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NU5M_ARBLI
ID   NU5M_ARBLI              Reviewed;         190 AA.
AC   Q33753; Q33755;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=NADH-ubiquinone oxidoreductase chain 5;
DE            EC=7.1.1.2;
DE   AltName: Full=NADH dehydrogenase subunit 5;
DE   Flags: Fragment;
GN   Name=ND5;
OS   Arbacia lixula (Black urchin) (Echinus lixula).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC   Euechinoidea; Echinacea; Arbacioida; Arbaciidae; Arbacia.
OX   NCBI_TaxID=7640;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1681410; DOI=10.1093/oxfordjournals.molbev.a040661;
RA   de Giorgi C., Lanave C., Musci M.D., Saccone C.;
RT   "Mitochondrial DNA in the sea urchin Arbacia lixula: evolutionary
RT   inferences from nucleotide sequence analysis.";
RL   Mol. Biol. Evol. 8:515-529(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-80.
RX   PubMed=1653758; DOI=10.1016/0378-1119(91)90281-f;
RA   de Giorgi C., de Luca F., Saccone C.;
RT   "Mitochondrial DNA in the sea urchin Arbacia lixula: nucleotide sequence
RT   differences between two polymorphic molecules indicate asymmetry of
RT   mutations.";
RL   Gene 103:249-252(1991).
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 inner membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 5 family. {ECO:0000305}.
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DR   EMBL; M74839; AAA98047.1; -; Genomic_DNA.
DR   EMBL; M79454; AAA31639.2; -; Genomic_DNA.
DR   AlphaFoldDB; Q33753; -.
DR   SMR; Q33753; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
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; IPR003945; NU5C-like.
DR   PANTHER; PTHR42829; PTHR42829; 1.
PE   3: Inferred from homology;
KW   Electron transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   NAD; Respiratory chain; Translocase; Transmembrane; Transmembrane helix;
KW   Transport; Ubiquinone.
FT   CHAIN           1..>190
FT                   /note="NADH-ubiquinone oxidoreductase chain 5"
FT                   /id="PRO_0000118060"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        68..88
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        94..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        118..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        146..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        167..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   VARIANT         14
FT                   /note="L -> S"
FT   NON_TER         190
SQ   SEQUENCE   190 AA;  21157 MW;  CEEAD130024F7C6F CRC64;
     MVISPSTLLV SITLSIICLI VSILYTSKSF VAQRNFLTSG NIAFSGASLN ITSDGSAVYS
     WTNGPFSINI LKFLAFLSLI NLFLFVGLEF QETNVTFSIW LSNTAANVSL SILFDHYFIV
     FLTVALVVTW SIMNFSLLYG EDPNKNVFLL LTIFLLNMLI LTCSNSLFLL FLGWEGVGFL
     SFLLIKMMNH
 
 
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