ID CALB_MOUSE STANDARD; PRT; 169 AA. AC Q63810; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE CALCINEURIN B SUBUNIT ISOFORM 1 (PROTEIN PHOSPHATASE 2B REGULATORY DE SUBUNIT). GN PPP3R1 OR CNB. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=BRAIN; RX MEDLINE=92392379; PubMed=1325794; RA Ueki K., Muramatsu T., Kincaid R.L.; RT "Structure and expression of two isoforms of the murine calmodulin- RT dependent protein phosphatase regulatory subunit (calcineurin B)."; RL Biochem. Biophys. Res. Commun. 187:537-543(1992). CC -!- FUNCTION: CALCINEURIN IS A CALCIUM BINDING AND CALMODULIN BINDING CC PROTEIN FOUND IN ALL CELLS FROM YEAST TO MAMMALS, IT IS A CALCIUM CC DEPENDENT, CALMODULIN STIMULATED PROTEIN PHOSPHATASE. CC -!- SUBUNIT: COMPOSED OF TWO COMPONENTS (A AND B), THE A COMPONENT IS CC THE CATALYTIC SUBUNIT AND THE B COMPONENT CONFERS CALCIUM CC SENSITIVITY. CC -!- ALTERNATIVE PRODUCTS: TWO FORMS OF CNB ARE PRODUCED BY ALTERNATIVE CC SPLICING. THEY DIFFER IN THE N-TERMINAL REGION. CC -!- MISCELLANEOUS: THIS PROTEIN HAS FOUR FUNCTIONAL CALCIUM-BINDING CC SITES. CC -!- SIMILARITY: TO OTHER EF-HAND CALCIUM BINDING PROTEINS. 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; S43864; AAB23171.1; -. DR HSSP; P06705; 1AUI. DR MGD; MGI:107172; Ppp3r1. DR INTERPRO; IPR002048; -. DR PFAM; PF00036; efhand; 4. DR PROSITE; PS00018; EF_HAND; 4. KW Calcium-binding; Repeat; Alternative splicing; Myristate. FT INIT_MET 0 0 BY SIMILARITY. FT LIPID 1 1 MYRISTATE (BY SIMILARITY). FT CA_BIND 30 41 SITE 1. FT CA_BIND 62 73 SITE 2. FT CA_BIND 99 110 SITE 3. FT CA_BIND 140 151 SITE 4. SQ SEQUENCE 169 AA; 19142 MW; D1490BA5BD2F432F CRC64; GSEASYPLEM CSHFDADEIK RLGKRFKKLD LDNSGSLSVE EFMSLPELQQ NPLVQRVIDI FDTDGNGEVD FKEFIEGVSQ FSVKGDKEQK LRFAFRIYDM DKDGYISNGE LFQVLKMMVG NNLKDTQLQQ IVDKTIINAD KDGDGRISFE EFCAVVGGLD IHKKMVVDV //