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ATPB_CHICK
ID   ATPB_CHICK              Reviewed;         533 AA.
AC   Q5ZLC5; P84168;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=ATP synthase subunit beta, mitochondrial {ECO:0000305};
DE            EC=7.1.2.2;
DE   AltName: Full=ATP synthase F1 subunit beta {ECO:0000250|UniProtKB:P06576};
DE   Flags: Precursor;
GN   Name=ATP5F1B {ECO:0000250|UniProtKB:P06576};
GN   Synonyms=ATP5B {ECO:0000250|UniProtKB:P00829}; ORFNames=RCJMB04_6l18;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:CAG31468.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB {ECO:0000312|EMBL:CAG31468.1};
RC   TISSUE=Bursa of Fabricius {ECO:0000312|EMBL:CAG31468.1};
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
RN   [2] {ECO:0000305}
RP   IDENTIFICATION, AND MASS SPECTROMETRY.
RC   TISSUE=Embryo {ECO:0000269|PubMed:16287166};
RX   PubMed=16287166; DOI=10.1002/pmic.200402056;
RA   Agudo D., Gomez-Esquer F., Diaz-Gil G., Martinez-Arribas F., Delcan J.,
RA   Schneider J., Palomar M.A., Linares R.;
RT   "Proteomic analysis of the Gallus gallus embryo at stage-29 of
RT   development.";
RL   Proteomics 5:4946-4957(2005).
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   -!- 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: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. {ECO:0000305}.
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   -!- MASS SPECTROMETRY: Mass=51171; Mass_error=1; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:16287166};
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000255}.
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DR   EMBL; AJ719809; CAG31468.1; -; mRNA.
DR   RefSeq; NP_001026562.2; NM_001031391.2.
DR   AlphaFoldDB; Q5ZLC5; -.
DR   SMR; Q5ZLC5; -.
DR   BioGRID; 686196; 2.
DR   IntAct; Q5ZLC5; 1.
DR   STRING; 9031.ENSGALP00000035339; -.
DR   PaxDb; Q5ZLC5; -.
DR   GeneID; 426673; -.
DR   KEGG; gga:426673; -.
DR   CTD; 11947; -.
DR   VEuPathDB; HostDB:geneid_426673; -.
DR   eggNOG; KOG1350; Eukaryota.
DR   InParanoid; Q5ZLC5; -.
DR   OrthoDB; 495235at2759; -.
DR   PhylomeDB; Q5ZLC5; -.
DR   PRO; PR:Q5ZLC5; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IBA:GO_Central.
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   GO; GO:0001525; P:angiogenesis; IMP:UniProtKB.
DR   GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IBA:GO_Central.
DR   Gene3D; 1.10.1140.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_01347; ATP_synth_beta_bact; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR005722; ATP_synth_F1_bsu.
DR   InterPro; IPR020003; ATPase_a/bsu_AS.
DR   InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR   InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
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   Pfam; PF02874; ATP-synt_ab_N; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF50615; SSF50615; 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   ATP synthesis; ATP-binding; CF(1); Hydrogen ion transport; Ion transport;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding;
KW   Reference proteome; Transit peptide; Translocase; Transport.
FT   TRANSIT         1..53
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250|UniProtKB:P00829"
FT   CHAIN           54..533
FT                   /note="ATP synthase subunit beta, mitochondrial"
FT                   /id="PRO_0000223501"
FT   BINDING         212..219
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P00829"
FT   BINDING         244
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P00829"
SQ   SEQUENCE   533 AA;  56628 MW;  84C9945D1AAD8832 CRC64;
     MLGLAGRCSA AAASAARPAL RRAAGPSHGF LPLLLSRGAG PAAAVGARRD HAAQAAPAAK
     AGSATGRIVA VIGAVVDVQF DEGLPPILNA LEVQGRETRL VLEVAQHLGE NTVRTIAMDG
     TEGLVRGQKV LDSGAPIRIP VGPETLGRIM NVIGEPIDER GPITTKQFAA IHAEAPEFVE
     MSVEQKILVT GIKVVDLLAP YAKGGKIGLF GGAGVGKTVL IMELINNVAK AHGGYSVFAG
     VGERTREGND LYHEMIESGV INLKDATSKV ALVYGQMNEP PGARARVALT GLTVAEYFRD
     QEGQDVLLFI DNIFRFTQAG SEVSALLGRI PSAVGYQPTL ATDMGTMQER ITTTRKGSIT
     SVQAIYVPAD DLTDPAPATT FAHLDATTVL SRAIAELGIY PAVDPLDSTS RIMDPNIVGP
     EHYDVARGVQ KILQDYKSLQ DIIAILGMDE LSEEDKLTVA RARKIQRFLS QPFQVAEVFT
     GHMGKLVPLK ETIKGFKQIL AGEYDHLPEQ AFYMVGPIEE AVAKAEKLAE EHA
 
 
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