位置:首页 > 蛋白库 > NDUS8_HUMAN
NDUS8_HUMAN
ID   NDUS8_HUMAN             Reviewed;         210 AA.
AC   O00217; B2RB86; Q0VDA8;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 203.
DE   RecName: Full=NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial;
DE            EC=7.1.1.2 {ECO:0000269|PubMed:22499348};
DE   AltName: Full=Complex I-23kD;
DE            Short=CI-23kD;
DE   AltName: Full=NADH-ubiquinone oxidoreductase 23 kDa subunit;
DE   AltName: Full=TYKY subunit;
DE   Flags: Precursor;
GN   Name=NDUFS8;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   PubMed=9116042; DOI=10.1016/s0167-4781(97)00020-1;
RA   Procaccio V., Depetris D., Soularue P., Mattei M.-G., Lunardi J.,
RA   Issartel J.-P.;
RT   "cDNA sequence and chromosomal localization of the NDUFS8 human gene coding
RT   for the 23 kDa subunit of the mitochondrial complex I.";
RL   Biochim. Biophys. Acta 1351:37-41(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=9666055; DOI=10.1016/s0378-1119(98)00275-3;
RA   de Sury R., Martinez P., Procaccio V., Lunardi J., Issartel J.-P.;
RT   "Genomic structure of the human NDUFS8 gene coding for the iron-sulfur TYKY
RT   subunit of the mitochondrial NADH:ubiquinone oxidoreductase.";
RL   Gene 215:1-10(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Uterus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE NADH-UBIQUINONE
RP   OXIDOREDUCTASE COMPLEX, AND SUBCELLULAR LOCATION.
RX   PubMed=12611891; DOI=10.1074/jbc.c300064200;
RA   Murray J., Zhang B., Taylor S.W., Oglesbee D., Fahy E., Marusich M.F.,
RA   Ghosh S.S., Capaldi R.A.;
RT   "The subunit composition of the human NADH dehydrogenase obtained by rapid
RT   one-step immunopurification.";
RL   J. Biol. Chem. 278:13619-13622(2003).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH RAB5IF.
RX   PubMed=31536960; DOI=10.1016/j.isci.2019.08.057;
RA   Moutaoufik M.T., Malty R., Amin S., Zhang Q., Phanse S., Gagarinova A.,
RA   Zilocchi M., Hoell L., Minic Z., Gagarinova M., Aoki H., Stockwell J.,
RA   Jessulat M., Goebels F., Broderick K., Scott N.E., Vlasblom J., Musso G.,
RA   Prasad B., Lamantea E., Garavaglia B., Rajput A., Murayama K., Okazaki Y.,
RA   Foster L.J., Bader G.D., Cayabyab F.S., Babu M.;
RT   "Rewiring of the Human Mitochondrial Interactome during Neuronal
RT   Reprogramming Reveals Regulators of the Respirasome and Neurogenesis.";
RL   IScience 19:1114-1132(2019).
RN   [10]
RP   INVOLVEMENT IN MC1DN2, AND VARIANTS MC1DN2 LEU-79 AND HIS-102.
RX   PubMed=9837812; DOI=10.1086/302154;
RA   Loeffen J., Smeitink J., Triepels R., Smeets R., Schuelke M., Sengers R.,
RA   Trijbels F., Hamel B.C.J., Mullaart R., van den Heuvel L.;
RT   "The first nuclear-encoded complex I mutation in a patient with Leigh
RT   syndrome.";
RL   Am. J. Hum. Genet. 63:1598-1608(1998).
RN   [11]
RP   VARIANTS MC1DN2 LEU-85 AND HIS-138.
RX   PubMed=15159508; DOI=10.1212/01.wnl.0000125251.56131.65;
RA   Procaccio V., Wallace D.C.;
RT   "Late-onset Leigh syndrome in a patient with mitochondrial complex I NDUFS8
RT   mutations.";
RL   Neurology 62:1899-1901(2004).
RN   [12]
RP   VARIANT MC1DN2 CYS-18.
RX   PubMed=16142472; DOI=10.1007/s00109-005-0712-y;
RA   Hinttala R., Uusimaa J., Remes A.M., Rantala H., Hassinen I.E., Majamaa K.;
RT   "Sequence analysis of nuclear genes encoding functionally important complex
RT   I subunits in children with encephalomyopathy.";
RL   J. Mol. Med. 83:786-794(2005).
