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ATPD_PENGL
ID   ATPD_PENGL              Reviewed;          17 AA.
AC   P85445;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   25-MAY-2022, entry version 22.
DE   RecName: Full=ATP synthase subunit delta, mitochondrial;
DE   AltName: Full=F-ATPase delta subunit;
DE   Flags: Fragment;
GN   Name=atp16;
OS   Penicillium glabrum (Penicillium frequentans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=69773;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, AND ALLERGEN.
RC   STRAIN=B7;
RA   Raquel H., Jeno P., Moita C., Cardoso C., Sao Jose H., San-Romao V.,
RA   Pinto Ricardo C., Oliveira M.M.;
RT   "Identification of putative allergens from Penicillium glabrum using two-
RT   dimensional (2-D) gel electrophoresis immunoblotting approach.";
RL   Submitted (FEB-2008) to UniProtKB.
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 turnover in
CC       the catalytic domain of F(1) is coupled via a rotary mechanism of the
CC       central stalk subunits to proton translocation. Part of the complex
CC       F(1) domain and of the central stalk which is part of the complex
CC       rotary element. Rotation of the central stalk against the surrounding
CC       alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate
CC       catalytic sites on the beta subunits.
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 {ECO:0000305}. Mitochondrion inner
CC       membrane {ECO:0000305}.
CC   -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE.
CC       {ECO:0000269|Ref.1}.
CC   -!- SIMILARITY: Belongs to the ATPase epsilon chain family. {ECO:0000255}.
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DR   AlphaFoldDB; P85445; -.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
DR   GO; GO:0006754; P:ATP biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Allergen; ATP synthesis; CF(1); Direct protein sequencing;
KW   Hydrogen ion transport; Ion transport; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Transport.
FT   CHAIN           <1..>17
FT                   /note="ATP synthase subunit delta, mitochondrial"
FT                   /id="PRO_0000324675"
FT   NON_TER         1
FT   NON_TER         17
SQ   SEQUENCE   17 AA;  1731 MW;  869EA5069517FCE9 CRC64;
     KIANGSGSEQ DIAEAKI
 
 
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