ID OTC_MOUSE STANDARD; PRT; 354 AA. AC P11725; DT 01-OCT-1989 (REL. 12, CREATED) DT 01-OCT-1989 (REL. 12, LAST SEQUENCE UPDATE) DT 01-NOV-1997 (REL. 35, LAST ANNOTATION UPDATE) DE ORNITHINE CARBAMOYLTRANSFERASE PRECURSOR (EC 2.1.3.3) (OTCASE) DE (ORNITHINE TRANSCARBAMYLASE). GN OTC. OS MUS MUSCULUS (MOUSE). OC EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; MAMMALIA; EUTHERIA; OC RODENTIA; SCIUROGNATHI; MURIDAE; MURINAE; MUS. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=C57BL/6J; RX MEDLINE; 87263407. RA VERES G., GIBBS R.A., SCHERER S.E., CASKEY C.T.; RT "The molecular basis of the sparse fur mouse mutation."; RL SCIENCE 237:415-417(1987). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE; 88157717. RA SCHERER S.E., VERES G., CASKEY C.T.; RT "The genetic structure of mouse ornithine transcarbamylase."; RL NUCLEIC ACIDS RES. 16:1593-1601(1988). RN [3] RP SEQUENCE OF 1-26 FROM N.A. RC STRAIN=C57BL/6J; RX MEDLINE; 86224037. RA VERES G., CRAIGEN W.J., CASKEY C.T.; RT "The 5' flanking region of the ornithine transcarbamylase gene RT contains DNA sequences regulating tissue-specific expression."; RL J. BIOL. CHEM. 261:7588-7591(1986). CC -!- CATALYTIC ACTIVITY: CARBAMOYL PHOSPHATE + ORNITHINE = CITRULLINE CC + ORTHOPHOSPHATE. CC -!- PATHWAY: SECOND STEP IN UREA CYCLE, ARGININE BIOSYNTHESIS. CC -!- SUBUNIT: HOMOTRIMER. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL MATRIX. CC -!- DISEASE: SPARSE FUR (SPF) MOUSE HAVE AN OTC WITH AN OVERALL CC DECREASE IN ACTIVITY, AND ALTERED SUBSTRATE AFFINITY. CC -!- SIMILARITY: STRONG TO ALL OTHER OTCASES, ALSO HIGH TO ATCASES. 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 -------------------------------------------------------------------------- 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; M17030; G200163; -. DR EMBL; M12716; G554248; ALT_SEQ. DR EMBL; X07092; G762985; -. DR EMBL; X07093; G762985; JOINED. DR EMBL; X07094; G762985; JOINED. DR EMBL; X07095; G762985; JOINED. DR EMBL; X07096; G762985; JOINED. DR EMBL; X07097; G762985; JOINED. DR EMBL; X07098; G762985; JOINED. DR EMBL; X07099; G762985; JOINED. DR EMBL; X07100; G762985; JOINED. DR PIR; S03407; OWMS. DR PIR; A43609; A43609. DR MGD; MGI:97448; OTC. DR PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1. DR PFAM; PF00185; OTCace; 1. DR HSSP; P04391; 1AKM. KW ARGININE BIOSYNTHESIS; UREA CYCLE; TRANSFERASE; MITOCHONDRION; KW TRANSIT PEPTIDE. FT TRANSIT 1 32 MITOCHONDRION. FT CHAIN 33 354 ORNITHINE CARBAMOYLTRANSFERASE. FT VARIANT 117 117 H -> N (IN SPARSE FUR MOUSE). FT CONFLICT 195 195 G -> R (IN REF. 2). SQ SEQUENCE 354 AA; 39765 MW; 6F1033BE CRC32; MLSNLRILLN NAALRKGHTS VVRHFWCGKP VQSQVQLKGR DLLTLKNFTG EEIQYMLWLS ADLKFRIKQK GEYLPLLQGK SLGMIFEKRS TRTRLSTETG FALLGGHPSF LTTQDIHLGV NESLTDTARV LSSMTDAVLA RVYKQSDLDT LAKEASIPIV NGLSDLYHPI QILADYLTLQ EHYGSLKGLT LSWIGDGNNI LHSIMMSAAK FGMHLQAATP KGYEPDPNIV KLAEQYAKEN GTKLSMTNDP LEAARGGNVL ITDTWISMGQ EDEKKKRLQA FQGYQVTMKT AKVAASDWTF LHCLPRKPEE VDDEVFYSPR SLVFPEAENR KWTIMAVMVS LLTDYSPVLQ KPKF //