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Reviewed, UniProtKB/Swiss-Prot P27791 (KAPCA_RAT)

Last modified October 13, 2009. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    cAMP-dependent protein kinase catalytic subunit alpha
      Short name=PKA C-alpha
    EC=2.7.11.11
Gene names
Name: Prkaca
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

Sequence length351 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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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. Isoform 2 is round spermatid specific. Ref.1 Ref.3

Developmental stage

In spermatids, isoform 1 is expressed until spermatids become elutriated, whereafter isoform 2 is expressed. Ref.3

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.

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Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Nucleotide-binding
cAMP
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMLipoprotein
Myristate
Phosphoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processnegative regulation of meiotic cell cycle

Inferred from direct assay. Source: RGD

peptidyl-serine phosphorylation

Inferred from direct assay. Source: RGD

regulation of cellular respiration

Inferred from direct assay. Source: RGD

regulation of synaptic transmission, glutamatergic

Inferred from direct assay. Source: RGD

   Cellular componentGolgi apparatus

Inferred from direct assay. Source: RGD

cAMP-dependent protein kinase complex

Inferred from direct assay. Source: RGD

cytosol

Inferred from Experiment. Source: Reactome

membrane fraction

Inferred from direct assay. Source: RGD

nucleus

Inferred from direct assay. Source: RGD

perinuclear region of cytoplasm

Inferred from direct assay. Source: RGD

soluble fraction

Inferred from direct assay. Source: RGD

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

cAMP-dependent protein kinase activity

Inferred from direct assay. Source: RGD

protein complex binding

Inferred from physical interaction. Source: RGD

protein kinase A regulatory subunit binding

Inferred by curator. Source: RGD

protein kinase binding

Inferred from physical interaction. Source: UniProtKB

Complete GO annotation...

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Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P27791-1)

Also known as: C-alpha-1;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P27791-2)

Also known as: Cs;

The sequence of this isoform differs from the canonical sequence as follows:
     1-15: MGNAAAAKKGSEQES → MASNSND

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 351350cAMP-dependent protein kinase catalytic subunit alpha
PRO_0000086055

Regions

Domain44 – 298255Protein kinase
Domain299 – 35153AGC-kinase C-terminal
Nucleotide binding50 – 589ATP By similarity

Sites

Active site1671Proton acceptor By similarity
Binding site731ATP By similarity

Amino acid modifications

Modified residue31Deamidated asparagine; partial
Modified residue111Phosphoserine; by autocatalysis By similarity
Modified residue351Phosphoserine By similarity
Modified residue491Phosphothreonine By similarity
Modified residue1401Phosphoserine By similarity
Modified residue1961Phosphothreonine By similarity
Modified residue1981Phosphothreonine By similarity
Modified residue2021Phosphothreonine By similarity
Modified residue3391Phosphoserine By similarity
Lipidation21N-myristoyl glycine

Natural variations

Alternative sequence1 – 1515MGNAA…SEQES → MASNSND in isoform 2.
VSP_013277

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Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (C-alpha-1) [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 4763ACD074AB2384

FASTA35140,620
        10         20         30         40         50         60 
MGNAAAAKKG SEQESVKEFL AKAKEDFLKK WEDPSQNTAQ LDHFDRIKTL GTGSFGRVML 

        70         80         90        100        110        120 
VKHKESGNHY AMKILDKQKV VKLKQIEHTL NEKRILQAVN FPFLVKLEFS 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 NEKCGKEFTE F

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Isoform 2 (Cs).

Checksum: A41B65C8AB162401
Show »

FASTA34339,879

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References

[1]"Rat C alpha catalytic subunit of the cAMP-dependent protein kinase: cDNA sequence and evidence that it is the only isoform expressed in myoblasts."
Wiemann S., Voss H., Kinzel V., Pyerin W.
Biochim. Biophys. Acta 1089:254-256(1991) [PubMed: 1711374] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
[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 (ISOFORM 1), MYRISTOYLATION AT GLY-2, DEAMIDATION AT ASN-3.
[3]"Phosphorylation of rat spermatidal protein TP2 by sperm-specific protein kinase A and modulation of its transport into the haploid nucleus."
Ullas K.S., Rao M.R.S.
J. Biol. Chem. 278:52673-52680(2003) [PubMed: 14514679] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-313 (ISOFORM 2), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Strain: Wistar.
+Additional computationally mapped references.

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Cross-references

Sequence databases

X57986 mRNA. Translation: CAA41052.1.
AY375243 mRNA. Translation: AAQ81631.1.
IPIIPI00200013.
IPI00555215.
PIROKRT2C. S16240.
UniGeneRn.20

3D structure databases

HSSPHSSP built from PDB template 1CTP based on UniProtKB P36887.
SMRP27791. Positions 10-351.
ModBaseSearch...

Protein-protein interaction databases

STRINGP27791.

PTM databases

PhosphoSiteP27791.

Proteomic databases

PRIDEP27791.

Genome annotation databases

EnsemblENSRNOT00000007281; ENSRNOP00000007281; ENSRNOG00000005257; Rattus norvegicus. [Genome view]
ENSRNOT00000007303; ENSRNOP00000007303; ENSRNOG00000005257; Rattus norvegicus. [Genome view]
ENSRNOT00000041717; ENSRNOP00000044732; ENSRNOG00000005257; Rattus norvegicus. [Genome view]

Organism-specific databases

RGD3389. Prkaca.

Phylogenomic databases

HOVERGENP27791.

Enzyme and pathway databases

BRENDA2.7.11.11. 248.

Gene expression databases

ArrayExpressP27791.
GenevestigatorP27791.
GermOnlineENSRNOG00000005257. Rattus norvegicus.

Family and domain databases

InterProIPR000961. 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]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
ProDomPD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
PROSITEPS51285. 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]
ProtoNetSearch...

Other Resources

BindingDBP27791.

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Entry information

Entry nameKAPCA_RAT
AccessionPrimary (citable) accession number: P27791
Secondary accession number(s): Q6UA68
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: October 13, 2009
This is version 98 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents