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NU2M_SHEEP
ID   NU2M_SHEEP              Reviewed;         347 AA.
AC   O78748;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=NADH-ubiquinone oxidoreductase chain 2 {ECO:0000250|UniProtKB:P03891};
DE            EC=7.1.1.2 {ECO:0000250|UniProtKB:P03891};
DE   AltName: Full=NADH dehydrogenase subunit 2;
GN   Name=MT-ND2 {ECO:0000250|UniProtKB:P03891}; Synonyms=MTND2, NADH2, ND2;
OS   Ovis aries (Sheep).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Merinolandschaf {ECO:0000312|Proteomes:UP000002356}; TISSUE=Liver;
RX   PubMed=9767689; DOI=10.1007/pl00006401;
RA   Hiendleder S., Lewalski H., Wassmuth R., Janke A.;
RT   "The complete mitochondrial DNA sequence of the domestic sheep (Ovis aries)
RT   and comparison with the other major ovine haplotype.";
RL   J. Mol. Evol. 47:441-448(1998).
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. Essential for the catalytic activity and assembly of complex
CC       I. {ECO:0000250|UniProtKB:P03891}.
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:0000250|UniProtKB:P03891};
CC   -!- SUBUNIT: Core subunit of respiratory chain NADH dehydrogenase (Complex
CC       I) which is composed of 45 different subunits. Interacts with TMEM242
CC       (By similarity). {ECO:0000250|UniProtKB:P03891,
CC       ECO:0000250|UniProtKB:P03892}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P03892}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 2 family. {ECO:0000305}.
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DR   EMBL; AF010406; AAD10097.1; -; Genomic_DNA.
DR   PIR; T11051; T11051.
DR   RefSeq; NP_008407.1; NC_001941.1.
DR   PDB; 5LNK; EM; 3.90 A; N=1-347.
DR   PDB; 6Q9B; EM; 3.90 A; D2=1-347.
DR   PDB; 6QA9; EM; 4.10 A; D2=1-347.
DR   PDB; 6QBX; EM; 4.20 A; D2=1-347.
DR   PDB; 6QC2; EM; 4.20 A; D2=1-347.
DR   PDB; 6QC3; EM; 4.20 A; D2=1-347.
DR   PDB; 6QC4; EM; 4.60 A; D2=1-347.
DR   PDB; 6QC5; EM; 4.30 A; D2=1-347.
DR   PDB; 6QC6; EM; 4.10 A; D2=1-347.
DR   PDB; 6QC7; EM; 4.40 A; D2=1-347.
DR   PDB; 6QC8; EM; 4.20 A; D2=1-347.
DR   PDB; 6QC9; EM; 5.70 A; D2=1-347.
DR   PDB; 6QCA; EM; 6.20 A; D2=1-347.
DR   PDB; 6QCF; EM; 6.50 A; D2=1-347.
DR   PDB; 6ZKA; EM; 2.50 A; N=1-347.
DR   PDB; 6ZKB; EM; 2.90 A; N=1-347.
DR   PDB; 6ZKC; EM; 3.10 A; N=1-347.
DR   PDB; 6ZKD; EM; 2.70 A; N=1-347.
DR   PDB; 6ZKE; EM; 2.60 A; N=1-347.
DR   PDB; 6ZKF; EM; 2.80 A; N=1-347.
DR   PDB; 6ZKG; EM; 3.40 A; N=1-347.
DR   PDB; 6ZKH; EM; 3.00 A; N=1-347.
DR   PDB; 6ZKI; EM; 2.80 A; N=1-347.
DR   PDB; 6ZKJ; EM; 3.00 A; N=1-347.
DR   PDB; 6ZKK; EM; 3.70 A; N=1-347.
DR   PDB; 6ZKL; EM; 3.10 A; N=1-347.
DR   PDB; 6ZKM; EM; 2.80 A; N=1-347.
DR   PDB; 6ZKN; EM; 2.90 A; N=1-347.
