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Protein

ATP synthase subunit beta, mitochondrial

Gene

atp-2

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Mitochondrial membrane ATP synthase (F1F0 ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F1 - containing the extramembraneous catalytic core, and F0 - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F1. Rotation of the central stalk against the surrounding alpha3beta3 subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Required during male mating behavior for the response to hermaphrodite contact, acting with lov-1 and pkd-2. May be involved in polycystin signaling.1 Publication

Catalytic activityi

ATP + H2O + H+(In) = ADP + phosphate + H+(Out).

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi215 – 2228ATPSequence analysis

GO - Molecular functioni

GO - Biological processi

  • ATP hydrolysis coupled proton transport Source: InterPro
  • ATP synthesis coupled proton transport Source: InterPro
  • dauer larval development Source: WormBase
  • defecation Source: WormBase
  • determination of adult lifespan Source: WormBase
  • embryonic morphogenesis Source: WormBase
  • gonad development Source: WormBase
  • inductive cell migration Source: WormBase
  • mating behavior Source: WormBase
  • nematode larval development Source: WormBase
  • pharyngeal pumping Source: WormBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

ATP synthesis, Behavior, Hydrogen ion transport, Ion transport, Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit beta, mitochondrial (EC:3.6.3.14)
Gene namesi
Name:atp-2
ORF Names:C34E10.6
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome III

Organism-specific databases

WormBaseiC34E10.6; CE29950; WBGene00000229; atp-2.

Subcellular locationi

  • Cell projectioncilium 1 Publication
  • Mitochondrion 1 Publication
  • Mitochondrion inner membrane 1 Publication

  • Note: Peripheral membrane protein. Localizes to the cilium only in male-specific sensory neurons.

GO - Cellular componenti

  • cilium Source: UniProtKB
  • mitochondrial inner membrane Source: UniProtKB-SubCell
  • mitochondrion Source: UniProtKB
  • nonmotile primary cilium Source: WormBase
  • proton-transporting ATP synthase complex, catalytic core F(1) Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, CF(1), Cilium, Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 538ATP synthase subunit beta, mitochondrialPRO_0000002450
Transit peptidei1 – ?MitochondrionSequence analysis

Proteomic databases

EPDiP46561.
PaxDbiP46561.
PRIDEiP46561.

Expressioni

Tissue specificityi

Expressed in three categories of adult male sensory neurons: tail ray B neurons, HOB hook neuron and head cephalic (CEM) neurons.1 Publication

Developmental stagei

Widely expressed throughout development in both males and hermaphrodites.

Interactioni

Subunit structurei

F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. CF1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1. CF0 has three main subunits: a, b and c. Interacts (via N-terminus) with lov-1 (via PLAT domain).1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
daf-4P504882EBI-316294,EBI-296172
lov-1Q096244EBI-316294,EBI-2529627

GO - Molecular functioni

  • protein domain specific binding Source: WormBase

Protein-protein interaction databases

BioGridi40947. 15 interactions.
DIPiDIP-24363N.
IntActiP46561. 15 interactions.
MINTiMINT-1076073.
STRINGi6239.C34E10.6.2.

Structurei

3D structure databases

ProteinModelPortaliP46561.
SMRiP46561. Positions 69-523.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase alpha/beta chains family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1350. Eukaryota.
COG0055. LUCA.
GeneTreeiENSGT00550000074800.
HOGENOMiHOG000009605.
InParanoidiP46561.
KOiK02133.
OMAiAEFGIYP.
OrthoDBiEOG73V6K6.
PhylomeDBiP46561.

