ETFA_SCHPO
ID ETFA_SCHPO Reviewed; 341 AA.
AC P78790; O42660;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 3.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Probable electron transfer flavoprotein subunit alpha, mitochondrial;
DE Short=Alpha-ETF;
DE Flags: Precursor;
GN ORFNames=SPAC27D7.06;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: The electron transfer flavoprotein serves as a specific
CC electron acceptor for several dehydrogenases, including five 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) (By similarity).
CC {ECO:0000250}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC Note=Binds 1 FAD per dimer. {ECO:0000250};
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ETF alpha-subunit/FixB family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA13801.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D89139; BAA13801.1; ALT_INIT; mRNA.
DR EMBL; CU329670; CAA15825.1; -; Genomic_DNA.
DR PIR; T38439; T38439.
DR RefSeq; NP_594612.1; NM_001020040.2.
DR AlphaFoldDB; P78790; -.
DR SMR; P78790; -.
DR BioGRID; 278552; 14.
DR STRING; 4896.SPAC27D7.06.1; -.
DR MaxQB; P78790; -.
DR PaxDb; P78790; -.
DR PRIDE; P78790; -.
DR EnsemblFungi; SPAC27D7.06.1; SPAC27D7.06.1:pep; SPAC27D7.06.
DR GeneID; 2542075; -.
DR KEGG; spo:SPAC27D7.06; -.
DR PomBase; SPAC27D7.06; -.
DR VEuPathDB; FungiDB:SPAC27D7.06; -.
DR eggNOG; KOG3954; Eukaryota.
DR HOGENOM; CLU_034178_0_0_1; -.
DR InParanoid; P78790; -.
DR OMA; WRPYAEQ; -.
DR PhylomeDB; P78790; -.
DR Reactome; R-SPO-611105; Respiratory electron transport.
DR PRO; PR:P78790; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:PomBase.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0009055; F:electron transfer activity; ISS:PomBase.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IBA:GO_Central.
DR GO; GO:0022904; P:respiratory electron transport chain; ISS:PomBase.
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 Electron transport; FAD; Flavoprotein; Mitochondrion; Reference proteome;
KW Transit peptide; Transport.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..341
FT /note="Probable electron transfer flavoprotein subunit
FT alpha, mitochondrial"
FT /id="PRO_0000008659"
FT BINDING 285..313
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT CONFLICT 6
FT /note="Missing (in Ref. 1; BAA13801)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="A -> P (in Ref. 1; BAA13801)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="E -> G (in Ref. 1; BAA13801)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 341 AA; 36394 MW; 6EE560FA609448A2 CRC64;
MLRTTSRTFS RALSSSNFKI NCGRRHWFSV LTLLEHQGGN LSPASLSAVE AAKRTGGDVF
GFVIGKDSSQ ISQKVAKSVN DLKKVIYVEN PSYEHNIPDQ IANVLFENVK KNEISHVFSA
HSTVGKGVMP RLAAMFDVMQ ISDIIGVVSA DTFVRPTYAG NVNVTVSTKD PIKIVTVRAS
AFDAAPSSGE GAATVVEGID PKPAALQEWV SENIIKNARP DLSSAERVVA GGRPLKDKET
FERILTPLAD KLGAAIGATR VAVDSGYADN SLQIGQTGKI IAPKLYIAVG IDGAIQHLAG
IKDSKVIAAI NRDENAPIFQ TADVGIVGDL FEIVPELTEK L
