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NDUV2_RAT
ID   NDUV2_RAT               Reviewed;         248 AA.
AC   P19234; Q6PDU9;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 2.
DT   03-AUG-2022, entry version 182.
DE   RecName: Full=NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial;
DE            EC=7.1.1.2;
DE   AltName: Full=NADH-ubiquinone oxidoreductase 24 kDa subunit;
DE   Flags: Precursor;
GN   Name=Ndufv2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pituitary;
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   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 8-248.
RX   PubMed=2974699; DOI=10.1016/s0006-291x(88)80961-6;
RA   Nishikimi M., Hosokawa Y., Toda H., Suzuki H., Ozawa T.;
RT   "The amino acid sequence of the 24-kDa subunit, an iron-sulfur protein, of
RT   rat liver mitochondrial NADH dehydrogenase deduced from cDNA sequence.";
RL   Biochem. Biophys. Res. Commun. 157:914-920(1988).
RN   [3]
RP   PROTEIN SEQUENCE OF 42-61; 75-87; 199-208 AND 222-248, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA   Lubec G., Chen W.-Q.;
RL   Submitted (APR-2007) to UniProtKB.
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. {ECO:0000250|UniProtKB:P04394}.
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   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000305};
CC       Note=Binds 1 [2Fe-2S] cluster. {ECO:0000305};
CC   -!- SUBUNIT: Core subunit of respiratory chain NADH dehydrogenase (Complex
CC       I) which is composed of 45 different subunits. This is a component of
CC       the flavoprotein-sulfur (FP) fragment of the enzyme (By similarity).
CC       {ECO:0000250|UniProtKB:P04394}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P04394}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P04394}; Matrix side
CC       {ECO:0000250|UniProtKB:P04394}.
CC   -!- SIMILARITY: Belongs to the complex I 24 kDa subunit family.
CC       {ECO:0000305}.
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DR   EMBL; BC058495; AAH58495.1; -; mRNA.
DR   EMBL; M22756; AAA41669.1; -; mRNA.
DR   PIR; A31868; A31868.
DR   RefSeq; NP_112326.1; NM_031064.2.
DR   AlphaFoldDB; P19234; -.
DR   SMR; P19234; -.
DR   BioGRID; 249601; 4.
DR   IntAct; P19234; 2.
DR   MINT; P19234; -.
DR   STRING; 10116.ENSRNOP00000016965; -.
DR   iPTMnet; P19234; -.
DR   PhosphoSitePlus; P19234; -.
DR   SwissPalm; P19234; -.
DR   UCD-2DPAGE; P19234; -.
DR   jPOST; P19234; -.
DR   PaxDb; P19234; -.
DR   PRIDE; P19234; -.
DR   Ensembl; ENSRNOT00000016965; ENSRNOP00000016965; ENSRNOG00000042503.
DR   GeneID; 81728; -.
DR   KEGG; rno:81728; -.
DR   CTD; 4729; -.
DR   RGD; 621733; Ndufv2.
DR   eggNOG; KOG3196; Eukaryota.
DR   GeneTree; ENSGT00390000017580; -.
DR   HOGENOM; CLU_054362_1_1_1; -.
DR   InParanoid; P19234; -.
DR   OMA; VGKFHVQ; -.
DR   OrthoDB; 1396088at2759; -.
DR   PhylomeDB; P19234; -.
DR   TreeFam; TF300004; -.
DR   Reactome; R-RNO-611105; Respiratory electron transport.
DR   Reactome; R-RNO-6799198; Complex I biogenesis.
DR   PRO; PR:P19234; -.
DR   Proteomes; UP000002494; Chromosome 9.
DR   Bgee; ENSRNOG00000042503; Expressed in heart and 20 other tissues.
DR   Genevisible; P19234; RN.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR   GO; GO:0005747; C:mitochondrial respiratory chain complex I; ISO:RGD.
DR   GO; GO:0005739; C:mitochondrion; ISO:RGD.
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:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR   GO; GO:0048738; P:cardiac muscle tissue development; ISO:RGD.
DR   GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; ISO:RGD.
DR   GO; GO:0007399; P:nervous system development; ISO:RGD.
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   TIGRFAMs; TIGR01958; nuoE_fam; 1.
DR   PROSITE; PS01099; COMPLEX1_24K; 1.
PE   1: Evidence at protein level;
KW   2Fe-2S; Direct protein sequencing; Electron transport; Iron; Iron-sulfur;
KW   Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane; NAD;
KW   Oxidoreductase; Phosphoprotein; Reference proteome; Respiratory chain;
KW   Transit peptide; Translocase; Transport; Ubiquinone.
FT   TRANSIT         1..31
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..248
FT                   /note="NADH dehydrogenase [ubiquinone] flavoprotein 2,
FT                   mitochondrial"
FT                   /id="PRO_0000020005"
FT   REGION          229..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         134
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255"
FT   BINDING         139
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255"
FT   BINDING         175
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255"
FT   BINDING         179
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         192
FT                   /note="Phosphotyrosine; by SRC"
FT                   /evidence="ECO:0000250|UniProtKB:P19404"
FT   CONFLICT        245
FT                   /note="Q -> P (in Ref. 2; AAA41669)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   248 AA;  27378 MW;  3A6AA85BB7A870B8 CRC64;
     MFSLALRARA SGLTAQWGRH ARNLHKTAVQ NGAGGALFVH RDTPENNPDT PFDFTPENYE
     RIEAIVRNYP EGHRAAAVLP VLDLAQRQNG WLPISAMNKV AEVLQVPPMR VYEVATFYTM
     YNRKPVGKYH IQVCTTTPCM LRDSDSILET LQRKLGIKVG ETTPDKLFTL IEVECLGACV
     NAPMVQINDD YYEDLTPKDI EEIIDELRAG KVPKPGPRSG RFCCEPAGGL TSLTEPPKGP
     GFGVQAGL
 
 
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