ID KAPCA_CRIGR Reviewed; 351 AA. AC P25321; DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 10-AUG-2010, entry version 84. DE RecName: Full=cAMP-dependent protein kinase catalytic subunit alpha; DE Short=PKA C-alpha; DE EC=2.7.11.11; GN Name=PRKACA; OS Cricetulus griseus (Chinese hamster). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Cricetidae; Cricetinae; Cricetulus. OX NCBI_TaxID=10029; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=91244783; PubMed=1645343; 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 subunit RT mRNA structure in a cAMP-resistant Chinese hamster ovary cell line."; RL J. Biol. Chem. 266:10189-10195(1991). CC -!- FUNCTION: Phosphorylates a large number of substrates in the CC cytoplasm and the nucleus. CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC -!- ENZYME REGULATION: Activated by cAMP. CC -!- SUBUNIT: A number of inactive tetrameric holoenzymes are produced CC by the combination of homo- or heterodimers of the different CC regulatory subunits associated with two catalytic subunits. cAMP CC causes the dissociation of the inactive holoenzyme into a dimer of CC regulatory subunits bound to four cAMP and two free monomeric CC catalytic subunits. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By CC similarity). Note=Translocates into the nucleus (monomeric CC catalytic subunit) (By similarity). The inactive holoenzyme is CC found in the cytoplasm (By similarity). CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in mammalian tissues. CC -!- PTM: Asn-3 is partially deaminated to Asp giving rise to 2 major CC isoelectric variants, called CB and CA respectively (By CC similarity). CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr CC protein kinase family. cAMP subfamily. CC -!- SIMILARITY: Contains 1 AGC-kinase C-terminal domain. CC -!- SIMILARITY: Contains 1 protein kinase domain. 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; AAA37010.1; -; mRNA. DR PIR; B40384; OKHYCA. DR ProteinModelPortal; P25321; -. DR SMR; P25321; 13-351. DR HOVERGEN; HBG108317; -. DR BRENDA; 2.7.11.11; 18. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004691; F:cAMP-dependent protein kinase activity; IEA:EC. DR GO; GO:0006468; P:protein amino acid phosphorylation; IEA:InterPro. DR InterPro; IPR000961; AGC-kinase_C. DR InterPro; IPR011009; Kinase-like_dom. DR InterPro; IPR000719; Prot_kinase_cat_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR017442; Se/Thr_prot_kinase-like_dom. DR InterPro; IPR008271; Ser/Thr_prot_kinase_AS. DR InterPro; IPR002290; Ser/Thr_prot_kinase_dom. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00133; S_TK_X; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Kinase_like; 1. DR PROSITE; PS51285; AGC_KINASE_CTER; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 2: Evidence at transcript level; KW ATP-binding; cAMP; Cytoplasm; Kinase; Lipoprotein; Myristate; KW Nucleotide-binding; Nucleus; Phosphoprotein; KW Serine/threonine-protein kinase; Transferase. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 351 cAMP-dependent protein kinase catalytic FT subunit alpha. FT /FTId=PRO_0000086051. FT DOMAIN 44 298 Protein kinase. FT DOMAIN 299 351 AGC-kinase C-terminal. FT NP_BIND 50 58 ATP (By similarity). FT ACT_SITE 167 167 Proton acceptor (By similarity). FT BINDING 73 73 ATP (By similarity). FT MOD_RES 3 3 Deamidated asparagine (By similarity). FT MOD_RES 11 11 Phosphoserine; by autocatalysis (By FT similarity). FT MOD_RES 35 35 Phosphoserine (By similarity). FT MOD_RES 49 49 Phosphothreonine (By similarity). FT MOD_RES 140 140 Phosphoserine (By similarity). FT MOD_RES 196 196 Phosphothreonine (By similarity). FT MOD_RES 198 198 Phosphothreonine (By similarity). FT MOD_RES 202 202 Phosphothreonine (By similarity). FT MOD_RES 339 339 Phosphoserine (By similarity). FT LIPID 2 2 N-myristoyl glycine (By similarity). SQ SEQUENCE 351 AA; 40620 MW; 84333CD0B439F356 CRC64; MGNAAAAKKG SEQESVKEFL AKAKEEFLKK WESPSQNTAQ LDHFDRIKTL GTGSFGRVML VKHKETGNHY AMKILDKQKV VKLKQIEHTL NEKRILQAVN FPFLVKLEFS FKDNSNLYMV MEYVPGGEMF SHLRRIGRFS EPHARFYAAQ IVLTFEYLHS LDLIYRDLKP ENLLIDQQGY IQVTDFGFAK RVKGRTWTLC GTPEYLAPEI ILSKGYNKAV DWWALGVLIY EMAAGYPPFF ADQPIQIYEK IVSGKVRFPS HFSSDLKDLL RNLLQVDLTK RFGNLKNGVN DIKNHKWFAT TDWIAIYQRK VEAPFIPKFK GPGDTSNFDD YEEEEIRVSI NEKCGKEFTE F //