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NDUS5_MOUSE
ID   NDUS5_MOUSE             Reviewed;         106 AA.
AC   Q99LY9; Q3U734;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=NADH dehydrogenase [ubiquinone] iron-sulfur protein 5;
DE   AltName: Full=Complex I-15 kDa;
DE            Short=CI-15 kDa;
DE   AltName: Full=NADH-ubiquinone oxidoreductase 15 kDa subunit;
GN   Name=Ndufs5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, and Pancreas;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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   PROTEIN SEQUENCE OF 1-7; 16-27 AND 57-68, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC   Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Accessory subunit of the mitochondrial membrane respiratory
CC       chain NADH dehydrogenase (Complex I), that is believed not to be
CC       involved in catalysis. Complex I functions in the transfer of electrons
CC       from NADH to the respiratory chain. The immediate electron acceptor for
CC       the enzyme is believed to be ubiquinone.
CC       {ECO:0000250|UniProtKB:O43920}.
CC   -!- SUBUNIT: Mammalian complex I is composed of 45 different subunits. This
CC       is a component of the iron-sulfur (IP) fragment of the enzyme.
CC       {ECO:0000250|UniProtKB:O43920}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:O43920}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:O43920}. Mitochondrion intermembrane space
CC       {ECO:0000250|UniProtKB:O43920}.
CC   -!- DOMAIN: Contains two C-X9-C motifs that are predicted to form a helix-
CC       coil-helix structure, permitting the formation of intramolecular
CC       disulfide bonds. {ECO:0000250|UniProtKB:O43920}.
CC   -!- SIMILARITY: Belongs to the complex I NDUFS5 subunit family.
CC       {ECO:0000305}.
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DR   EMBL; AK148505; BAE28590.1; -; mRNA.
DR   EMBL; AK152845; BAE31538.1; -; mRNA.
DR   EMBL; AL606932; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466521; EDK98017.1; -; Genomic_DNA.
DR   EMBL; CH466552; EDL30376.1; -; Genomic_DNA.
DR   EMBL; BC081434; AAH81434.1; -; mRNA.
DR   CCDS; CCDS18618.1; -.
DR   RefSeq; NP_001025445.1; NM_001030274.1.
DR   PDB; 6G2J; EM; 3.30 A; e=1-106.
DR   PDB; 6G72; EM; 3.90 A; e=1-106.
DR   PDB; 6ZR2; EM; 3.10 A; e=1-106.
DR   PDB; 6ZTQ; EM; 3.00 A; e=1-106.
DR   PDB; 7AK5; EM; 3.17 A; e=1-106.
DR   PDB; 7AK6; EM; 3.82 A; e=1-106.
DR   PDB; 7B93; EM; 3.04 A; e=1-106.
DR   PDB; 7PSA; EM; 3.40 A; e=1-106.
DR   PDBsum; 6G2J; -.
DR   PDBsum; 6G72; -.
DR   PDBsum; 6ZR2; -.
DR   PDBsum; 6ZTQ; -.
DR   PDBsum; 7AK5; -.
DR   PDBsum; 7AK6; -.
DR   PDBsum; 7B93; -.
DR   PDBsum; 7PSA; -.
DR   AlphaFoldDB; Q99LY9; -.
DR   SMR; Q99LY9; -.
DR   BioGRID; 546774; 49.
DR   ComplexPortal; CPX-266; Mitochondrial respiratory chain complex I.
DR   CORUM; Q99LY9; -.
DR   IntAct; Q99LY9; 2.
DR   STRING; 10090.ENSMUSP00000030401; -.
DR   iPTMnet; Q99LY9; -.
DR   PhosphoSitePlus; Q99LY9; -.
DR   EPD; Q99LY9; -.
DR   jPOST; Q99LY9; -.
DR   MaxQB; Q99LY9; -.
DR   PaxDb; Q99LY9; -.
DR   PeptideAtlas; Q99LY9; -.
DR   PRIDE; Q99LY9; -.
DR   ProteomicsDB; 253049; -.
DR   Antibodypedia; 31851; 230 antibodies from 30 providers.
DR   DNASU; 595136; -.
