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ETFA_BOVIN
ID   ETFA_BOVIN              Reviewed;         333 AA.
AC   Q2KJE4;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Electron transfer flavoprotein subunit alpha, mitochondrial;
DE            Short=Alpha-ETF;
DE   Flags: Precursor;
GN   Name=ETFA;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Testis;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Heterodimeric electron transfer flavoprotein that accepts
CC       electrons from several mitochondrial dehydrogenases, including acyl-CoA
CC       dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase. It transfers
CC       the electrons to the main mitochondrial respiratory chain via ETF-
CC       ubiquinone oxidoreductase (ETF dehydrogenase). Required for normal
CC       mitochondrial fatty acid oxidation and normal amino acid metabolism.
CC       {ECO:0000250|UniProtKB:P13804}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:P13804};
CC       Note=Binds 1 FAD per dimer. {ECO:0000250|UniProtKB:P13804};
CC   -!- SUBUNIT: Heterodimer composed of ETFA and ETFB. Identified in a complex
CC       that contains ETFA, ETFB and ETFRF1. Interaction with ETFRF1 promotes
CC       dissociation of the bound FAD and loss of electron transfer activity
CC       (By similarity). Interacts with TASOR (By similarity).
CC       {ECO:0000250|UniProtKB:P13804, ECO:0000250|UniProtKB:Q99LC5}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000250|UniProtKB:P13804}.
CC   -!- DOMAIN: Domain I shares an identical polypeptide fold with the beta
CC       subunit ETFB though there is no sequence similarity.
CC       {ECO:0000250|UniProtKB:P13804}.
CC   -!- SIMILARITY: Belongs to the ETF alpha-subunit/FixB family.
CC       {ECO:0000305}.
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DR   EMBL; BC105382; AAI05383.1; -; mRNA.
DR   RefSeq; NP_001069290.1; NM_001075822.1.
DR   AlphaFoldDB; Q2KJE4; -.
DR   SMR; Q2KJE4; -.
DR   STRING; 9913.ENSBTAP00000016570; -.
DR   PaxDb; Q2KJE4; -.
DR   PeptideAtlas; Q2KJE4; -.
DR   PRIDE; Q2KJE4; -.
DR   GeneID; 521892; -.
DR   KEGG; bta:521892; -.
DR   CTD; 2108; -.
DR   eggNOG; KOG3954; Eukaryota.
DR   InParanoid; Q2KJE4; -.
DR   OrthoDB; 1128607at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron transfer activity; ISS:UniProtKB.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; ISS:UniProtKB.
DR   CDD; cd01715; ETF_alpha; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR014730; ETF_a/b_N.
DR   InterPro; IPR001308; ETF_a/FixB.
DR   InterPro; IPR033947; ETF_alpha_N.
DR   InterPro; IPR014731; ETF_asu_C.
DR   InterPro; IPR018206; ETF_asu_C_CS.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR43153; PTHR43153; 1.
DR   Pfam; PF01012; ETF; 1.
DR   Pfam; PF00766; ETF_alpha; 1.
DR   PIRSF; PIRSF000089; Electra_flavoP_a; 1.
DR   SMART; SM00893; ETF; 1.
DR   SUPFAM; SSF52467; SSF52467; 1.
DR   PROSITE; PS00696; ETF_ALPHA; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Electron transport; FAD; Flavoprotein; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Transit peptide; Transport.
FT   TRANSIT         1..19
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..333
FT                   /note="Electron transfer flavoprotein subunit alpha,
FT                   mitochondrial"
FT                   /id="PRO_0000247194"
FT   REGION          20..204
FT                   /note="Domain I"
FT                   /evidence="ECO:0000250|UniProtKB:P13804"
FT   REGION          205..333
FT                   /note="Domain II"
FT                   /evidence="ECO:0000250|UniProtKB:P13804"
FT   BINDING         223
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P13804"
FT   BINDING         248
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P13804"
FT   BINDING         263..266
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P13804"
FT   BINDING         281..286
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P13804"
FT   BINDING         300
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P13804"
FT   BINDING         318..319
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P13804"
FT   MOD_RES         59
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q99LC5"
FT   MOD_RES         59
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q99LC5"
FT   MOD_RES         62
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99LC5"
FT   MOD_RES         69
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q99LC5"
FT   MOD_RES         69
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q99LC5"
FT   MOD_RES         75
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99LC5"
FT   MOD_RES         85
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q99LC5"
FT   MOD_RES         85
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q99LC5"
FT   MOD_RES         93
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99LC5"
FT   MOD_RES         101
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99LC5"
FT   MOD_RES         139
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99LC5"
FT   MOD_RES         140
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P13804"
FT   MOD_RES         158
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q99LC5"
FT   MOD_RES         158
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q99LC5"
FT   MOD_RES         164
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99LC5"
FT   MOD_RES         187
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99LC5"
FT   MOD_RES         203
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q99LC5"
FT   MOD_RES         203
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q99LC5"
FT   MOD_RES         216
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99LC5"
FT   MOD_RES         226
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q99LC5"
FT   MOD_RES         226
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q99LC5"
FT   MOD_RES         232
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q99LC5"
FT   MOD_RES         232
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q99LC5"
FT   MOD_RES         301
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99LC5"
SQ   SEQUENCE   333 AA;  34961 MW;  8E05E2B71A822510 CRC64;
     MFRAAAPGQL RRATSLLRFQ STLVIAEHAN DTLAPITLNT ITAAKHLGGE VSCLVAGTKC
     DKVAQDLCKV AGVAKVLVAQ HDAYKGLLPE ELTPLILATQ KQFNHTHICA GASAFGKNLL
     PRIAAKLDVA PISDIIAIKS PDTFVRTIYA GNAICTVKCD EKVKVFSVRG TSFEAAAASG
     GSASSEKASS TSPVGISEWL DQKLTKSDRP ELTGAKVVVS GGRGLKSGEN FKLLYDLADQ
     LHAAVGASRA AVDAGFVTND LQVGQTGKIV APELYIAVGI SGAIQHLAGM KDSKTIVAIN
     KDPEAPIFQV ADYGIVADLF KVVPEMTELL KKK
 
 
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