AT5F2_CAEEL
ID AT5F2_CAEEL Reviewed; 305 AA.
AC Q19126;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=ATP synthase F(0) complex subunit B2, mitochondrial {ECO:0000305};
DE AltName: Full=ATP synthase peripheral stalk-membrane subunit B2 {ECO:0000305};
DE AltName: Full=ATP synthase proton-transporting mitochondrial F(0) complex subunit B2 {ECO:0000305};
DE AltName: Full=ATP synthase subunit B2 {ECO:0000305};
DE Short=ATPase subunit B2 {ECO:0000305};
DE Flags: Precursor;
GN Name=asb-2 {ECO:0000312|WormBase:F02E8.1};
GN ORFNames=F02E8.1 {ECO:0000312|WormBase:F02E8.1};
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, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=17223323; DOI=10.1016/j.mod.2006.11.004;
RA Kawasaki I., Hanazawa M., Gengyo-Ando K., Mitani S., Maruyama I., Iino Y.;
RT "ASB-1, a germline-specific isoform of mitochondrial ATP synthase b
RT subunit, is required to maintain the rate of germline development in
RT Caenorhabditis elegans.";
RL Mech. Dev. 124:237-251(2007).
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. Part of the complex
CC F(0) domain and the peripheric stalk, which acts as a stator to hold
CC the subunits of the catalytic subcomplexes relative to the rotary
CC elements (Probable). Plays a role in somatic development
CC (PubMed:17223323). Does not play a role in germline development
CC (PubMed:17223323). {ECO:0000269|PubMed:17223323, ECO:0000305}.
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 {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|RuleBase:RU368017}.
CC Mitochondrion inner membrane {ECO:0000255|RuleBase:RU368017}.
CC -!- DEVELOPMENTAL STAGE: Expressed in somatic tissues throughout the larval
CC stages and in adults. {ECO:0000269|PubMed:17223323}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in either
CC embryonic lethality or arrest at the L2 to L3 larval stages
CC (PubMed:17223323). RNAi-mediated knockdown results in a delay in
CC somatic development (PubMed:17223323). RNAi-mediated knockdown does not
CC cause sterility (PubMed:17223323). {ECO:0000269|PubMed:17223323}.
CC -!- SIMILARITY: Belongs to the eukaryotic ATPase B chain family.
CC {ECO:0000255|RuleBase:RU368017}.
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DR EMBL; BX284606; CCD83382.1; -; Genomic_DNA.
DR PIR; T15960; T15960.
DR RefSeq; NP_508770.1; NM_076369.3.
DR AlphaFoldDB; Q19126; -.
DR SMR; Q19126; -.
DR DIP; DIP-25346N; -.
DR IntAct; Q19126; 2.
DR STRING; 6239.F02E8.1.3; -.
DR EPD; Q19126; -.
DR PaxDb; Q19126; -.
DR PeptideAtlas; Q19126; -.
DR EnsemblMetazoa; F02E8.1.1; F02E8.1.1; WBGene00000207.
DR EnsemblMetazoa; F02E8.1.2; F02E8.1.2; WBGene00000207.
DR GeneID; 180718; -.
DR KEGG; cel:CELE_F02E8.1; -.
DR UCSC; F02E8.1.2; c. elegans.
DR CTD; 180718; -.
DR WormBase; F02E8.1; CE07016; WBGene00000207; asb-2.
DR eggNOG; KOG3976; Eukaryota.
DR GeneTree; ENSGT00390000001958; -.
DR HOGENOM; CLU_925122_0_0_1; -.
DR InParanoid; Q19126; -.
DR OMA; YHVEREN; -.
DR OrthoDB; 1314411at2759; -.
DR PhylomeDB; Q19126; -.
DR Reactome; R-CEL-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-CEL-8949613; Cristae formation.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00000207; Expressed in larva and 3 other tissues.
DR GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IBA:GO_Central.
DR GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
DR InterPro; IPR008688; ATP_synth_Bsub_B/MI25.
DR InterPro; IPR013837; ATP_synth_F0_suB.
DR PANTHER; PTHR12733; PTHR12733; 1.
DR Pfam; PF05405; Mt_ATP-synt_B; 1.
PE 2: Evidence at transcript level;
KW CF(0); Hydrogen ion transport; Ion transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Transit peptide;
KW Transport.
FT TRANSIT 1..22
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 23..305
FT /note="ATP synthase F(0) complex subunit B2, mitochondrial"
FT /id="PRO_0000454589"
SQ SEQUENCE 305 AA; 34937 MW; CBA6F0E6023E9B0D CRC64;
MSLSRCLPLG QNARVIIIPA RLAHAASTQA AAATDDAPNF FQKLAHRFQG VPLKGEAHAP
KSMFEDCNKE WSAPEPLPAI PKDFKEHPDR DLVNYPYPAR PMYPPKSRLL MMPDSWFTPF
QKVTGVSGPY LFFGGLFAFL VNKELWVFEE QGHMTVGWIL FYLLVTRTAG YKIDQGLYNG
YQERVNFFKG LIQEDLKEAV EFKKTSAKQT ESLNSIKESY PTALKESMAL QLEATYRKNV
QSVATELKRR IDYLKETEES KARVEREQLL KLINSEVDKE FSDRSFKDKY LQNAIQQLKG
LNVQL
