NU2M_LATCH
ID NU2M_LATCH Reviewed; 348 AA.
AC O03166;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 101.
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 Latimeria chalumnae (Coelacanth).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=9215903; DOI=10.1093/genetics/146.3.995;
RA Zardoya R., Meyer A.;
RT "The complete DNA sequence of the mitochondrial genome of a 'living
RT fossil,' the coelacanth (Latimeria chalumnae).";
RL Genetics 146:995-1010(1997).
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; U82228; AAC60319.1; -; Genomic_DNA.
DR PIR; B58892; B58892.
DR RefSeq; NP_008330.1; NC_001804.1.
DR AlphaFoldDB; O03166; -.
DR SMR; O03166; -.
DR STRING; 7897.ENSLACP00000021806; -.
DR Ensembl; ENSLACT00000024849; ENSLACP00000021806; ENSLACG00000022065.
DR GeneID; 808084; -.
DR KEGG; lcm:808084; -.
DR CTD; 4536; -.
DR eggNOG; KOG4668; Eukaryota.
DR GeneTree; ENSGT00730000111348; -.
DR HOGENOM; CLU_007100_1_3_1; -.
DR InParanoid; O03166; -.
DR OMA; HFWVPEV; -.
DR OrthoDB; 1153818at2759; -.
DR TreeFam; TF343996; -.
DR Proteomes; UP000008672; Mitochondrion.
DR Bgee; ENSLACG00000022065; Expressed in pelvic fin and 6 other tissues.
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_0000117599"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 326..346
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 348 AA; 38165 MW; 11E22A9210B9638A CRC64;
MSPYVTMILI SSLGLGTTIT FTSSSWLMAW MGLEINTLAI TPLMVKQHHP RATEATTKYF
LTQATASGLL LFATLNNAWM TGEWNTMELS NNLSAPMITM ALALKMGVAP MHFWLPEVLQ
GLPLLTGLIL STWQKLAPFT LLYMTSHELN TTTMTILGLT STIIGGLGGL NQTQLRKVLA
YSSIAHLGWM VIIIQYSKTL ALLNLLLYIT MTSTAFLTLM TLSATKINTL STKWATTPIA
TMTAMLALLA LGGLPPLTGF MPKWLILQEL TKQNLPALAT LMALSALLSL FFYLRMCHTM
TLTISPNTNN NMITWRKKPG QKALPLAMLS IMTLMALPTT PTMVAIMN