ETP1_SCHPO
ID ETP1_SCHPO Reviewed; 616 AA.
AC Q10361;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Electron transfer protein 1, mitochondrial;
DE Flags: Precursor;
GN Name=etp1; ORFNames=SPAC22E12.10c;
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 [GENOMIC DNA], IDENTIFICATION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=11841224; DOI=10.1021/bi0157870;
RA Bureik M., Schiffler B., Hiraoka Y., Vogel F., Bernhardt R.;
RT "Functional expression of human mitochondrial CYP11B2 in fission yeast and
RT identification of a new internal electron transfer protein, etp1.";
RL Biochemistry 41:2311-2321(2002).
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 -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000269|PubMed:11841224}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:11841224}.
CC -!- SIMILARITY: Belongs to the COX15/CtaA family. {ECO:0000305}.
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DR EMBL; CU329670; CAA93897.2; -; Genomic_DNA.
DR PIR; T38167; T38167.
DR RefSeq; NP_594836.2; NM_001020265.3.
DR PDB; 2WLB; X-ray; 2.60 A; A/B=516-603.
DR PDBsum; 2WLB; -.
DR AlphaFoldDB; Q10361; -.
DR SMR; Q10361; -.
DR BioGRID; 278330; 1.
DR STRING; 4896.SPAC22E12.10c.1; -.
DR iPTMnet; Q10361; -.
DR MaxQB; Q10361; -.
DR PaxDb; Q10361; -.
DR PRIDE; Q10361; -.
DR EnsemblFungi; SPAC22E12.10c.1; SPAC22E12.10c.1:pep; SPAC22E12.10c.
DR GeneID; 2541839; -.
DR KEGG; spo:SPAC22E12.10c; -.
DR PomBase; SPAC22E12.10c; etp1.
DR VEuPathDB; FungiDB:SPAC22E12.10c; -.
DR eggNOG; KOG2725; Eukaryota.
DR eggNOG; KOG3309; Eukaryota.
DR HOGENOM; CLU_017627_3_0_1; -.
DR InParanoid; Q10361; -.
DR OMA; HPRVSHY; -.
DR PhylomeDB; Q10361; -.
DR Reactome; R-SPO-189451; Heme biosynthesis.
DR EvolutionaryTrace; Q10361; -.
DR PRO; PR:Q10361; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IC:PomBase.
DR GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:PomBase.
DR GO; GO:0009055; F:electron transfer activity; IDA:PomBase.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IDA:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IDA:PomBase.
DR GO; GO:0016653; F:oxidoreductase activity, acting on NAD(P)H, heme protein as acceptor; IBA:GO_Central.
DR GO; GO:0044571; P:[2Fe-2S] cluster assembly; IC:PomBase.
DR GO; GO:0006784; P:heme A biosynthetic process; ISO:PomBase.
DR GO; GO:0140647; P:P450-containing electron transport chain; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR HAMAP; MF_01665; HemeA_synth_type2; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR001055; Adrenodoxin.
DR InterPro; IPR018298; Adrenodoxin_Fe-S_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR003780; COX15/CtaA_fam.
DR InterPro; IPR023754; HemeA_Synthase_type2.
DR PANTHER; PTHR23289; PTHR23289; 1.
DR Pfam; PF02628; COX15-CtaA; 1.
DR Pfam; PF00111; Fer2; 1.
DR PRINTS; PR00355; ADRENODOXIN.
DR SUPFAM; SSF54292; SSF54292; 1.
DR PROSITE; PS00814; ADX; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Electron transport; Iron; Iron-sulfur; Membrane;
KW Metal-binding; Mitochondrion; Reference proteome; Transit peptide;
KW Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..616
FT /note="Electron transfer protein 1, mitochondrial"
FT /id="PRO_0000006079"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 440..460
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 502..606
FT /note="2Fe-2S ferredoxin-type"
FT BINDING 541
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 547
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 550
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 587
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT CONFLICT 94
FT /note="P -> S (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="I -> T (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 443
FT /note="A -> V (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT STRAND 519..524
FT /evidence="ECO:0007829|PDB:2WLB"
FT STRAND 530..535
FT /evidence="ECO:0007829|PDB:2WLB"
FT TURN 540..543
FT /evidence="ECO:0007829|PDB:2WLB"
FT STRAND 551..554
FT /evidence="ECO:0007829|PDB:2WLB"
FT HELIX 556..561
FT /evidence="ECO:0007829|PDB:2WLB"
FT HELIX 567..573
FT /evidence="ECO:0007829|PDB:2WLB"
FT STRAND 583..585
FT /evidence="ECO:0007829|PDB:2WLB"
FT TURN 586..588
FT /evidence="ECO:0007829|PDB:2WLB"
FT HELIX 593..595
FT /evidence="ECO:0007829|PDB:2WLB"
FT STRAND 598..601
FT /evidence="ECO:0007829|PDB:2WLB"
SQ SEQUENCE 616 AA; 68584 MW; D5E3846A28789691 CRC64;
MNISRSSGLM RQFLLQPLRK GCDISCLGRS SWRMSRSFSG SSVLNEINLS RTKNLFLNDC
KFNKNSFEKF FARRLSNSVA PTPGGILQET EKIPSKKVAF WLLGSSALVL AIVVVGGITR
LTESGLSITE WKPITGVIPP LTDEQWNQEF ELYKKSPEFE KLNSHMTVDE FKNIFFWEWF
HRVLGRGIGL TILLPSIYMI VTKRASPWLS KRLIGLTGLV GLQGVIGWWM VKSGLSEELF
SDGSHPRVSH YRLATHLAAA VALYIGLVWT GHGILQRHAF LKSMKSGSTS QLTSMVSSVQ
KMKGFRTSVN SFVGLVLITL LSGAFVAGLD AGMIYCTFPE MGEGRLAPSK SELFDQRFCR
KDDKSDLIWR NMIDNPSLVQ LEHRILAITT FVAACGLFIF SRAKRNILPK KIKTSINVVT
GVVTAQATLG IMTLIYVVPV PLAALHQAGS LVTLTAALSL AQRLHPEYAL KNIRSWTKLI
SSPPKSSISS SILTQQRQFH TFRPSFHSEI KKPLPGTGIK VFFVTPEGRE IMIEGNEEGA
CEGSVACSTC HVIVDPEHYE LLDPPEEDEE DMLDLAFGLE ETSRLGCQVL LRKDLDGIRV
RIPAQTRNIR LERPKA
