ID A0A516IBF8_9GOBI Unreviewed; 348 AA. AC A0A516IBF8; DT 16-OCT-2019, integrated into UniProtKB/TrEMBL. DT 16-OCT-2019, sequence version 1. DT 13-NOV-2019, entry version 2. 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:QDP13450.1}; OS Stiphodon pelewensis. OG Mitochondrion {ECO:0000313|EMBL:QDP13450.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Gobiaria; Gobiiformes; Gobioidei; Gobiidae; Sicydiinae; Stiphodon. OX NCBI_TaxID=870289 {ECO:0000313|EMBL:QDP13450.1}; RN [1] {ECO:0000313|EMBL:QDP13450.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Atra3 {ECO:0000313|EMBL:QDP13450.1}; RA Lord C., Bellec L., Dettai A., Bonillo C., Keith P.; RT "Does your lip stick? Evolutionary aspects of the mouth morphology of RT the Indo-Pacific clinging goby of the Sicyopterus genus (Teleostei: RT Gobioidei: Sicydiinae) based on mitogenome phylogeny."; RL J. Zoolog. Syst. Evol. Res. 0:0-0(2019). RN [2] {ECO:0000313|EMBL:QDP13450.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Atra3 {ECO:0000313|EMBL:QDP13450.1}; RA Lord C.A.; RL Submitted (FEB-2019) to the EMBL/GenBank/DDBJ databases. 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; MK496967; QDP13450.1; -; Genomic_DNA. 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:QDP13450.1}; 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}; 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 TRANSMEM 7 28 Helical. {ECO:0000256|RuleBase:RU003403}. FT TRANSMEM 60 80 Helical. {ECO:0000256|RuleBase:RU003403}. FT TRANSMEM 92 115 Helical. {ECO:0000256|RuleBase:RU003403}. FT TRANSMEM 152 170 Helical. {ECO:0000256|RuleBase:RU003403}. FT TRANSMEM 177 195 Helical. {ECO:0000256|RuleBase:RU003403}. FT TRANSMEM 201 220 Helical. {ECO:0000256|RuleBase:RU003403}. FT TRANSMEM 232 253 Helical. {ECO:0000256|RuleBase:RU003403}. FT TRANSMEM 273 293 Helical. {ECO:0000256|RuleBase:RU003403}. FT TRANSMEM 323 346 Helical. {ECO:0000256|RuleBase:RU003403}. FT DOMAIN 23 287 Proton_antipo_M. {ECO:0000259|Pfam: FT PF00361}. FT DOMAIN 289 342 NADH_dehy_S2_C. {ECO:0000259|Pfam: FT PF06444}. SQ SEQUENCE 348 AA; 38058 MW; 4EC14DA39AEB8E60 CRC64; MNPYIMAFLY LCLILGTTIT VSSSHWLLAW MGLEINTLAI IPLMAQNHHP RATEAATKYF LTQATAAATL LFASITNAWL TGQWDIKLMT HPIPTTMILL ALSLKIGLAP LHTWLPEVLQ GLDLTTGLIL STWQKLAPFS LLLQIPAYSQ DLLILMGLAS TLVGGWGGLN QTQLRKILAY SSIAHLGWML IIIQFSPSLT LLALITYLVM TTSTFLILNF NDSKNINSLA TSWAKAPLMT AMTPLLLLSL GGLPPMTGFM PKWLILQELT KQQLPMTAVI AALTALLSLY FYLRLSYAMT LTITPNNLAG TTLWRFSSSH PSLVLTTATL TAILLLPLTP AVTALLTI //