Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P46561 (ATPB_CAEEL)

Last modified November 24, 2009. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    ATP synthase subunit beta, mitochondrial
    EC=3.6.3.14
Gene names
Name: atp-2
ORF Names: C34E10.6
OrganismCaenorhabditis elegans [Complete proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Hide | Top

Protein attributes

Sequence length538 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

Hide | Top

General annotation (Comments)

Function

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. Ref.2

Catalytic activity

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

Subunit structure

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). Ref.2

Subcellular location

Cell projection › cilium. Mitochondrion. Mitochondrion inner membrane. Note: Peripheral membrane protein. Localizes to the cilium only in male-specific sensory neurons. Ref.2

Tissue specificity

Expressed in three categories of adult male sensory neurons: tail ray B neurons, HOB hook neuron and head cephalic (CEM) neurons. Ref.2

Developmental stage

Widely expressed throughout development in both males and hermaphrodites.

Sequence similarities

Belongs to the ATPase alpha/beta chains family.

Hide | Top

Ontologies

Keywords
   Biological processATP synthesis
Behavior
Hydrogen ion transport
Ion transport
Transport
   Cellular componentCF(1)
Cell projection
Cilium
Membrane
Mitochondrion
Mitochondrion inner membrane
   DomainTransit peptide
   LigandATP-binding
Nucleotide-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processATP synthesis coupled proton transport

Inferred from electronic annotation. Source: InterPro

behavior

Inferred from electronic annotation. Source: UniProtKB-KW

embryonic development ending in birth or egg hatching Ref.2

Inferred from mutant phenotype. Source: WormBase

growth Ref.2

Inferred from mutant phenotype. Source: WormBase

nematode larval development Ref.2

Inferred from mutant phenotype. Source: WormBase

positive regulation of growth rate Ref.2

Inferred from mutant phenotype. Source: WormBase

reproduction Ref.2

Inferred from mutant phenotype. Source: WormBase

   Cellular componentcilium Ref.2

Inferred from direct assay. Source: UniProtKB

mitochondrial inner membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

proton-transporting ATP synthase complex, catalytic core F(1)

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

hydrogen ion transporting ATP synthase activity, rotational mechanism

Inferred from electronic annotation. Source: InterPro

hydrogen-exporting ATPase activity, phosphorylative mechanism

Inferred from electronic annotation. Source: InterPro

protein binding Ref.2

Inferred from physical interaction. Source: UniProtKB

proton-transporting ATPase activity, rotational mechanism

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 538ATP synthase subunit beta, mitochondrialPRO_0000002450

Regions

Nucleotide binding215 – 2228ATP Potential

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
P46561-1 [UniParc].

Last modified June 6, 2002. Version 2.
Checksum: 5B4D4A9C45D337D5

FASTA53857,527
        10         20         30         40         50         60 
MASRSLASIS RSASRLLQSN VQKCALPAAS IRLSSNNVES KKGIHTGVAT QQAAAATKVS 

        70         80         90        100        110        120 
AKATAANASG RIVAVIGAVV DVQFDENLPP ILNGLEVVGR SPRLILEVSQ HLGDNVVRCI 

       130        140        150        160        170        180 
AMDGTEGLVR GQPVADTGDP IKIPVGPETL GRIMNVIGEP IDERGPIASK NFAAIHAEAP 

       190        200        210        220        230        240 
EFVEMSVEQE ILVTGIKVVD LLAPYAKGGK IGLFGGAGVG KTVLIMELIN NVAKAHGGYS 

       250        260        270        280        290        300 
VFAGVGERTR EGNDLYHEMI EGGVIDLKGK NSKVSLVYGQ MNEPPGARAR VCLTGLTVAE 

       310        320        330        340        350        360 
YFRDQEGQDV LLFIDNIFRF TQAGSEVSAL LGRIPSAVGY QPTLATDMGS MQERITTTKK 

       370        380        390        400        410        420 
GSITSVQAIY VPADDLTDPA PATTFAHLDA TTVLSRGIAE LAIYPAVDPL DSTSRIMDPN 

       430        440        450        460        470        480 
VVGQNHYDIA RGVQKILQDY KSLQDIIAIL GMDELSEEDK LTVSRARKIQ RFLSQPFQVA 

       490        500        510        520        530 
EVFTGHQGKF VSLEETIRGF TMILKGELDH LPEVAFYMQG GIDDVFKKAE ELAKQHGN

« Hide

Hide | Top

References

« Hide 'large scale' references
[1]"Genome sequence of the nematode C. elegans: a platform for investigating biology."
The C. elegans sequencing consortium
Science 282:2012-2018(1998) [PubMed: 9851916] [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: 15563610] [Abstract]
Cited for: FUNCTION, INTERACTION WITH LOV-1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases

U10402 Genomic DNA. Translation: AAA19068.2.
PIRT15763.
RefSeqNP_498111.2.
UniGeneCel.17897

3D structure databases

SMRP46561. Positions 69-533.
ModBaseSearch...

Protein-protein interaction databases

IntActP46561. 13 interactions.
STRINGP46561.

Genome annotation databases

EnsemblC34E10.6.1; C34E10.6.1; C34E10.6; Caenorhabditis elegans. [Genome view]
C34E10.6.2; C34E10.6.2; C34E10.6; Caenorhabditis elegans. [Genome view]
C34E10.6.3; C34E10.6.3; C34E10.6; Caenorhabditis elegans. [Genome view]
GeneID175716.
KEGGcel:C34E10.6.
UCSCC34E10.6.2. c. elegans.

Organism-specific databases

CTD175716.
WormBaseWBGene00000229. atp-2.
WormPepC34E10.6. CE29950. [WorfDB]

Phylogenomic databases

OMAIGQEHYD

Enzyme and pathway databases

BRENDA3.6.3.14. 672.

Gene expression databases

ArrayExpressP46561.

Family and domain databases

InterProIPR003593. ATPase_AAA+_core.
IPR005722. ATPase_F1-cplx_bsu.
IPR018118. ATPase_F1/A1-cplx_a/bsu_N.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR004100. ATPase_F1/V1/A1-cplx_a/bsu_N.
IPR020003. ATPase_F1/V1/A1_a/bsu_AS.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
[Graphical view]
PANTHERPTHR15184:SF8. ATPase_F1_b. 1 hit.
PfamPF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
SMARTSM00382. AAA. 1 hit.
[Graphical view]
TIGRFAMsTIGR01039. atpD. 1 hit.
PROSITEPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio889338.

Hide | Top

Entry information

Entry nameATPB_CAEEL
AccessionPrimary (citable) accession number: P46561
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: June 6, 2002
Last modified: November 24, 2009
This is version 84 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectCaenorhabditis annotation project

Hide | Top

Relevant documents

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormPep

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents