NDUV2_SCHPO
ID NDUV2_SCHPO Reviewed; 162 AA.
AC O13691;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=NADH-ubiquinone oxidoreductase 24 kDa subunit homolog C11E3.12, mitochondrial;
DE EC=1.6.-.-;
GN ORFNames=SPAC11E3.12;
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 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).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000255};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000255};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the complex I 24 kDa subunit family.
CC {ECO:0000305}.
CC -!- CAUTION: Was previously considered as a subunit of the NADH
CC dehydrogenase of the mitochondrial respiratory chain complex I. Due to
CC lack of 38 of the other 40 subunits that are present in that complex in
CC mammals, this attribution is unlikely. {ECO:0000305}.
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DR EMBL; CU329670; CAB11191.1; -; Genomic_DNA.
DR PIR; T37540; T37540.
DR RefSeq; NP_594937.1; NM_001020368.2.
DR AlphaFoldDB; O13691; -.
DR SMR; O13691; -.
DR BioGRID; 279395; 9.
DR STRING; 4896.SPAC11E3.12.1; -.
DR PaxDb; O13691; -.
DR EnsemblFungi; SPAC11E3.12.1; SPAC11E3.12.1:pep; SPAC11E3.12.
DR PomBase; SPAC11E3.12; -.
DR VEuPathDB; FungiDB:SPAC11E3.12; -.
DR eggNOG; KOG3196; Eukaryota.
DR HOGENOM; CLU_1636373_0_0_1; -.
DR InParanoid; O13691; -.
DR OMA; WIPPSAM; -.
DR PhylomeDB; O13691; -.
DR PRO; PR:O13691; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd03064; TRX_Fd_NuoE; 1.
DR Gene3D; 1.10.10.1590; -; 1.
DR InterPro; IPR002023; NuoE-like.
DR InterPro; IPR042128; NuoE_dom.
DR InterPro; IPR041921; NuoE_N.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PIRSF; PIRSF000216; NADH_DH_24kDa; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS01099; COMPLEX1_24K; 1.
PE 3: Inferred from homology;
KW 2Fe-2S; Iron; Iron-sulfur; Metal-binding; Mitochondrion; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..162
FT /note="NADH-ubiquinone oxidoreductase 24 kDa subunit
FT homolog C11E3.12, mitochondrial"
FT /id="PRO_0000020009"
FT BINDING 88
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
FT BINDING 93
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
FT BINDING 125
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
FT BINDING 129
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
SQ SEQUENCE 162 AA; 18501 MW; 750DEFCF647A74DD CRC64;
MKPIRFFKPE NLQLAKAILA RYPLRFQSAA LVPLLDLAQR QHGTWIPPTA MYEIASLAGV
SIDYVHSLIL AYPNDFFWRP KKPRVRICNS WMCQQAAEEQ GNSNWDSQCR SVATKYGFDV
ENTGCLGNCF QGPAMWINDK IYGVNTKEKL VDIMEALTQK KN
