ID A0A3B1JAQ4_ASTMX Unreviewed; 256 AA.
AC A0A3B1JAQ4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 18-JUN-2025, entry version 28.
DE RecName: Full=ATP synthase subunit b {ECO:0000256|RuleBase:RU368017};
OS Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Acestrorhamphidae; Acestrorhamphinae; Astyanax.
OX NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000038945.1, ECO:0000313|Proteomes:UP000018467};
RN [1] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA Jeffery W., Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX PubMed=25329095; DOI=10.1038/ncomms6307;
RA McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA Yoshizawa M., Warren W.C.;
RT "The cavefish genome reveals candidate genes for eye loss.";
RL Nat. Commun. 5:5307-5307(2014).
RN [3] {ECO:0000313|Ensembl:ENSAMXP00000038945.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2025) to UniProtKB.
CC -!- FUNCTION: Subunit b, of the mitochondrial membrane ATP synthase complex
CC (F(1)F(0) ATP synthase or Complex V) that produces ATP from ADP in the
CC presence of a proton gradient across the membrane which is generated by
CC electron transport complexes of the respiratory chain. ATP synthase
CC complex consist of a soluble F(1) head domain - the catalytic core
CC - and a membrane F(1) domain - the membrane proton channel. These two
CC domains are linked by a central stalk rotating inside the F(1) region
CC and a stationary peripheral stalk. During catalysis, ATP synthesis in
CC the catalytic domain of F(1) is coupled via a rotary mechanism of the
CC central stalk subunits to proton translocation. In vivo, can only
CC synthesize ATP although its ATP hydrolase activity can be activated
CC artificially in vitro. Part of the complex F(0) domain. Part of the
CC complex F(0) domain and the peripheric stalk, which acts as a stator to
CC hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static
CC relative to the rotary elements. {ECO:0000256|ARBA:ARBA00055529,
CC ECO:0000256|RuleBase:RU368017}.
CC -!- SUBUNIT: Component of the ATP synthase complex composed at least of
CC ATP5F1A/subunit alpha, ATP5F1B/subunit beta, ATP5MC1/subunit c
CC (homooctomer), MT-ATP6/subunit a, MT-ATP8/subunit 8, ATP5ME/subunit e,
CC ATP5MF/subunit f, ATP5MG/subunit g, ATP5MK/subunit k, ATP5MJ/subunit j,
CC ATP5F1C/subunit gamma, ATP5F1D/subunit delta, ATP5F1E/subunit epsilon,
CC ATP5PF/subunit F6, ATP5PB/subunit b, ATP5PD/subunit d, ATP5PO/subunit
CC OSCP. ATP synthase complex consists of a soluble F(1) head domain
CC (subunits alpha(3) and beta(3)) - the catalytic core - and a membrane
CC F(0) domain - the membrane proton channel (subunits c, a, 8, e, f, g, k
CC and j). These two domains are linked by a central stalk (subunits
CC gamma, delta, and epsilon) rotating inside the F1 region and a
CC stationary peripheral stalk (subunits F6, b, d, and OSCP).
CC {ECO:0000256|ARBA:ARBA00064647}.
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. CF(1) and CF(0) have
CC multiple subunits. {ECO:0000256|RuleBase:RU368017}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|RuleBase:RU368017}.
CC Mitochondrion inner membrane {ECO:0000256|RuleBase:RU368017}.
CC -!- SIMILARITY: Belongs to the eukaryotic ATPase B chain family.
CC {ECO:0000256|ARBA:ARBA00007479, ECO:0000256|RuleBase:RU368017}.
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DR AlphaFoldDB; A0A3B1JAQ4; -.
DR STRING; 7994.ENSAMXP00000038945; -.
DR Ensembl; ENSAMXT00000040227.1; ENSAMXP00000038945.1; ENSAMXG00000029023.1.
DR GeneTree; ENSGT00390000001958; -.
DR InParanoid; A0A3B1JAQ4; -.
DR Proteomes; UP000018467; Unassembled WGS sequence.
DR Bgee; ENSAMXG00000029023; Expressed in head kidney and 14 other cell types or tissues.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045259; C:proton-transporting ATP synthase complex; IEA:UniProtKB-KW.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:TreeGrafter.
DR FunFam; 1.20.5.2210:FF:000001; ATP synthase F(0) complex subunit B1, mitochondrial; 1.
DR Gene3D; 1.20.5.2210; -; 1.
DR InterPro; IPR008688; ATP_synth_Bsub_B/MI25.
DR InterPro; IPR013837; ATP_synth_F0_suB.
DR PANTHER; PTHR12733:SF3; ATP SYNTHASE F(0) COMPLEX SUBUNIT B1, MITOCHONDRIAL; 1.
DR PANTHER; PTHR12733; MITOCHONDRIAL ATP SYNTHASE B CHAIN; 1.
DR Pfam; PF05405; Mt_ATP-synt_B; 1.
DR SUPFAM; SSF161060; ATP synthase B chain-like; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW CF(0) {ECO:0000256|ARBA:ARBA00022547, ECO:0000256|RuleBase:RU368017};
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781,
KW ECO:0000256|RuleBase:RU368017};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU368017};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU368017};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW ECO:0000256|RuleBase:RU368017};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792,
KW ECO:0000256|RuleBase:RU368017};
KW Reference proteome {ECO:0000313|Proteomes:UP000018467};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU368017}.
SQ SEQUENCE 256 AA; 29015 MW; 81139D216E5A4EF9 CRC64;
MAFKSLNQPK IFCMSVSPLK QIAKQLVVQA SRSIHSSPQS KAPLPPLPEK GGKIRHGIFP
EELFSLLYPK TGVTGPYMLG TGLLLYMLSK EIYVINHETF AALSISSVII YGIKKFGPGV
AAYADKLNEE KVAKAQEVKD VAVARLAQAI EDEKKEQWRV EGRHMLFDTK RNNVTMLLET
NYRERLHMVT SEVKRRLDYQ VELQNLHRRM EQEHMVNWVE QNVVKSITPQ QEKESIAKCI
SDLKVLAKAT QARAAV
//