Family and domain databases

Gene3Di1.10.1140.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_01347. ATP_synth_beta_bact.
InterProiIPR003593. AAA+_ATPase.
IPR020003. ATPase_a/bsu_AS.
IPR005722. ATPase_F1-cplx_bsu.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR004100. ATPase_F1_a/bsu_N.
IPR024034. ATPase_F1_bsu/V1_C.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00006. ATP-synt_ab. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF47917. SSF47917. 1 hit.
SSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01039. atpD. 1 hit.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P46561-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASRSLASIS RSASRLLQSN VQKCALPAAS IRLSSNNVES KKGIHTGVAT
60 70 80 90 100
QQAAAATKVS AKATAANASG RIVAVIGAVV DVQFDENLPP ILNGLEVVGR
110 120 130 140 150
SPRLILEVSQ HLGDNVVRCI AMDGTEGLVR GQPVADTGDP IKIPVGPETL
160 170 180 190 200
GRIMNVIGEP IDERGPIASK NFAAIHAEAP EFVEMSVEQE ILVTGIKVVD
210 220 230 240 250
LLAPYAKGGK IGLFGGAGVG KTVLIMELIN NVAKAHGGYS VFAGVGERTR
260 270 280 290 300
EGNDLYHEMI EGGVIDLKGK NSKVSLVYGQ MNEPPGARAR VCLTGLTVAE
310 320 330 340 350
YFRDQEGQDV LLFIDNIFRF TQAGSEVSAL LGRIPSAVGY QPTLATDMGS
360 370 380 390 400
MQERITTTKK GSITSVQAIY VPADDLTDPA PATTFAHLDA TTVLSRGIAE
410 420 430 440 450
LAIYPAVDPL DSTSRIMDPN VVGQNHYDIA RGVQKILQDY KSLQDIIAIL
460 470 480 490 500
GMDELSEEDK LTVSRARKIQ RFLSQPFQVA EVFTGHQGKF VSLEETIRGF
510 520 530
TMILKGELDH LPEVAFYMQG GIDDVFKKAE ELAKQHGN
Length:538
Mass (Da):57,527
Last modified:June 6, 2002 - v2
Checksum:i5B4D4A9C45D337D5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FO080774 Genomic DNA. Translation: CCD66650.1.
PIRiT15763.
RefSeqiNP_498111.2. NM_065710.5.
UniGeneiCel.38639.

Genome annotation databases

EnsemblMetazoaiC34E10.6.1; C34E10.6.1; WBGene00000229.
C34E10.6.2; C34E10.6.2; WBGene00000229.
C34E10.6.3; C34E10.6.3; WBGene00000229.
GeneIDi175716.
KEGGicel:CELE_C34E10.6.
UCSCiC34E10.6.2. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FO080774 Genomic DNA. Translation: CCD66650.1.
PIRiT15763.
RefSeqiNP_498111.2. NM_065710.5.
UniGeneiCel.38639.

3D structure databases

ProteinModelPortaliP46561.
SMRiP46561. Positions 69-523.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi40947. 15 interactions.
DIPiDIP-24363N.
IntActiP46561. 15 interactions.
MINTiMINT-1076073.
STRINGi6239.C34E10.6.2.

Proteomic databases

EPDiP46561.
PaxDbiP46561.
PRIDEiP46561.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiC34E10.6.1; C34E10.6.1; WBGene00000229.
C34E10.6.2; C34E10.6.2; WBGene00000229.
C34E10.6.3; C34E10.6.3; WBGene00000229.
GeneIDi175716.
KEGGicel:CELE_C34E10.6.
UCSCiC34E10.6.2. c. elegans.

Organism-specific databases

CTDi175716.
WormBaseiC34E10.6; CE29950; WBGene00000229; atp-2.

Phylogenomic databases

eggNOGiKOG1350. Eukaryota.
COG0055. LUCA.
GeneTreeiENSGT00550000074800.
HOGENOMiHOG000009605.
InParanoidiP46561.
KOiK02133.
OMAiAEFGIYP.
OrthoDBiEOG73V6K6.
PhylomeDBiP46561.

Miscellaneous databases

PROiP46561.

Family and domain databases

Gene3Di1.10.1140.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_01347. ATP_synth_beta_bact.
InterProiIPR003593. AAA+_ATPase.
IPR020003. ATPase_a/bsu_AS.
IPR005722. ATPase_F1-cplx_bsu.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR004100. ATPase_F1_a/bsu_N.
IPR024034. ATPase_F1_bsu/V1_C.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00006. ATP-synt_ab. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF47917. SSF47917. 1 hit.
SSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01039. atpD. 1 hit.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2.
  2. "ATP-2 interacts with the PLAT domain of LOV-1 and is involved in Caenorhabditis elegans polycystin signaling."
    Hu J., Barr M.M.
    Mol. Biol. Cell 16:458-469(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH LOV-1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiATPB_CAEEL
AccessioniPrimary (citable) accession number: P46561
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: June 6, 2002
Last modified: June 8, 2016
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.