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ATP synthase F(0) complex subunit B1, mitochondrial (ATP synthase subunit b) (ATPase subunit b)

 AT5F1_RAT               Reviewed;         256 AA.
P19511;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
01-FEB-1991, sequence version 1.
05-DEC-2018, entry version 152.
RecName: Full=ATP synthase F(0) complex subunit B1, mitochondrial {ECO:0000305};
AltName: Full=ATP synthase peripheral stalk-membrane subunit b {ECO:0000305};
AltName: Full=ATP synthase subunit b;
Short=ATPase subunit b;
Flags: Precursor;
Name=Atp5pb {ECO:0000312|RGD:620041}; Synonyms=Atp5f, Atp5f1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2140936; DOI=10.1016/0006-291X(90)91444-W;
Tsurumi C., Yoshihara Y., Osaka F., Yamada F., Tani I., Higuti T.,
Shimizu M., Oeda K., Ohkawa H., Toda H., Kakuno T., Sakiyama F.,
Kumatori A., Tanaka K., Ichihara A.;
"cDNA cloning and sequencing for the import precursor of subunit B in
H(+)-ATP synthase from rat mitochondria.";
Biochem. Biophys. Res. Commun. 169:136-142(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pituitary;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE ATP
SYNTHASE COMPLEX.
PubMed=17575325; DOI=10.1074/mcp.M700097-MCP200;
Meyer B., Wittig I., Trifilieff E., Karas M., Schaegger H.;
"Identification of two proteins associated with mammalian ATP
synthase.";
Mol. Cell. Proteomics 6:1690-1699(2007).
-!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) 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, F(1) - containing the
extramembraneous catalytic core, and F(0) - containing the
membrane proton channel, linked together by a central stalk and a
peripheral stalk. During catalysis, ATP synthesis in the catalytic
domain of F(1) is coupled via a rotary mechanism of the central
stalk subunits to proton translocation. Part of the complex F(0)
domain and the peripheric stalk, which acts as a stator to hold
the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static
relative to the rotary elements.
-!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic
core - and CF(0) - the membrane proton channel. CF(1) has five
subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0)
has three main subunits: a, b and c. Component of an ATP synthase
complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME,
ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D,
ATP5F1C, ATP5PO, ATP5MG, ATP5MD and MP68.
{ECO:0000269|PubMed:17575325}.
-!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
-!- SIMILARITY: Belongs to the eukaryotic ATPase B chain family.
{ECO:0000305}.
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EMBL; M35052; AAA42187.1; -; mRNA.
EMBL; BC063808; AAH63808.1; -; mRNA.
PIR; A35340; A35340.
RefSeq; NP_599192.1; NM_134365.2.
RefSeq; XP_003749420.1; XM_003749372.2.
UniGene; Rn.3689; -.
ProteinModelPortal; P19511; -.
SMR; P19511; -.
CORUM; P19511; -.
IntAct; P19511; 4.
MINT; P19511; -.
STRING; 10116.ENSRNOP00000065147; -.
CarbonylDB; P19511; -.
iPTMnet; P19511; -.
PhosphoSitePlus; P19511; -.
SwissPalm; P19511; -.
PaxDb; P19511; -.
PRIDE; P19511; -.
Ensembl; ENSRNOT00000021920; ENSRNOP00000021920; ENSRNOG00000016000.
Ensembl; ENSRNOT00000075083; ENSRNOP00000065147; ENSRNOG00000046299.
GeneID; 100911417; -.
GeneID; 171375; -.
KEGG; rno:100911417; -.
KEGG; rno:171375; -.
UCSC; RGD:620041; rat.
CTD; 515; -.
RGD; 620041; Atp5pb.
eggNOG; ENOG410INNH; Eukaryota.
eggNOG; ENOG4111WYE; LUCA.
GeneTree; ENSGT00390000001958; -.
HOGENOM; HOG000007163; -.
HOVERGEN; HBG050604; -.
InParanoid; P19511; -.
KO; K02127; -.
OMA; KEIYVIN; -.
OrthoDB; EOG091G0DPN; -.
PhylomeDB; P19511; -.
TreeFam; TF313250; -.
Reactome; R-RNO-163210; Formation of ATP by chemiosmotic coupling.
Reactome; R-RNO-8949613; Cristae formation.
PRO; PR:P19511; -.
Proteomes; UP000002494; Chromosome 2.
Bgee; ENSRNOG00000016000; Expressed in 9 organ(s), highest expression level in heart.
Genevisible; P19511; RN.
GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IDA:UniProtKB.
GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IDA:RGD.
GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
GO; GO:0099132; P:ATP hydrolysis coupled cation transmembrane transport; IEA:GOC.
GO; GO:0046034; P:ATP metabolic process; IDA:RGD.
GO; GO:0015986; P:ATP synthesis coupled proton transport; IBA:GO_Central.
GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD.
InterPro; IPR008688; ATP_synth_Bsub_B/MI25.
InterPro; IPR013837; ATP_synth_F0_suB.
PANTHER; PTHR12733; PTHR12733; 1.
Pfam; PF05405; Mt_ATP-synt_B; 1.
1: Evidence at protein level;
Acetylation; CF(0); Complete proteome; Hydrogen ion transport;
Ion transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
Reference proteome; Transit peptide; Transport.
TRANSIT 1 42 Mitochondrion.
CHAIN 43 256 ATP synthase F(0) complex subunit B1,
mitochondrial.
/FTId=PRO_0000002516.
MOD_RES 131 131 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q9CQQ7}.
MOD_RES 139 139 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9CQQ7}.
MOD_RES 154 154 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9CQQ7}.
MOD_RES 162 162 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9CQQ7}.
MOD_RES 221 221 N6-acetyllysine.
{ECO:0000250|UniProtKB:P24539}.
MOD_RES 233 233 N6-acetyllysine.
{ECO:0000250|UniProtKB:P24539}.
MOD_RES 244 244 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9CQQ7}.
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


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