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ATPB_MESAU
ID   ATPB_MESAU              Reviewed;         362 AA.
AC   Q0QEP2;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=ATP synthase subunit beta, mitochondrial {ECO:0000250|UniProtKB:P56480};
DE            EC=7.1.2.2;
DE   AltName: Full=ATP synthase F1 subunit beta {ECO:0000250|UniProtKB:P06576};
DE   Flags: Fragment;
GN   Name=ATP5F1B {ECO:0000250|UniProtKB:P06576};
GN   Synonyms=ATP5B {ECO:0000312|EMBL:ABD77235.1};
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036;
RN   [1] {ECO:0000312|EMBL:ABD77235.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver {ECO:0000312|EMBL:ABD77235.1};
RX   PubMed=16751257; DOI=10.1093/molbev/msl027;
RA   Kullberg M., Nilsson M.A., Arnason U., Harley E.H., Janke A.;
RT   "Housekeeping genes for phylogenetic analysis of eutherian relationships.";
RL   Mol. Biol. Evol. 23:1493-1503(2006).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=20400973; DOI=10.1038/aja.2010.19;
RA   Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.;
RT   "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen
RT   (GP96) are unique to hamster caput epididymal spermatozoa.";
RL   Asian J. Androl. 12:344-355(2010).
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. Subunits alpha and
CC       beta form the catalytic core in F(1). Rotation of the central stalk
CC       against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of
CC       ATP in three separate catalytic sites on the beta subunits.
CC       {ECO:0000305}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate;
CC         Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10106, ECO:0000305};
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 (By similarity). Interacts with PPIF (By similarity). Interacts
CC       with BCL2L1 isoform BCL-X(L); the interaction mediates the association
CC       of BCL2L1 isoform BCL-X(L) with the mitochondrial membrane F(1)F(0) ATP
CC       synthase and enhances neurons metabolic efficiency (By similarity).
CC       Interacts with CLN5 and PPT1. Interacts with S100A1; this interaction
CC       increases F1-ATPase activity (By similarity). Interacts with MTLN (By
CC       similarity). Interacts with TTC5/STRAP; the interaction results in
CC       decreased mitochondrial ATP production (By similarity).
CC       {ECO:0000250|UniProtKB:P00829, ECO:0000250|UniProtKB:P06576,
CC       ECO:0000250|UniProtKB:P10719, ECO:0000250|UniProtKB:P56480}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P00829}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P00829}; Matrix side
CC       {ECO:0000250|UniProtKB:P00829}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000255}.
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DR   EMBL; DQ403102; ABD77235.1; -; mRNA.
DR   AlphaFoldDB; Q0QEP2; -.
DR   SMR; Q0QEP2; -.
DR   PRIDE; Q0QEP2; -.
DR   Proteomes; UP000189706; Unplaced.
DR   GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-EC.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
DR   Gene3D; 1.10.1140.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR005722; ATP_synth_F1_bsu.
DR   InterPro; IPR020003; ATPase_a/bsu_AS.
DR   InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR   InterPro; IPR024034; ATPase_F1/V1_b/a_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00006; ATP-synt_ab; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01039; atpD; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP synthesis; ATP-binding; CF(1); Hydrogen ion transport;
KW   Ion transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; Translocase;
KW   Transport.
FT   CHAIN           <1..>362
FT                   /note="ATP synthase subunit beta, mitochondrial"
FT                   /id="PRO_0000394745"
FT   BINDING         60..67
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P00829"
FT   BINDING         92
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P00829"
FT   MOD_RES         14
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P56480"
FT   MOD_RES         14
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P56480"
FT   MOD_RES         51
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P06576"
FT   MOD_RES         112
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P56480"
FT   MOD_RES         112
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P56480"
FT   MOD_RES         117
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P56480"
FT   MOD_RES         117
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P56480"
FT   MOD_RES         165
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P56480"
FT   MOD_RES         279
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P06576"
FT   MOD_RES         286
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10719"
FT   MOD_RES         333
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P56480"
FT   MOD_RES         338
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P56480"
FT   NON_TER         1
FT                   /evidence="ECO:0000312|EMBL:ABD77235.1"
FT   NON_TER         362
FT                   /evidence="ECO:0000312|EMBL:ABD77235.1"
SQ   SEQUENCE   362 AA;  39384 MW;  C5E7CBBD7FF09C1B CRC64;
     IGEPINERGP IKTKQFAPIH AEAPDFLNMS VDQEILVTGI KVVDLLAPYA KGGKIGLFGG
     AVVGKTVLIM ELINNVAKAH GGYSVFAGVG ERTREGNDLY HEMIESGVIN LKDATSKVAL
     VYGQMNEPPG ARARVALTGL TVAEYFRDQE GQDVLLFIDN IFRFTQAGSE VSALLGRIPS
     AVGYQPTLAT DMGTMQERIT TTKKGSITSV QAIYVPADDL TDPAPATTFA HLDATTVLSR
     AIAELGIYPA VDPLDSTSRI MDPNIVGNEH YDVARGVQKI LQDYKSLQDI IAILGMDELS
     EEDKLTVSRA RKIQRFLSQP FQVAEVFTGH MGKLVPLKET IKGFQQMLAG DYDHLPEQAY
     YI
 
 
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