Reviewed, UniProtKB/Swiss-Prot P36887 (KAPCA_PIG)

Names and origin

Protein names

Recommended name:
    cAMP-dependent protein kinase catalytic subunit alpha
      Short name=PKA C-alpha
    EC=2.7.11.11

Gene names

Name:

PRKACA

Organism

Sus scrofa (Pig)

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length	351 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Phosphorylates a large number of substrates in the cytoplasm and the nucleus.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	Activated by cAMP.
Subunit structure	A number of inactive tetrameric holoenzymes are produced by the combination of homo- or heterodimers of the different regulatory subunits associated with two catalytic subunits. cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to four cAMP and two free monomeric catalytic subunits.
Subcellular location	Cytoplasm By similarity. Nucleus By similarity. Note: Translocates into the nucleus (monomeric catalytic subunit) By similarity. The inactive holoenzyme is found in the cytoplasm By similarity.
Tissue specificity	Ubiquitously expressed in mammalian tissues.
Post-translational modification	Asn-3 is deaminated to Asp in more than 25% of the proteins, giving rise to 2 major isoelectric variants, called CB and CA respectively (0.4 pH unit change). Deamidation proceeds via the so-called beta-aspartyl shift mechanism and yields either 'D-Asp-2' (major) or 'D-isoAsp-2' (minor), in addition to L-isomers. Deamidation occurs after the addition of myristate. The Asn-3 form reaches a significantly larger nuclear/cytoplasmic ratio than the 'Asp-2' form.
Sequence similarities	Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. cAMP subfamily. Contains 1 AGC-kinase C-terminal domain. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Ligand	ATP-binding Nucleotide-binding cAMP
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Lipoprotein Myristate Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW cAMP-dependent protein kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.2

Chain

2 – 351

350

cAMP-dependent protein kinase catalytic subunit alpha

PRO_0000086054

Regions

Domain

44 – 298

255

Protein kinase

Domain

299 – 351

53

AGC-kinase C-terminal

Nucleotide binding

50 – 58

9

ATP

Sites

Active site

167

1

Proton acceptor By similarity

Binding site

73

1

ATP

Amino acid modifications

Modified residue

3

1

Deamidated asparagine; partial

Modified residue

11

1

Phosphoserine; by autocatalysis By similarity

Modified residue

49

1

Phosphothreonine By similarity

Modified residue

140

1

Phosphoserine By similarity

Modified residue

196

1

Phosphothreonine By similarity

Modified residue

198

1

Phosphothreonine By similarity

Modified residue

202

1

Phosphothreonine By similarity

Modified residue

339

1

Phosphoserine By similarity

Lipidation

2

1

N-myristoyl glycine

Secondary structure

1

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351

Helix Strand Turn

Details...

Helix

9 – 32

24

Helix

41 – 43

3

Beta strand

44 – 51

8

Beta strand

54 – 63

10

Turn

64 – 66

3

Beta strand

69 – 76

8

Helix

77 – 82

6

Helix

86 – 96

11

Beta strand

107 – 112

6

Beta strand

114 – 122

9

Helix

130 – 136

7

Helix

141 – 160

20

Helix

170 – 172

3

Beta strand

173 – 175

3

Beta strand

181 – 183

3

Helix

203 – 205

3

Helix

208 – 211

4

Helix

219 – 234

16

Helix

244 – 253

10

Helix

264 – 273

10

Turn

278 – 280

3

Turn

282 – 284

3

Turn

286 – 289

4

Helix

290 – 293

4

Helix

296 – 298

3

Helix

303 – 307

5

Turn

345 – 350

6

Sequences

	Sequence		Length	Mass (Da)
	P36887-1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: B65EC7C42DD56DE5	FASTA	351	40,617
	10 20 30 40 50 60 MGNAAAAKKG SEQESVKEFL AKAKEDFLKK WENPAQNTAH LDQFERIKTL GTGSFGRVML 70 80 90 100 110 120 VKHKETGNHF AMKILDKQKV VKLKQIEHTL NEKRILQAVN FPFLVKLEYS FKDNSNLYMV 130 140 150 160 170 180 MEYVPGGEMF SHLRRIGRFS EPHARFYAAQ IVLTFEYLHS LDLIYRDLKP ENLLIDQQGY 190 200 210 220 230 240 IQVTDFGFAK RVKGRTWTLC GTPEYLAPEI ILSKGYNKAV DWWALGVLIY EMAAGYPPFF 250 260 270 280 290 300 ADQPIQIYEK IVSGKVRFPS HFSSDLKDLL RNLLQVDLTK RFGNLKNGVN DIKNHKWFAT 310 320 330 340 350 TDWIAIYQRK VEAPFIPKFK GPGDTSNFDD YEEEEIRVSI NEKCGKEFSE F

References

[1]	"Multiple mRNA species code for the catalytic subunit of the cAMP-dependent protein kinase from LLC-PK1 cells. Evidence for two forms of the catalytic subunit." Adavani S.R., Schwarz M., Showers M.O., Maurer R.A., Hemmings B.A. Eur. J. Biochem. 167:221-226(1987) [PubMed: 2441988] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 195-351.
[2]	"A conserved deamidation site at Asn 2 in the catalytic subunit of mammalian cAMP-dependent protein kinase detected by capillary LC-MS and tandem mass spectrometry." Jedrzejewski P.T., Girod A., Tholey A., Koenig N., Thullner S., Kinzel V., Bossemeyer D. Protein Sci. 7:457-469(1998) [PubMed: 9521123] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-8, MYRISTOYLATION AT GLY-2, DEAMIDATION AT ASN-3.
[3]	"Intracellular distribution of mammalian protein kinase A catalytic subunit altered by conserved Asn2 deamidation." Pepperkok R., Hotz-Wagenblatt A., Koenig N., Girod A., Bossemeyer D., Kinzel V. J. Cell Biol. 148:715-726(2000) [PubMed: 10684253] [Abstract] Cited for: DEAMIDATION AT ASN-3, SUBCELLULAR LOCATION.
[4]	"Crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MgATP and peptide inhibitor." Zheng J., Knighton D.R., ten Eyck L.F., Karlsson R., Xuong N.-H., Taylor S.S., Sowadski J.M. Biochemistry 32:2154-2161(1993) [PubMed: 8443157] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH PKIA.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X07617 mRNA. Translation: CAA30470.1.

PIR

S00086.

UniGene

Ssc.13872

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CDK	X-ray	2.00	A/B	2-351	[»]
1CMK	X-ray	2.90	E	2-351	[»]
1CTP	X-ray	2.90	E	2-350	[»]

ModBase

Search...

Phylogenomic databases

HOVERGEN

P36887.

Enzyme and pathway databases

BRENDA

2.7.11.11. 249.

Family and domain databases

InterPro

IPR000961. AGC-kinase_C.
IPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_pkinase-rel.
IPR008271. Ser_thr_pkin_AS.
IPR002290. Ser_thr_pkinase.
[Graphical view]

Pfam

PF00069. Pkinase. 1 hit.
[Graphical view]

ProDom

PD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]

PROSITE

PS51285. AGC_KINASE_CTER. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

KAPCA_PIG

Accession

Primary (citable) accession number: P36887

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 90 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)