AT5F1_CAEEL
ID AT5F1_CAEEL Reviewed; 301 AA.
AC Q20053;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=ATP synthase F(0) complex subunit B1, mitochondrial {ECO:0000305};
DE AltName: Full=ATP synthase peripheral stalk-membrane subunit B1 {ECO:0000305};
DE AltName: Full=ATP synthase proton-transporting mitochondrial F(0) complex subunit B1 {ECO:0000305};
DE AltName: Full=ATP synthase subunit B1 {ECO:0000305};
DE Short=ATPase subunit B1 {ECO:0000305};
DE Flags: Precursor;
GN Name=asb-1 {ECO:0000303|PubMed:17223323, ECO:0000312|WormBase:F35G12.10};
GN ORFNames=F35G12.10 {ECO:0000312|WormBase:F35G12.10};
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, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP 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 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 ECO:0000269|PubMed:17223323}. Mitochondrion inner membrane
CC {ECO:0000255|RuleBase:RU368017}.
CC -!- DEVELOPMENTAL STAGE: Specifically expressed in the germline from the L1
CC larval stage. {ECO:0000269|PubMed:17223323}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in sterility
CC (PubMed:17223323). RNAi-mediated knockdown does not affect the timing
CC of hypodermal and vulval development (PubMed:17223323).
CC {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; BX284603; CAA86329.1; -; Genomic_DNA.
DR PIR; T21803; T21803.
DR RefSeq; NP_497938.1; NM_065537.4.
DR AlphaFoldDB; Q20053; -.
DR SMR; Q20053; -.
DR STRING; 6239.F35G12.10.1; -.
DR EPD; Q20053; -.
DR PaxDb; Q20053; -.
DR PeptideAtlas; Q20053; -.
DR EnsemblMetazoa; F35G12.10.1; F35G12.10.1; WBGene00000206.
DR GeneID; 175605; -.
DR KEGG; cel:CELE_F35G12.10; -.
DR UCSC; F35G12.10.1; c. elegans.
DR CTD; 175605; -.
DR WormBase; F35G12.10; CE00968; WBGene00000206; asb-1.
DR eggNOG; KOG3976; Eukaryota.
DR GeneTree; ENSGT00390000001958; -.
DR HOGENOM; CLU_925122_0_0_1; -.
DR InParanoid; Q20053; -.
DR OMA; HKYTGTS; -.
DR OrthoDB; 1314411at2759; -.
DR PhylomeDB; Q20053; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00000206; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:WormBase.
DR GO; GO:0097730; C:non-motile cilium; IDA:WormBase.
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..21
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 22..301
FT /note="ATP synthase F(0) complex subunit B1, mitochondrial"
FT /id="PRO_0000454588"
SQ SEQUENCE 301 AA; 34368 MW; DADDF5C4C020221B CRC64;
MSLSRLSSPQ TFSRVFIVAR GAATGHAVAP SSDNSIGYFE KIAYRFKGIP LPTETEAPKS
MFDACNKEWS APELLPSVPK DFKEHPDRDL TNYPYPSRPM YPPKTRLLMM PDSWFTAFQK
VTGTSGPYLF FGGLFAFLVN KELWVFEEQG HMTVGWILFY LLVSRTAGYK IDAGLYKDYQ
ERVGFFKGLI QEDLKEAVDF RKTSAAQTAS FAALKEGMPT SLKDSMQLQL EAAYRKNVQT
ISNEIKRRIE YLKETEETKA RFERDQLLKL INDSVEKQVS QKDFQEKFLQ NAIQQLKGIA
V