DR   PDB; 6ZKO; EM; 3.80 A; N=1-347.
DR   PDB; 6ZKP; EM; 3.20 A; N=1-347.
DR   PDB; 6ZKQ; EM; 3.30 A; N=1-347.
DR   PDB; 6ZKR; EM; 3.50 A; N=1-347.
DR   PDB; 6ZKS; EM; 3.10 A; N=1-347.
DR   PDB; 6ZKT; EM; 2.80 A; N=1-347.
DR   PDB; 6ZKU; EM; 3.00 A; N=1-347.
DR   PDB; 6ZKV; EM; 2.90 A; N=1-347.
DR   PDBsum; 5LNK; -.
DR   PDBsum; 6Q9B; -.
DR   PDBsum; 6QA9; -.
DR   PDBsum; 6QBX; -.
DR   PDBsum; 6QC2; -.
DR   PDBsum; 6QC3; -.
DR   PDBsum; 6QC4; -.
DR   PDBsum; 6QC5; -.
DR   PDBsum; 6QC6; -.
DR   PDBsum; 6QC7; -.
DR   PDBsum; 6QC8; -.
DR   PDBsum; 6QC9; -.
DR   PDBsum; 6QCA; -.
DR   PDBsum; 6QCF; -.
DR   PDBsum; 6ZKA; -.
DR   PDBsum; 6ZKB; -.
DR   PDBsum; 6ZKC; -.
DR   PDBsum; 6ZKD; -.
DR   PDBsum; 6ZKE; -.
DR   PDBsum; 6ZKF; -.
DR   PDBsum; 6ZKG; -.
DR   PDBsum; 6ZKH; -.
DR   PDBsum; 6ZKI; -.
DR   PDBsum; 6ZKJ; -.
DR   PDBsum; 6ZKK; -.
DR   PDBsum; 6ZKL; -.
DR   PDBsum; 6ZKM; -.
DR   PDBsum; 6ZKN; -.
DR   PDBsum; 6ZKO; -.
DR   PDBsum; 6ZKP; -.
DR   PDBsum; 6ZKQ; -.
DR   PDBsum; 6ZKR; -.
DR   PDBsum; 6ZKS; -.
DR   PDBsum; 6ZKT; -.
DR   PDBsum; 6ZKU; -.
DR   PDBsum; 6ZKV; -.
DR   AlphaFoldDB; O78748; -.
DR   SMR; O78748; -.
DR   STRING; 9940.ENSOARP00000000002; -.
DR   Ensembl; ENSOART00000000010; ENSOARP00000000002; ENSOARG00000000010.
DR   Ensembl; ENSOART00020000011; ENSOARP00020000003; ENSOARG00020000011.
DR   GeneID; 808250; -.
DR   KEGG; oas:808250; -.
DR   CTD; 4536; -.
DR   eggNOG; KOG4668; Eukaryota.
DR   HOGENOM; CLU_007100_1_3_1; -.
DR   OMA; HFWVPEV; -.
DR   OrthoDB; 1153818at2759; -.
DR   Proteomes; UP000002356; Mitochondrion.
DR   Bgee; ENSOARG00000000010; Expressed in cardiac muscle tissue of left auricle and 55 other tissues.
DR   ExpressionAtlas; O78748; baseline.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR   GO; GO:0005747; C:mitochondrial respiratory chain complex I; IEA:Ensembl.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; ISS:UniProtKB.
DR   GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; ISS:UniProtKB.
DR   GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; ISS:UniProtKB.
DR   GO; GO:0072593; P:reactive oxygen species metabolic process; IEA:Ensembl.
DR   InterPro; IPR010933; NADH_DH_su2_C.
DR   InterPro; IPR003917; NADH_UbQ_OxRdtase_chain2.
DR   InterPro; IPR001750; ND/Mrp_mem.
DR   Pfam; PF06444; NADH_dehy_S2_C; 1.
DR   Pfam; PF00361; Proton_antipo_M; 1.
