AT5F1_RAT
ID AT5F1_RAT Reviewed; 256 AA.
AC P19511;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=ATP synthase F(0) complex subunit B1, mitochondrial {ECO:0000305};
DE AltName: Full=ATP synthase peripheral stalk-membrane subunit b {ECO:0000305};
DE AltName: Full=ATP synthase subunit b;
DE Short=ATPase subunit b;
DE Flags: Precursor;
GN Name=Atp5pb {ECO:0000312|RGD:620041}; Synonyms=Atp5f, Atp5f1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2140936; DOI=10.1016/0006-291x(90)91444-w;
RA Tsurumi C., Yoshihara Y., Osaka F., Yamada F., Tani I., Higuti T.,
RA Shimizu M., Oeda K., Ohkawa H., Toda H., Kakuno T., Sakiyama F.,
RA Kumatori A., Tanaka K., Ichihara A.;
RT "cDNA cloning and sequencing for the import precursor of subunit B in H(+)-
RT ATP synthase from rat mitochondria.";
RL Biochem. Biophys. Res. Commun. 169:136-142(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE ATP SYNTHASE
RP COMPLEX.
RX PubMed=17575325; DOI=10.1074/mcp.m700097-mcp200;
RA Meyer B., Wittig I., Trifilieff E., Karas M., Schaegger H.;
RT "Identification of two proteins associated with mammalian ATP synthase.";
RL Mol. Cell. Proteomics 6:1690-1699(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 catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static
CC relative to the rotary elements.
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main
CC subunits: a, b and c. Component of an ATP synthase complex composed of
CC ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-
CC ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MK and
CC ATP5MJ. {ECO:0000269|PubMed:17575325}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC -!- SIMILARITY: Belongs to the eukaryotic ATPase B chain family.
CC {ECO:0000305}.
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DR EMBL; M35052; AAA42187.1; -; mRNA.
DR EMBL; BC063808; AAH63808.1; -; mRNA.
DR PIR; A35340; A35340.
DR RefSeq; NP_599192.1; NM_134365.2.
DR RefSeq; XP_003749420.1; XM_003749372.2.
DR AlphaFoldDB; P19511; -.
DR SMR; P19511; -.
DR BioGRID; 251213; 3.
DR CORUM; P19511; -.
DR IntAct; P19511; 6.
DR MINT; P19511; -.
DR STRING; 10116.ENSRNOP00000021920; -.
DR CarbonylDB; P19511; -.
DR iPTMnet; P19511; -.
DR PhosphoSitePlus; P19511; -.
DR SwissPalm; P19511; -.
DR jPOST; P19511; -.
DR PaxDb; P19511; -.
DR PRIDE; P19511; -.
DR Ensembl; ENSRNOT00000021920; ENSRNOP00000021920; ENSRNOG00000064742.
DR GeneID; 171375; -.
DR KEGG; rno:171375; -.
DR UCSC; RGD:620041; rat.
DR CTD; 515; -.
DR RGD; 620041; Atp5pb.
DR eggNOG; KOG3976; Eukaryota.
DR GeneTree; ENSGT00390000001958; -.
DR HOGENOM; CLU_087186_1_0_1; -.
DR InParanoid; P19511; -.
DR OMA; HMVNWIV; -.
DR OrthoDB; 1314411at2759; -.
DR PhylomeDB; P19511; -.
DR TreeFam; TF313250; -.
DR Reactome; R-RNO-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-RNO-8949613; Cristae formation.
DR PRO; PR:P19511; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000016000; Expressed in heart and 19 other tissues.
DR ExpressionAtlas; P19511; baseline.
DR Genevisible; P19511; RN.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IDA:UniProtKB.
DR GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IDA:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0046034; P:ATP metabolic process; IDA:RGD.
DR GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; ISO:RGD.
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 1: Evidence at protein level;
KW Acetylation; CF(0); Hydrogen ion transport; Ion transport; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Transit peptide; Transport.
FT TRANSIT 1..42
FT /note="Mitochondrion"
FT CHAIN 43..256
FT /note="ATP synthase F(0) complex subunit B1, mitochondrial"
FT /id="PRO_0000002516"
FT MOD_RES 131
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CQQ7"
FT MOD_RES 139
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CQQ7"
FT MOD_RES 154
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CQQ7"
FT MOD_RES 162
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CQQ7"
FT MOD_RES 221
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P24539"
FT MOD_RES 233
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P24539"
FT MOD_RES 244
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CQQ7"
SQ SEQUENCE 256 AA; 28869 MW; 8E27538E6DF682BE CRC64;
MLSRVVLSAA ATAAPCLKNA AVLGPGVLQA TRVFHTGQPR LAPLPPLPEY GGKVRLGLIP
EEFFQFLYPK TGVTGPYVLG TGLSLYFLSK EIYVITPETF STISVVGLIV YVIKKYGASI
GEFIDKLNEE KIAQLEEIKQ SSMKQIQDAI NREKAQQALV QKRHYLFDVQ RNNIALALEV
TYRERLHKAY KEVKNRLDYH ISVQDMMRRK EGEHMINWVE KHVIQSISAQ QEKETIAKCI
GDLKMLAKKA QAQPIM
