ID A0A343VWK1_SYLVI Unreviewed; 344 AA. AC A0A343VWK1; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 31-JUL-2019, entry version 7. DE RecName: Full=NADH-ubiquinone oxidoreductase chain 2 {ECO:0000256|RuleBase:RU003403, ECO:0000256|SAAS:SAAS00093744}; DE EC=7.1.1.2 {ECO:0000256|RuleBase:RU003403, ECO:0000256|SAAS:SAAS01109717}; GN Name=ND2 {ECO:0000313|EMBL:AVP81792.1}; OS Sylvirana nigrovittata (Black-striped frog) (Hylarana nigrovittata). OG Mitochondrion {ECO:0000313|EMBL:AVP81792.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; OC Sylvirana. OX NCBI_TaxID=127021 {ECO:0000313|EMBL:AVP81792.1}; RN [1] {ECO:0000313|EMBL:AVP81792.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=29538432; DOI=10.1371/journal.pone.0192766; RA Sheridan J.A., Stuart B.L.; RT "Hidden species diversity in Sylvirana nigrovittata (Amphibia: RT Ranidae) highlights the importance of taxonomic revisions in RT biodiversity conservation."; RL PLoS ONE 13:e0192766-e0192766(2018). CC -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory CC chain NADH dehydrogenase (Complex I) that is believed to belong to CC the minimal assembly required for catalysis. Complex I functions CC in the transfer of electrons from NADH to the respiratory chain. CC The immediate electron acceptor for the enzyme is believed to be CC ubiquinone. {ECO:0000256|RuleBase:RU003403, CC ECO:0000256|SAAS:SAAS00093760}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 CC H(+)(out) + NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, CC Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, CC ChEBI:CHEBI:17976, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; CC EC=7.1.1.2; Evidence={ECO:0000256|RuleBase:RU003403, CC ECO:0000256|SAAS:SAAS01125045}; CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000256|RuleBase:RU003403, ECO:0000256|SAAS:SAAS00387338}; CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU003403, CC ECO:0000256|SAAS:SAAS00387338}. CC -!- SIMILARITY: Belongs to the complex I subunit 2 family. CC {ECO:0000256|RuleBase:RU003403, ECO:0000256|SAAS:SAAS00573211}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; MG606946; AVP81792.1; -; Genomic_DNA. 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 {ECO:0000256|RuleBase:RU003403, KW ECO:0000256|SAAS:SAAS00093681}; KW Membrane {ECO:0000256|RuleBase:RU003403, KW ECO:0000256|SAAS:SAAS00464716}; KW Mitochondrion {ECO:0000256|RuleBase:RU003403, KW ECO:0000256|SAAS:SAAS00093699, ECO:0000313|EMBL:AVP81792.1}; KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU003403, KW ECO:0000256|SAAS:SAAS00093736}; KW NAD {ECO:0000256|RuleBase:RU003403, ECO:0000256|SAAS:SAAS00464384}; KW Respiratory chain {ECO:0000256|RuleBase:RU003403, KW ECO:0000256|SAAS:SAAS00464594}; Signal {ECO:0000256|SAM:SignalP}; KW Translocase {ECO:0000256|RuleBase:RU003403, KW ECO:0000256|SAAS:SAAS01109684}; KW Transmembrane {ECO:0000256|RuleBase:RU003403, KW ECO:0000256|SAAS:SAAS00464491}; KW Transmembrane helix {ECO:0000256|RuleBase:RU003403, KW ECO:0000256|SAAS:SAAS00093666}; KW Transport {ECO:0000256|SAAS:SAAS00464711}; KW Ubiquinone {ECO:0000256|RuleBase:RU003403, KW ECO:0000256|SAAS:SAAS00464648}. FT SIGNAL 1 16 {ECO:0000256|SAM:SignalP}. FT CHAIN 17 344 NADH-ubiquinone oxidoreductase chain 2. FT {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5016963562. FT TRANSMEM 58 80 Helical. {ECO:0000256|RuleBase:RU003403}. FT TRANSMEM 92 114 Helical. {ECO:0000256|RuleBase:RU003403}. FT TRANSMEM 121 141 Helical. {ECO:0000256|RuleBase:RU003403}. FT TRANSMEM 147 165 Helical. {ECO:0000256|RuleBase:RU003403}. FT TRANSMEM 201 221 Helical. {ECO:0000256|RuleBase:RU003403}. FT TRANSMEM 233 254 Helical. {ECO:0000256|RuleBase:RU003403}. FT TRANSMEM 274 301 Helical. {ECO:0000256|RuleBase:RU003403}. FT TRANSMEM 322 343 Helical. {ECO:0000256|RuleBase:RU003403}. FT DOMAIN 23 283 Proton_antipo_M. {ECO:0000259|Pfam: FT PF00361}. FT DOMAIN 289 340 NADH_dehy_S2_C. {ECO:0000259|Pfam: FT PF06444}. SQ SEQUENCE 344 AA; 38348 MW; F69781CB371EC405 CRC64; MLRMATTLMM FSLALGTTLT LSSHHWILAW MGLEINSLAI IPLITTKPHP RAIEAASKYF LTQATASALI LFSSLINAWY TGGWDIHTLN DLPTNAITIA LMMKLGLVPV HFWMPEVIQG TPLFTGLILS TWQKVAPMAI IVQCSHLMNL NLVILLGFAS ILIAGWSGIS QTQLRKIMAF SSIGHLGWTI LVLKLSPELA LYNFFLYVIM TTAMFATLIS INTTKMSEIA TSFYKNPYLT LITMLLLLSL AGLPPLTGFI PKILISLELI KYNAILLATM VMLISMLSLF FYLRLSYLLF LTMSPNIFNS SSMWRTSKNH HIIHALIDLL ALMILPLTPS VLFL //