ID V5N318_9PRIM Unreviewed; 347 AA. AC V5N318; DT 19-FEB-2014, integrated into UniProtKB/TrEMBL. DT 19-FEB-2014, sequence version 1. DT 20-JAN-2016, entry version 16. DE RecName: Full=NADH-ubiquinone oxidoreductase chain 2 {ECO:0000256|RuleBase:RU003403, ECO:0000256|SAAS:SAAS00387861}; DE EC=1.6.5.3 {ECO:0000256|RuleBase:RU003403, ECO:0000256|SAAS:SAAS00387747}; GN Name=ND2 {ECO:0000313|EMBL:AHA82094.1}; OS Homo heidelbergensis (Heidelberg man). OG Mitochondrion {ECO:0000313|EMBL:AHA82094.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=1425170 {ECO:0000313|EMBL:AHA82094.1}; RN [1] {ECO:0000313|EMBL:AHA82094.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Femur VIII {ECO:0000313|EMBL:AHA82094.1}; RC TISSUE=Bone {ECO:0000313|EMBL:AHA82094.1}; RX PubMed=24305051; RA Meyer M., Fu Q., Aximu-Petri A., Glocke I., Nickel B., Arsuaga J.L., RA Martinez I., Gracia A., de Castro J.M., Carbonell E., Paabo S.; RT "A mitochondrial genome sequence of a hominin from Sima de los RT Huesos."; RL Nature 505:403-406(2014). 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 (By similarity). {ECO:0000256|SAAS:SAAS00387883}. CC -!- CATALYTIC ACTIVITY: NADH + ubiquinone + 5 H(+)(In) = NAD(+) + CC ubiquinol + 4 H(+)(Out). {ECO:0000256|RuleBase:RU003403, CC ECO:0000256|SAAS:SAAS00387632}. 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}. 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; KF683087; AHA82094.1; -; Genomic_DNA. DR RefSeq; YP_008963988.1; NC_023100.1. DR GeneID; 17961566; -. DR CTD; 4536; -. 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:respiratory chain; 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|SAAS:SAAS00093681}; KW Membrane {ECO:0000256|SAAS:SAAS00093718, ECO:0000256|SAM:Phobius}; KW Mitochondrion {ECO:0000256|RuleBase:RU000318, KW ECO:0000256|SAAS:SAAS00093699, ECO:0000313|EMBL:AHA82094.1}; KW Mitochondrion inner membrane {ECO:0000256|SAAS:SAAS00093736}; KW NAD {ECO:0000256|RuleBase:RU000317, ECO:0000256|SAAS:SAAS00093707}; KW Oxidoreductase {ECO:0000256|RuleBase:RU000317, KW ECO:0000256|SAAS:SAAS00093734}; KW Respiratory chain {ECO:0000256|SAAS:SAAS00093685}; KW Transmembrane {ECO:0000256|SAAS:SAAS00093696, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00093666, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|SAAS:SAAS00093687}; KW Ubiquinone {ECO:0000256|RuleBase:RU000318, KW ECO:0000256|SAAS:SAAS00093675}. FT TRANSMEM 56 76 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 96 115 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 151 171 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 178 196 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 202 219 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 239 257 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 277 305 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 325 344 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 23 284 Proton_antipo_M. {ECO:0000259|Pfam: FT PF00361}. FT DOMAIN 290 343 NADH_dehy_S2_C. {ECO:0000259|Pfam: FT PF06444}. SQ SEQUENCE 347 AA; 38887 MW; 5C9A30A2742F700C CRC64; MNPLAQPXXX STIFTGTLIT ALSSHWFFTW VGLEMNMLAF IPVLTKKMNP RSTEAAIKYF LTQATASMIL LMAILFNNML SGQWTMTNTX XXXXSLMIMM AMAMKLGMAP FHFWVPEVTQ GTPLTSGLLL LTWQKLAPIS IMYQISPSLN VSLLLTLSIL SIMAGSWGGL NQTQLRKILA YSSITHMGWM MAVLPYNPNM TILNLTIYIX LTTTAFLLLN LNSSTTTLLL SRTWNKLTWL TPLIPSTLLS LGGLPPLTGF LPKWAIIEEF TKNNSLIIPT IMATITLLNL YFYLRLIYST SITLLPMSNN VKMKWQFEHT KPTPFLPTLI ALTTLLLPIS PFMLXXX //