RN   [13]
RP   VARIANTS MC1DN2 GLN-63; TRP-77 AND ASP-159, CHARACTERIZATION OF VARIANTS
RP   MC1DN2 GLN-63; TRP-77 AND ASP-159, FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=22499348; DOI=10.1136/jmedgenet-2012-100846;
RA   Haack T.B., Haberberger B., Frisch E.M., Wieland T., Iuso A., Gorza M.,
RA   Strecker V., Graf E., Mayr J.A., Herberg U., Hennermann J.B., Klopstock T.,
RA   Kuhn K.A., Ahting U., Sperl W., Wilichowski E., Hoffmann G.F., Tesarova M.,
RA   Hansikova H., Zeman J., Plecko B., Zeviani M., Wittig I., Strom T.M.,
RA   Schuelke M., Freisinger P., Meitinger T., Prokisch H.;
RT   "Molecular diagnosis in mitochondrial complex I deficiency using exome
RT   sequencing.";
RL   J. Med. Genet. 49:277-283(2012).
CC   -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory chain
CC       NADH dehydrogenase (Complex I) which catalyzes electron transfer from
CC       NADH through the respiratory chain, using ubiquinone as an electron
CC       acceptor (PubMed:22499348). Essential for the catalytic activity and
CC       assembly of complex I (PubMed:22499348). {ECO:0000269|PubMed:22499348}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) +
CC         NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-
CC         COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2;
CC         Evidence={ECO:0000269|PubMed:22499348};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250|UniProtKB:Q56224};
CC       Note=Binds 2 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:Q56224};
CC   -!- SUBUNIT: Core subunit of respiratory chain NADH dehydrogenase (Complex
CC       I) which is composed of 45 different subunits (PubMed:12611891). This
CC       is a component of the iron-sulfur (IP) fragment of the enzyme (By
CC       similarity). Interacts with RAB5IF (PubMed:31536960).
CC       {ECO:0000250|UniProtKB:P42028, ECO:0000269|PubMed:12611891,
CC       ECO:0000269|PubMed:31536960}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000305|PubMed:12611891, ECO:0000305|PubMed:9666055}; Peripheral
CC       membrane protein {ECO:0000250|UniProtKB:P42028}; Matrix side
CC       {ECO:0000250|UniProtKB:P42028}.
CC   -!- TISSUE SPECIFICITY: Expressed in all tissues with the highest level in
CC       heart and skeletal muscle and the lowest level in lung.
CC       {ECO:0000269|PubMed:9666055}.
CC   -!- DISEASE: Mitochondrial complex I deficiency, nuclear type 2 (MC1DN2)
CC       [MIM:618222]: A form of mitochondrial complex I deficiency, the most
CC       common biochemical signature of mitochondrial disorders, a group of
CC       highly heterogeneous conditions characterized by defective oxidative
CC       phosphorylation, which collectively affects 1 in 5-10000 live births.
CC       Clinical disorders have variable severity, ranging from lethal neonatal
CC       disease to adult-onset neurodegenerative disorders. Phenotypes include
CC       macrocephaly with progressive leukodystrophy, non-specific
CC       encephalopathy, cardiomyopathy, myopathy, liver disease, Leigh
CC       syndrome, Leber hereditary optic neuropathy, and some forms of
CC       Parkinson disease. MC1DN2 inheritance is autosomal recessive.
CC       {ECO:0000269|PubMed:15159508, ECO:0000269|PubMed:16142472,
CC       ECO:0000269|PubMed:22499348, ECO:0000269|PubMed:9837812}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- SIMILARITY: Belongs to the complex I 23 kDa subunit family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U65579; AAB51776.1; -; mRNA.
DR   EMBL; AF038406; AAC34273.1; -; Genomic_DNA.
DR   EMBL; AK314546; BAG37133.1; -; mRNA.
DR   EMBL; BC119754; AAI19755.1; -; mRNA.
DR   CCDS; CCDS8176.1; -.
DR   RefSeq; NP_002487.1; NM_002496.3.
DR   RefSeq; XP_005274070.1; XM_005274013.1.
DR   RefSeq; XP_005274071.1; XM_005274014.2.
DR   RefSeq; XP_011543355.1; XM_011545053.2.
DR   PDB; 5XTB; EM; 3.40 A; B=35-210.
DR   PDB; 5XTD; EM; 3.70 A; B=35-210.
DR   PDB; 5XTH; EM; 3.90 A; B=35-210.
DR   PDB; 5XTI; EM; 17.40 A; B/BB=35-210.
DR   PDBsum; 5XTB; -.
DR   PDBsum; 5XTD; -.
DR   PDBsum; 5XTH; -.
DR   PDBsum; 5XTI; -.
DR   AlphaFoldDB; O00217; -.
DR   SMR; O00217; -.
DR   BioGRID; 110806; 247.
DR   ComplexPortal; CPX-577; Mitochondrial respiratory chain complex I.
DR   CORUM; O00217; -.
DR   IntAct; O00217; 55.
DR   MINT; O00217; -.
DR   STRING; 9606.ENSP00000315774; -.
DR   BindingDB; O00217; -.
DR   ChEMBL; CHEMBL2363065; -.
DR   DrugBank; DB00157; NADH.
