DR UCSC; C34E10.6.2; c. elegans.
DR CTD; 175716; -.
DR WormBase; C34E10.6; CE29950; WBGene00000229; atp-2.
DR eggNOG; KOG1350; Eukaryota.
DR GeneTree; ENSGT00550000074800; -.
DR HOGENOM; CLU_022398_0_2_1; -.
DR InParanoid; P46561; -.
DR OMA; GFNMIMD; -.
DR OrthoDB; 495235at2759; -.
DR PhylomeDB; P46561; -.
DR Reactome; R-CEL-1268020; Mitochondrial protein import.
DR Reactome; R-CEL-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-CEL-8949613; Cristae formation.
DR SignaLink; P46561; -.
DR PRO; PR:P46561; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00000229; Expressed in embryo and 4 other tissues.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0097730; C:non-motile cilium; IDA:WormBase.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019904; F:protein domain specific binding; IPI:WormBase.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-EC.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
DR GO; GO:0040024; P:dauer larval development; IMP:WormBase.
DR GO; GO:0030421; P:defecation; IMP:WormBase.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:UniProtKB.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:WormBase.
DR GO; GO:0048598; P:embryonic morphogenesis; IMP:WormBase.
DR GO; GO:0008406; P:gonad development; IMP:WormBase.
DR GO; GO:0040039; P:inductive cell migration; IMP:WormBase.
DR GO; GO:0007617; P:mating behavior; IMP:WormBase.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR GO; GO:0043050; P:pharyngeal pumping; IMP:WormBase.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IBA:GO_Central.
DR Gene3D; 1.10.1140.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01347; ATP_synth_beta_bact; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR005722; ATP_synth_F1_bsu.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR024034; ATPase_F1/V1_b/a_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF50615; SSF50615; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01039; atpD; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 1: Evidence at protein level;
KW ATP synthesis; ATP-binding; Behavior; Cell projection; CF(1); Cilium;
KW Hydrogen ion transport; Ion transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Nucleotide-binding; Reference proteome;
KW Transit peptide; Translocase; Transport.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..538
FT /note="ATP synthase subunit beta, mitochondrial"
FT /id="PRO_0000002450"
FT BINDING 215..222
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 538 AA; 57527 MW; 5B4D4A9C45D337D5 CRC64;
MASRSLASIS RSASRLLQSN VQKCALPAAS IRLSSNNVES KKGIHTGVAT QQAAAATKVS
AKATAANASG RIVAVIGAVV DVQFDENLPP ILNGLEVVGR SPRLILEVSQ HLGDNVVRCI
AMDGTEGLVR GQPVADTGDP IKIPVGPETL GRIMNVIGEP IDERGPIASK NFAAIHAEAP
EFVEMSVEQE ILVTGIKVVD LLAPYAKGGK IGLFGGAGVG KTVLIMELIN NVAKAHGGYS
VFAGVGERTR EGNDLYHEMI EGGVIDLKGK NSKVSLVYGQ MNEPPGARAR VCLTGLTVAE
YFRDQEGQDV LLFIDNIFRF TQAGSEVSAL LGRIPSAVGY QPTLATDMGS MQERITTTKK
GSITSVQAIY VPADDLTDPA PATTFAHLDA TTVLSRGIAE LAIYPAVDPL DSTSRIMDPN
VVGQNHYDIA RGVQKILQDY KSLQDIIAIL GMDELSEEDK LTVSRARKIQ RFLSQPFQVA
EVFTGHQGKF VSLEETIRGF TMILKGELDH LPEVAFYMQG GIDDVFKKAE ELAKQHGN