DR   Ensembl; ENSMUST00000030401; ENSMUSP00000030401; ENSMUSG00000028648.
DR   Ensembl; ENSMUST00000106206; ENSMUSP00000101812; ENSMUSG00000028648.
DR   Ensembl; ENSMUST00000106207; ENSMUSP00000101813; ENSMUSG00000028648.
DR   GeneID; 595136; -.
DR   KEGG; mmu:595136; -.
DR   UCSC; uc008upu.1; mouse.
DR   CTD; 4725; -.
DR   MGI; MGI:1890889; Ndufs5.
DR   VEuPathDB; HostDB:ENSMUSG00000028648; -.
DR   eggNOG; KOG4110; Eukaryota.
DR   GeneTree; ENSGT00390000002919; -.
DR   HOGENOM; CLU_176387_0_0_1; -.
DR   InParanoid; Q99LY9; -.
DR   OMA; CAHGIGQ; -.
DR   OrthoDB; 1549192at2759; -.
DR   PhylomeDB; Q99LY9; -.
DR   TreeFam; TF332111; -.
DR   Reactome; R-MMU-611105; Respiratory electron transport.
DR   Reactome; R-MMU-6799198; Complex I biogenesis.
DR   BioGRID-ORCS; 595136; 21 hits in 72 CRISPR screens.
DR   PRO; PR:Q99LY9; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; Q99LY9; protein.
DR   Bgee; ENSMUSG00000028648; Expressed in sternocleidomastoid and 262 other tissues.
DR   ExpressionAtlas; Q99LY9; baseline and differential.
DR   Genevisible; Q99LY9; MM.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISO:MGI.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR   GO; GO:0005747; C:mitochondrial respiratory chain complex I; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0009060; P:aerobic respiration; IC:ComplexPortal.
DR   GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; ISS:UniProtKB.
DR   GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IC:ComplexPortal.
DR   InterPro; IPR019342; NADH_UbQ_OxRdtase_FeS-su5.
DR   PANTHER; PTHR15224; PTHR15224; 1.
DR   Pfam; PF10200; Ndufs5; 1.
DR   PROSITE; PS51808; CHCH; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond;
KW   Electron transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Reference proteome; Respiratory chain; Transport.
FT   CHAIN           1..106
FT                   /note="NADH dehydrogenase [ubiquinone] iron-sulfur protein
FT                   5"
FT                   /id="PRO_0000118787"
FT   DOMAIN          30..74
FT                   /note="CHCH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   REGION          79..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           33..43
FT                   /note="Cx9C motif 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   MOTIF           56..66
FT                   /note="Cx9C motif 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   DISULFID        33..66
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   DISULFID        43..56
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   HELIX           6..10
FT                   /evidence="ECO:0007829|PDB:6ZTQ"
FT   STRAND          14..16
FT                   /evidence="ECO:0007829|PDB:7B93"
FT   STRAND          18..23
FT                   /evidence="ECO:0007829|PDB:6ZTQ"
FT   STRAND          26..28
FT                   /evidence="ECO:0007829|PDB:6ZTQ"
FT   HELIX           34..43
FT                   /evidence="ECO:0007829|PDB:6ZTQ"
FT   STRAND          44..47
FT                   /evidence="ECO:0007829|PDB:6ZTQ"
FT   HELIX           49..51
FT                   /evidence="ECO:0007829|PDB:6ZTQ"
FT   HELIX           52..55
FT                   /evidence="ECO:0007829|PDB:6ZTQ"
FT   HELIX           57..67
FT                   /evidence="ECO:0007829|PDB:6ZTQ"
FT   HELIX           71..89
FT                   /evidence="ECO:0007829|PDB:6ZTQ"
FT   HELIX           96..99
FT                   /evidence="ECO:0007829|PDB:6ZTQ"
SQ   SEQUENCE   106 AA;  12648 MW;  DA74C0EEE1EB5C54 CRC64;
     MPFLDIQKKL GISLDRHFMF LSAEQPYKNA ARCHAFEKEW IECAHGIGGT RAKKECKIEF
     DDFEECLLRY KTMRRMHDIK KQREKLMKEG KYTPPPHHSG REEPRP
 
 
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