DR   DrugCentral; O00217; -.
DR   CarbonylDB; O00217; -.
DR   GlyGen; O00217; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; O00217; -.
DR   PhosphoSitePlus; O00217; -.
DR   SwissPalm; O00217; -.
DR   BioMuta; NDUFS8; -.
DR   OGP; O00217; -.
DR   EPD; O00217; -.
DR   jPOST; O00217; -.
DR   MassIVE; O00217; -.
DR   MaxQB; O00217; -.
DR   PaxDb; O00217; -.
DR   PeptideAtlas; O00217; -.
DR   PRIDE; O00217; -.
DR   ProteomicsDB; 47787; -.
DR   TopDownProteomics; O00217; -.
DR   Antibodypedia; 1263; 269 antibodies from 34 providers.
DR   DNASU; 4728; -.
DR   Ensembl; ENST00000313468.10; ENSP00000315774.5; ENSG00000110717.13.
DR   GeneID; 4728; -.
DR   KEGG; hsa:4728; -.
DR   MANE-Select; ENST00000313468.10; ENSP00000315774.5; NM_002496.4; NP_002487.1.
DR   UCSC; uc001onc.4; human.
DR   CTD; 4728; -.
DR   DisGeNET; 4728; -.
DR   GeneCards; NDUFS8; -.
DR   GeneReviews; NDUFS8; -.
DR   HGNC; HGNC:7715; NDUFS8.
DR   HPA; ENSG00000110717; Low tissue specificity.
DR   MalaCards; NDUFS8; -.
DR   MIM; 602141; gene.
DR   MIM; 618222; phenotype.
DR   neXtProt; NX_O00217; -.
DR   OpenTargets; ENSG00000110717; -.
DR   Orphanet; 2609; Isolated complex I deficiency.
DR   Orphanet; 255241; Leigh syndrome with leukodystrophy.
DR   PharmGKB; PA31525; -.
DR   VEuPathDB; HostDB:ENSG00000110717; -.
DR   eggNOG; KOG3256; Eukaryota.
DR   GeneTree; ENSGT00390000003049; -.
DR   HOGENOM; CLU_067218_5_1_1; -.
DR   InParanoid; O00217; -.
DR   OMA; RGDLYYT; -.
DR   OrthoDB; 1283957at2759; -.
DR   PhylomeDB; O00217; -.
DR   TreeFam; TF105610; -.
DR   BioCyc; MetaCyc:HS03332-MON; -.
DR   PathwayCommons; O00217; -.
DR   Reactome; R-HSA-611105; Respiratory electron transport.
DR   Reactome; R-HSA-6799198; Complex I biogenesis.
DR   SignaLink; O00217; -.
DR   SIGNOR; O00217; -.
DR   BioGRID-ORCS; 4728; 287 hits in 1092 CRISPR screens.
DR   ChiTaRS; NDUFS8; human.
DR   GeneWiki; NDUFS8; -.
DR   GenomeRNAi; 4728; -.
DR   Pharos; O00217; Tclin.
DR   PRO; PR:O00217; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; O00217; protein.
DR   Bgee; ENSG00000110717; Expressed in apex of heart and 206 other tissues.
DR   ExpressionAtlas; O00217; baseline and differential.
DR   Genevisible; O00217; HS.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR   GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR   GO; GO:0005747; C:mitochondrial respiratory chain complex I; IDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IMP:UniProtKB.
DR   GO; GO:0009060; P:aerobic respiration; IBA:GO_Central.
DR   GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IMP:UniProtKB.
DR   GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; IMP:UniProtKB.
DR   GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IC:ComplexPortal.
DR   GO; GO:0006979; P:response to oxidative stress; IDA:UniProtKB.
DR   HAMAP; MF_01351; NDH1_NuoI; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR010226; NADH_quinone_OxRdtase_chainI.
DR   PANTHER; PTHR10849; PTHR10849; 1.
DR   Pfam; PF12838; Fer4_7; 1.
DR   TIGRFAMs; TIGR01971; NuoI; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   1: Evidence at protein level;
KW   3D-structure; 4Fe-4S; Disease variant; Electron transport; Iron;
KW   Iron-sulfur; Membrane; Metal-binding; Mitochondrion;
KW   Mitochondrion inner membrane; NAD; Oxidoreductase;
KW   Primary mitochondrial disease; Reference proteome; Repeat;
KW   Respiratory chain; Transit peptide; Translocase; Transport; Ubiquinone.
