NU2M_TETNG
ID NU2M_TETNG Reviewed; 348 AA.
AC Q4JQI6;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=NADH-ubiquinone oxidoreductase chain 2;
DE EC=7.1.1.2;
DE AltName: Full=NADH dehydrogenase subunit 2;
GN Name=MT-ND2; Synonyms=MTND2, NADH2, ND2;
OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17076253; DOI=10.1080/10425170600700378;
RA Yue G.H., Lo L.C., Zhu Z.Y., Lin G., Feng F.;
RT "The complete nucleotide sequence of the mitochondrial genome of Tetraodon
RT nigroviridis.";
RL DNA Seq. 17:115-121(2006).
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; Multi-pass membrane
CC protein.
CC -!- SIMILARITY: Belongs to the complex I subunit 2 family. {ECO:0000305}.
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DR EMBL; DQ019313; AAY26165.1; -; Genomic_DNA.
DR AlphaFoldDB; Q4JQI6; -.
DR SMR; Q4JQI6; -.
DR STRING; 99883.ENSTNIP00000007011; -.
DR Ensembl; ENSTNIT00000007167; ENSTNIP00000007011; ENSTNIG00000004377.
DR GeneTree; ENSGT00730000111348; -.
DR HOGENOM; CLU_007100_1_3_1; -.
DR InParanoid; Q4JQI6; -.
DR OMA; HFWVPEV; -.
DR TreeFam; TF343996; -.
DR Proteomes; UP000007303; Mitochondrion.
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:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IEA:InterPro.
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 3: Inferred from homology;
KW Electron transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW NAD; Reference proteome; Respiratory chain; Translocase; Transmembrane;
KW Transmembrane helix; Transport; Ubiquinone.
FT CHAIN 1..348
FT /note="NADH-ubiquinone oxidoreductase chain 2"
FT /id="PRO_0000117642"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..293
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 348 AA; 37952 MW; DD213E6E10827EB9 CRC64;
MSPYITASLL FGLLLGPTIT ATSSHWLIAW MGLEINTLAI IPLMAQHHHP RAVEATTKYF
LTQATAAAML LFASTTNAWL TGQWELQQMT HPLPSTLIIL ALALKIGLAP LHTWLPEVLQ
GLDLTTGLIL STWQKLAPFA LLLQLQPNNP TLLVILGVLS TLIGGWGGLN QTQLRKILAY
SSIAHLGWMI LILQFSPTLT LLTLMLYLIM TSSAFLTFIL NKTTTINALA TSWAKTPILT
SLLPLVLLSL GGLPPLTGFM PKWLILQELT KHDLAPTATL AALSALLSLY FYLRLSYAMT
LTIAPNNLTG TLPWRTQTTQ PNMMTATMAA SSILLLPMTP GILTLFNI