DR   PRINTS; PR01436; NADHDHGNASE2.
PE   1: Evidence at protein level;
KW   3D-structure; Electron transport; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; NAD; Reference proteome; Respiratory chain;
KW   Translocase; Transmembrane; Transmembrane helix; Transport; Ubiquinone.
FT   CHAIN           1..347
FT                   /note="NADH-ubiquinone oxidoreductase chain 2"
FT                   /id="PRO_0000117638"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        25..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        67..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        96..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        122..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        145..165
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        178..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        200..220
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        237..257
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        274..294
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        325..345
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   HELIX           3..22
FT                   /evidence="ECO:0007829|PDB:6ZKA"
FT   HELIX           26..44
FT                   /evidence="ECO:0007829|PDB:6ZKA"
FT   HELIX           50..81
FT                   /evidence="ECO:0007829|PDB:6ZKA"
FT   STRAND          85..88
FT                   /evidence="ECO:0007829|PDB:6ZKA"
FT   HELIX           92..106
FT                   /evidence="ECO:0007829|PDB:6ZKA"
FT   HELIX           112..114
FT                   /evidence="ECO:0007829|PDB:6ZKJ"
FT   HELIX           115..121
FT                   /evidence="ECO:0007829|PDB:6ZKA"
FT   HELIX           124..144
FT                   /evidence="ECO:0007829|PDB:6ZKA"
FT   TURN            145..148
FT                   /evidence="ECO:0007829|PDB:6ZKA"
FT   HELIX           151..170
FT                   /evidence="ECO:0007829|PDB:6ZKA"
FT   HELIX           175..192
FT                   /evidence="ECO:0007829|PDB:6ZKA"
FT   TURN            193..196
FT                   /evidence="ECO:0007829|PDB:6ZKA"
FT   HELIX           198..222
FT                   /evidence="ECO:0007829|PDB:6ZKA"
FT   HELIX           227..230
FT                   /evidence="ECO:0007829|PDB:6ZKA"
FT   HELIX           231..235
FT                   /evidence="ECO:0007829|PDB:6ZKA"
FT   HELIX           238..251
FT                   /evidence="ECO:0007829|PDB:6ZKA"
FT   HELIX           260..270
FT                   /evidence="ECO:0007829|PDB:6ZKA"
FT   TURN            271..274
FT                   /evidence="ECO:0007829|PDB:6ZKA"
FT   HELIX           277..300
FT                   /evidence="ECO:0007829|PDB:6ZKA"
FT   TURN            301..303
FT                   /evidence="ECO:0007829|PDB:6ZKV"
FT   STRAND          307..309
FT                   /evidence="ECO:0007829|PDB:6ZKE"
FT   HELIX           311..314
FT                   /evidence="ECO:0007829|PDB:6ZKA"
FT   HELIX           326..334
FT                   /evidence="ECO:0007829|PDB:6ZKA"
FT   HELIX           337..346
FT                   /evidence="ECO:0007829|PDB:6ZKA"
SQ   SEQUENCE   347 AA;  39128 MW;  5202DF0A0D6C991B CRC64;
     MNPIILIIIL MTVMLGTIIV MISTHWLLIW IGFEMNMLAI IPIMMKKHNP RATEASTKYF
     LTQSTASMLL MMAIIINLMF SGQWTVMKLF NPMASMLMTM ALAMKLGMAP FHFWVPEVTQ
     GIPLSSGLIL LTWQKLAPMS VLYQILPSIN LDLILTLSIL SITIGGWGGL NQTQLRKIMA
     YSSIAHMGWM TAVLLYNPTM TLLNLIIYII MTSTMFTLFM ANSTTTTLSL SHTWNKAPIM
     TILVLITLLS MGGLPPLSGF MPKWMIIQEM TKNDSIILPT LMAITALLNL YFYMRLTYST
     ALTMFPSTNN MKMKWQFPTT KRMTLLPTMT VLSTMLLPLT PILSILE
 
 
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