ID NB8M_HUMAN STANDARD; PRT; 134 AA. AC P17568; DT 01-AUG-1990 (Rel. 15, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE NADH-UBIQUINONE OXIDOREDUCTASE B18 SUBUNIT (EC 1.6.5.3) (EC 1.6.99.3) DE (COMPLEX I-B18) (CI-B18) (CELL ADHESION PROTEIN SQM1). GN NDUFB7. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90147818; PubMed=2302251; RA Wong Y.-C., Tsao S.-W., Kakefuda M., Bernal S.D.; RT "cDNA cloning of a novel cell adhesion protein expressed in human RT squamous carcinoma cells."; RL Biochem. Biophys. Res. Commun. 166:984-992(1990). RN [2] RP IDENTIFICATION OF PROBABLE FRAMESHIFTS. RA Bairoch A.; RL Unpublished observations (SEP-1997). CC -!- FUNCTION: TRANSFER OF ELECTRONS FROM NADH TO THE RESPIRATORY CC CHAIN. THE IMMEDIATE ELECTRON ACCEPTOR FOR THE ENZYME IS BELIEVED CC TO BE UBIQUINONE. CC -!- CATALYTIC ACTIVITY: NADH + UBIQUINONE = NAD(+) + UBIQUINOL. CC -!- SUBUNIT: COMPLEX I IS COMPOSED OF ABOUT 40 DIFFERENT SUBUNITS. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL INNER MEMBRANE; MATRIX SIDE. CC -!- CAUTION: THE RECONSTRUCTION OF THE SEQUENCE WAS HELPED BY TWO CC PARTIAL EST SEQUENCES (AA548676 AND N31341). THERE ARE PROBABLY CC SOME MORE ERRORS IN THE C-TERMINAL PART. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M33374; AAA35675.1; -. DR PIR; A34653; A34653. DR MIM; 603842; -. KW Oxidoreductase; NAD; Ubiquinone; Mitochondrion; Myristate. FT INIT_MET 0 0 BY SIMILARITY. FT LIPID 1 1 MYRISTATE (BY SIMILARITY). FT CONFLICT 74 81 NFLACKQE -> SCWPASRK (IN REF. 1). FT CONFLICT 85 92 WDYCEHRD -> SGLLRTAS (IN REF. 1). SQ SEQUENCE 134 AA; 15648 MW; 4D15DAEE84AC92CF CRC64; GAHLVRRYLG DASVEPDPLQ MPTFPPDYGF PERKEREMVA TQQEMMDASE AQLRDYCAHH LIRLLKCKRD SFPNFLACKQ ERHDWDYCEH RDYVMRMKEF ERDEGCSSGR SGGRRRRQIC KGQGPGEVDP KVAL //