ID KAPA_CRIGR STANDARD; PRT; 350 AA. AC P25321; DT 01-MAY-1992 (REL. 22, CREATED) DT 01-MAY-1992 (REL. 22, LAST SEQUENCE UPDATE) DT 01-NOV-1997 (REL. 35, LAST ANNOTATION UPDATE) DE CAMP-DEPENDENT PROTEIN KINASE, ALPHA-CATALYTIC SUBUNIT (EC 2.7.1.37) DE (PKA C-ALPHA). GN PRKACA. OS CRICETULUS GRISEUS (CHINESE HAMSTER). OC EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; MAMMALIA; EUTHERIA; OC RODENTIA; SCIUROGNATHI; MURIDAE; CRICETINAE; CRICETULUS. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 91244783. RA HOWARD P., DAY K.H., KIM K.E., RICHARDSON J., THOMAS J., ABRAHAM I., RA FLEISCHMANN R.D., GOTTESMAN M.M., MAURER R.A.; RT "Decreased catalytic subunit mRNA levels and altered catalytic RT subunit mRNA structure in a cAMP-resistant Chinese hamster ovary cell RT line."; RL J. BIOL. CHEM. 266:10189-10195(1991). CC -!- CATALYTIC ACTIVITY: ATP + A PROTEIN = ADP + A PHOSPHOPROTEIN. CC -!- ENZYME REGULATION: THIS ENZYME IS ACTIVATED BY CAMP. CC -!- SUBUNIT: COMPOSED OF TWO REGULATORY CHAINS AND TWO CATALYTIC CC CHAINS. 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; M63311; G191175; -. DR PIR; B40384; OKHYCA. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PFAM; PF00069; pkinase; 1. DR PFAM; PF00433; pkinase_C; 1. DR HSSP; P05132; 1CTP. KW TRANSFERASE; SERINE/THREONINE-PROTEIN KINASE; ATP-BINDING; CAMP; KW PHOSPHORYLATION; MYRISTYLATION; MULTIGENE FAMILY. FT INIT_MET 0 0 FT LIPID 1 1 MYRISTATE (BY SIMILARITY). FT DOMAIN 43 297 PROTEIN KINASE. FT NP_BIND 49 57 ATP (BY SIMILARITY). FT BINDING 72 72 ATP (BY SIMILARITY). FT ACT_SITE 166 166 BY SIMILARITY. FT MOD_RES 197 197 PHOSPHORYLATION (BY SIMILARITY). FT MOD_RES 338 338 PHOSPHORYLATION (BY SIMILARITY). SQ SEQUENCE 350 AA; 40488 MW; 687A12CB CRC32; GNAAAAKKGS EQESVKEFLA KAKEEFLKKW ESPSQNTAQL DHFDRIKTLG TGSFGRVMLV KHKETGNHYA MKILDKQKVV KLKQIEHTLN EKRILQAVNF PFLVKLEFSF KDNSNLYMVM EYVPGGEMFS HLRRIGRFSE PHARFYAAQI VLTFEYLHSL DLIYRDLKPE NLLIDQQGYI QVTDFGFAKR VKGRTWTLCG TPEYLAPEII LSKGYNKAVD WWALGVLIYE MAAGYPPFFA DQPIQIYEKI VSGKVRFPSH FSSDLKDLLR NLLQVDLTKR FGNLKNGVND IKNHKWFATT DWIAIYQRKV EAPFIPKFKG PGDTSNFDDY EEEEIRVSIN EKCGKEFTEF //