FT   TRANSIT         1..34
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250|UniProtKB:P42028"
FT   CHAIN           35..210
FT                   /note="NADH dehydrogenase [ubiquinone] iron-sulfur protein
FT                   8, mitochondrial"
FT                   /id="PRO_0000020012"
FT   DOMAIN          102..131
FT                   /note="4Fe-4S ferredoxin-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   DOMAIN          141..170
FT                   /note="4Fe-4S ferredoxin-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   BINDING         111
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   BINDING         114
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   BINDING         117
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   BINDING         121
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   BINDING         150
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   BINDING         153
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   BINDING         156
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   BINDING         160
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   VARIANT         18
FT                   /note="R -> C (in MC1DN2; unknown pathological
FT                   significance; dbSNP:rs750062334)"
FT                   /evidence="ECO:0000269|PubMed:16142472"
FT                   /id="VAR_083603"
FT   VARIANT         63
FT                   /note="E -> Q (in MC1DN2; decrease in enzyme activity;
FT                   impaired assembly of complex I; dbSNP:rs397514618)"
FT                   /evidence="ECO:0000269|PubMed:22499348"
FT                   /id="VAR_081440"
FT   VARIANT         77
FT                   /note="R -> W (in MC1DN2; unknown pathological
FT                   significance; decrease in enzyme activity; impaired
FT                   assembly of complex I; dbSNP:rs146766138)"
FT                   /evidence="ECO:0000269|PubMed:22499348"
FT                   /id="VAR_081441"
FT   VARIANT         79
FT                   /note="P -> L (in MC1DN2; dbSNP:rs28939679)"
FT                   /evidence="ECO:0000269|PubMed:9837812"
FT                   /id="VAR_019538"
FT   VARIANT         85
FT                   /note="P -> L (in MC1DN2; unknown pathological
FT                   significance; dbSNP:rs121912639)"
FT                   /evidence="ECO:0000269|PubMed:15159508"
FT                   /id="VAR_081442"
FT   VARIANT         102
FT                   /note="R -> H (in MC1DN2; dbSNP:rs121912638)"
FT                   /evidence="ECO:0000269|PubMed:9837812"
FT                   /id="VAR_019539"
FT   VARIANT         138
FT                   /note="R -> H (in MC1DN2; unknown pathological
FT                   significance; dbSNP:rs111033588)"
FT                   /evidence="ECO:0000269|PubMed:15159508"
FT                   /id="VAR_081443"
FT   VARIANT         159
FT                   /note="A -> D (in MC1DN2; unknown pathological
FT                   significance; decrease in enzyme activity; impaired
FT                   assembly of complex I; dbSNP:rs397514617)"
FT                   /evidence="ECO:0000269|PubMed:22499348"
FT                   /id="VAR_081444"
FT   STRAND          36..38
FT                   /evidence="ECO:0007829|PDB:5XTB"
FT   HELIX           48..60
FT                   /evidence="ECO:0007829|PDB:5XTB"
FT   HELIX           63..76
FT                   /evidence="ECO:0007829|PDB:5XTB"
FT   TURN            84..86
FT                   /evidence="ECO:0007829|PDB:5XTB"
FT   STRAND          98..101
FT                   /evidence="ECO:0007829|PDB:5XTB"
FT   HELIX           117..120
FT                   /evidence="ECO:0007829|PDB:5XTB"
FT   STRAND          130..132
FT                   /evidence="ECO:0007829|PDB:5XTB"
FT   STRAND          138..141
FT                   /evidence="ECO:0007829|PDB:5XTB"
FT   STRAND          144..146
FT                   /evidence="ECO:0007829|PDB:5XTB"
FT   TURN            147..149
FT                   /evidence="ECO:0007829|PDB:5XTB"
FT   HELIX           155..159
FT                   /evidence="ECO:0007829|PDB:5XTB"
FT   STRAND          165..167
FT                   /evidence="ECO:0007829|PDB:5XTB"
FT   STRAND          175..177
FT                   /evidence="ECO:0007829|PDB:5XTB"
FT   HELIX           178..181
FT                   /evidence="ECO:0007829|PDB:5XTB"
FT   STRAND          182..184
FT                   /evidence="ECO:0007829|PDB:5XTB"
FT   HELIX           185..194
FT                   /evidence="ECO:0007829|PDB:5XTB"
FT   HELIX           196..206
FT                   /evidence="ECO:0007829|PDB:5XTB"
FT   HELIX           207..209
FT                   /evidence="ECO:0007829|PDB:5XTB"
SQ   SEQUENCE   210 AA;  23705 MW;  8C3EBD205BFA0112 CRC64;
     MRCLTTPMLL RALAQAARAG PPGGRSLHSS AVAATYKYVN MQDPEMDMKS VTDRAARTLL
     WTELFRGLGM TLSYLFREPA TINYPFEKGP LSPRFRGEHA LRRYPSGEER CIACKLCEAI
     CPAQAITIEA EPRADGSRRT TRYDIDMTKC IYCGFCQEAC PVDAIVEGPN FEFSTETHEE
     LLYNKEKLLN NGDKWEAEIA ANIQADYLYR
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024