ID KAPCA_CRIGR STANDARD; PRT; 350 AA. AC P25321; DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1992, sequence version 1. DT 07-MAR-2006, entry version 49. DE cAMP-dependent protein kinase, alpha-catalytic subunit (EC 2.7.1.37) DE (PKA C-alpha). 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: Cytoplasmic (inactive holoenzyme and CC monomeric catalytic subunit). Translocates into the nucleus CC (monomeric catalytic subunit) (By similarity). CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in mammalian tissues. CC -!- PTM: Asn-2 is partially deaminated to Asp-2 giving rise to 2 major CC isoelectric variants, called CB and CA respectively (By CC similarity). CC -!- SIMILARITY: Belongs to the Ser/Thr protein kinase family. cAMP CC subfamily. 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 HSSP; P36887; 1CTP. DR SMR; P25321; 9-350. DR InterPro; IPR000961; Pkinase_C. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR002290; Ser_thr_pkinase. DR InterPro; IPR001245; Tyr_pkinase. DR Pfam; PF00069; Pkinase; 1. DR Pfam; PF00433; Pkinase_C; 1. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00133; S_TK_X; 1. DR SMART; SM00220; S_TKc; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. KW ATP-binding; cAMP; Kinase; Lipoprotein; Myristate; Nuclear protein; KW Nucleotide-binding; Phosphorylation; Serine/threonine-protein kinase; KW Transferase. FT INIT_MET 0 0 By similarity. FT CHAIN 1 350 cAMP-dependent protein kinase, alpha- FT catalytic subunit. FT /FTId=PRO_0000086051. FT DOMAIN 43 297 Protein kinase. FT NP_BIND 49 57 ATP (By similarity). FT ACT_SITE 166 166 Proton acceptor (By similarity). FT BINDING 72 72 ATP (By similarity). FT MOD_RES 2 2 Deamidated asparagine (partial) (By FT similarity). FT MOD_RES 10 10 Phosphoserine (by autocatalysis) (By FT similarity). FT MOD_RES 139 139 Phosphoserine (By similarity). FT MOD_RES 195 195 Phosphothreonine (By similarity). FT MOD_RES 197 197 Phosphothreonine (By similarity). FT MOD_RES 338 338 Phosphoserine (By similarity). FT LIPID 1 1 N-myristoyl glycine (By similarity). SQ SEQUENCE 350 AA; 40489 MW; 2EFC89F73A0DE53D CRC64; 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 //