ID   A0A068EV73_9TELE        Unreviewed;       348 AA.
AC   A0A068EV73;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-NOV-2024, entry version 42.
DE   RecName: Full=NADH-ubiquinone oxidoreductase chain 2 {ECO:0000256|ARBA:ARBA00021008, ECO:0000256|RuleBase:RU003403};
DE            EC=7.1.1.2 {ECO:0000256|ARBA:ARBA00012944, ECO:0000256|RuleBase:RU003403};
GN   Name=ND2 {ECO:0000313|EMBL:AID52436.1};
OS   Rhynchocypris lagowskii (Amur minnow).
OG   Mitochondrion {ECO:0000313|EMBL:AID52436.1}.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Leuciscidae; Pseudaspininae; Rhynchocypris.
OX   NCBI_TaxID=219677 {ECO:0000313|EMBL:AID52436.1};
RN   [1] {ECO:0000313|EMBL:AID52436.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=24865913;
RA   Sun Q., Wang D., Wei Q.;
RT   "The complete mitochondrial gemone of Phoxinus lagowskii (Teleostei,
RT   Cypriniformes: Cyprinidae).";
RL   Mitochondrial DNA 0:0-0(2014).
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:0000256|RuleBase:RU003403}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ubiquinone + NADH + 5 H(+)(in) = a ubiquinol + NAD(+) + 4
CC         H(+)(out); 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:0000256|ARBA:ARBA00000766,
CC         ECO:0000256|RuleBase:RU003403};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000256|ARBA:ARBA00004448, ECO:0000256|RuleBase:RU003403}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004448,
CC       ECO:0000256|RuleBase:RU003403}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 2 family.
CC       {ECO:0000256|ARBA:ARBA00007012, ECO:0000256|RuleBase:RU003403}.
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DR   EMBL; KJ641843; AID52436.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A068EV73; -.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
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; IPR050175; Complex_I_Subunit_2.
DR   InterPro; IPR010933; NADH_DH_su2_C.
DR   InterPro; IPR003917; NADH_UbQ_OxRdtase_chain2.
DR   InterPro; IPR001750; ND/Mrp_mem.
DR   PANTHER; PTHR46552; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 2; 1.
DR   PANTHER; PTHR46552:SF1; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 2; 1.
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 {ECO:0000256|ARBA:ARBA00022982,
KW   ECO:0000256|RuleBase:RU003403};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU003403};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW   ECO:0000256|RuleBase:RU003403};
KW   Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792,
KW   ECO:0000256|RuleBase:RU003403};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU003403};
KW   Respiratory chain {ECO:0000256|ARBA:ARBA00022660,
KW   ECO:0000256|RuleBase:RU003403};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU003403};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU003403};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU003403}; Transport {ECO:0000256|ARBA:ARBA00022448};
KW   Ubiquinone {ECO:0000256|ARBA:ARBA00023075, ECO:0000256|RuleBase:RU003403}.
FT   TRANSMEM        57..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003403"
FT   TRANSMEM        92..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003403"
FT   TRANSMEM        152..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003403"
FT   TRANSMEM        178..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003403"
FT   TRANSMEM        202..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003403"
FT   TRANSMEM        274..294
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003403"
FT   TRANSMEM        326..347
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003403"
FT   DOMAIN          23..288
FT                   /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT                   subunit"
FT                   /evidence="ECO:0000259|Pfam:PF00361"
FT   DOMAIN          290..344
FT                   /note="NADH dehydrogenase subunit 2 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06444"
SQ   SEQUENCE   348 AA;  37567 MW;  24A160198FCD9AA8 CRC64;
     MNPYVLMTLL SSLGLGTTLT FASSHWLLAW MGLEINTLAI VPLMAQHHHP RAVEATTKYF
     LVQATAAAMI LFASTTNAWI TGQWDINGID SPIATTMVMA ALALKIGLAP MHLWMPEVLQ
     GLDLLTGLVL STWQKLAPLA LIIQAAQAID PFTLTAFGLA SALVGGWGGL NQTQLRKILA
     YSSIAHMGWM IIVLQYAPQL TLLALITYIF MTSAAFLALK ASSATKISTI AVVWSKSPTL
     TMTTALVLLS LGGLPPLTGF MPKWFIMQEL ATQNLPLTAT IMALAALLSL YFYLRLCYAM
     TLTISPNTFN STTPWRVQAA QTSLPLALST LMALALLPMA PTIMMLIT
//