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NU4M_WHEAT
ID   NU4M_WHEAT              Reviewed;         495 AA.
AC   P27572;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2003, sequence version 2.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=NADH-ubiquinone oxidoreductase chain 4;
DE            EC=7.1.1.2;
DE   AltName: Full=NADH dehydrogenase subunit 4;
GN   Name=ND4; Synonyms=NAD4;
OS   Triticum aestivum (Wheat).
OG   Mitochondrion.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4565;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND RNA EDITING.
RC   STRAIN=cv. Capitole; TISSUE=Etiolated seedling;
RX   PubMed=1712098; DOI=10.1093/nar/19.12.3275;
RA   Lamattina L., Grienenberger J.-M.;
RT   "RNA editing of the transcript coding for subunit 4 of NADH dehydrogenase
RT   in wheat mitochondria: uneven distribution of the editing sites among the
RT   four exons.";
RL   Nucleic Acids Res. 19:3275-3282(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 295-346, AND RNA EDITING.
RX   PubMed=2687023; DOI=10.1016/0014-5793(89)81620-5;
RA   Lamattina L., Weil J.H., Grienenberger J.M.;
RT   "RNA editing at a splicing site of NADH dehydrogenase subunit IV gene
RT   transcript in wheat mitochondria.";
RL   FEBS Lett. 258:79-83(1989).
CC   -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory chain
CC       NADH dehydrogenase (Complex I) that is believed to belong to the
CC       minimal assembly required for catalysis. Complex I functions in the
CC       transfer of electrons from NADH to the respiratory chain. The immediate
CC       electron acceptor for the enzyme is believed to be ubiquinone (By
CC       similarity). {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- RNA EDITING: Modified_positions=15 {ECO:0000269|PubMed:1712098,
CC       ECO:0000269|PubMed:2687023}, 25 {ECO:0000269|PubMed:1712098,
CC       ECO:0000269|PubMed:2687023}, 26 {ECO:0000269|PubMed:1712098,
CC       ECO:0000269|PubMed:2687023}, 36 {ECO:0000269|PubMed:1712098,
CC       ECO:0000269|PubMed:2687023}, 52 {ECO:0000269|PubMed:1712098,
CC       ECO:0000269|PubMed:2687023}, 53 {ECO:0000269|PubMed:1712098,
CC       ECO:0000269|PubMed:2687023}, 55 {ECO:0000269|PubMed:1712098,
CC       ECO:0000269|PubMed:2687023}, 56 {ECO:0000269|PubMed:1712098,
CC       ECO:0000269|PubMed:2687023}, 66 {ECO:0000269|PubMed:1712098,
CC       ECO:0000269|PubMed:2687023}, 106 {ECO:0000269|PubMed:1712098,
CC       ECO:0000269|PubMed:2687023}, 121 {ECO:0000269|PubMed:1712098,
CC       ECO:0000269|PubMed:2687023}, 126 {ECO:0000269|PubMed:1712098,
CC       ECO:0000269|PubMed:2687023}, 134 {ECO:0000269|PubMed:1712098,
CC       ECO:0000269|PubMed:2687023}, 139 {ECO:0000269|PubMed:1712098,
CC       ECO:0000269|PubMed:2687023}, 145 {ECO:0000269|PubMed:1712098,
CC       ECO:0000269|PubMed:2687023}, 146 {ECO:0000269|PubMed:1712098,
CC       ECO:0000269|PubMed:2687023}, 150 {ECO:0000269|PubMed:1712098,
CC       ECO:0000269|PubMed:2687023}, 326 {ECO:0000269|PubMed:1712098,
CC       ECO:0000269|PubMed:2687023}, 458 {ECO:0000269|PubMed:1712098,
CC       ECO:0000269|PubMed:2687023}, 469 {ECO:0000269|PubMed:1712098,
CC       ECO:0000269|PubMed:2687023}, 473 {ECO:0000269|PubMed:1712098,
CC       ECO:0000269|PubMed:2687023}, 478 {ECO:0000269|PubMed:1712098,
CC       ECO:0000269|PubMed:2687023};
CC   -!- SIMILARITY: Belongs to the complex I subunit 4 family. {ECO:0000305}.
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DR   EMBL; X57163; CAA40452.1; ALT_SEQ; mRNA.
DR   EMBL; X57164; CAA40453.1; ALT_SEQ; Genomic_DNA.
DR   PIR; S16447; S16447.
DR   AlphaFoldDB; P27572; -.
DR   SMR; P27572; -.
DR   STRING; 4565.EPlTAEP00000010093; -.
DR   eggNOG; KOG4845; Eukaryota.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009536; C:plastid; IEA:UniProt.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR   GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR   InterPro; IPR010227; NADH_Q_OxRdtase_chainM/4.
DR   InterPro; IPR003918; NADH_UbQ_OxRdtase.
DR   InterPro; IPR001750; ND/Mrp_mem.
DR   PANTHER; PTHR43507; PTHR43507; 1.
DR   Pfam; PF00361; Proton_antipo_M; 1.
DR   PRINTS; PR01437; NUOXDRDTASE4.
DR   TIGRFAMs; TIGR01972; NDH_I_M; 1.
PE   2: Evidence at transcript level;
KW   Electron transport; Membrane; Mitochondrion; NAD; Respiratory chain;
KW   RNA editing; Translocase; Transmembrane; Transmembrane helix; Transport;
KW   Ubiquinone.
FT   CHAIN           1..495
FT                   /note="NADH-ubiquinone oxidoreductase chain 4"
FT                   /id="PRO_0000118003"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        39..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        89..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        118..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        139..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        173..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        214..234
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        245..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        272..292
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        313..333
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        335..355
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        367..387
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        388..408
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        413..433
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        457..477
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   495 AA;  55898 MW;  DCFF0B867527D628 CRC64;
     MLEHFCECYF DLSGLILCPV LGSIILLFIP NSSIRLIRLI GLCVSLITFL YSLVLWIQFD
     PSTAKFQFVE SLRWLPYENI HLYMGIDGLS LFFVILTTFL IPICILVGWS GMRSFGKEYI
     IAFLICEFLM IAVFCMLDLL LFYVFFESVL IPMFIIIGVW GSRQRKIKAA YQFFLYTLLG
     SVFMLLAILL ILLQTGTTDL QILLTTEFSE RRQILLWIAF FASFAVKVPM VPVHIWLPEA
     HVEAPTAGSV ILAGILLKLG TYGFLRFSIP MFPEATLCFT PFIYTLSAIA IIYTSLTTLR
     QIDLKKIIAY SSVAHMNLVT IGMFSLNIQG IGGSILLMLS HGLVSSALFL CVGVLYDRHK
     TRLVRYYGGL VSTMPNFSTI FFFFTLANMS LPGTSSFIGE FLILVGAFQR NSLVATLRAL
     GMILGAAYSL WLYNRVVSGN LKPDFLYKFS DLNGREVFIF LPFLVGVVWM GVYPKVFLDC
     MHTSVSNLVQ HGKFH
 
 
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