Q9DBC7 (KAP0_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
cAMP-dependent protein kinase type I-alpha regulatory subunit

Cleaved into the following chain:

1. cAMP-dependent protein kinase type I-alpha regulatory subunit, N-terminally processed

Gene names

Name:

Prkar1a

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	381 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	Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells By similarity.
Subunit structure	The inactive holoenzyme is composed of two regulatory chains and two catalytic chains. Activation by cAMP releases the two active catalytic monomers and the regulatory dimer. PRKAR1A also interacts with RFC2; the complex may be involved in cell survival. Interacts with AKAP4. Interacts with RARA; the interaction occurs in the presence of cAMP or FSH and regulates RARA transcriptional activity. Interacts with the phosphorylated form of PJA2. Interacts with PRKX; regulates this cAMP-dependent protein kinase By similarity. Interacts with CBFA2T3. Interacts with smAKAP; this interaction may target PRKAR1A to the plasma membrane. Interacts with AICDA By similarity. Ref.4 Ref.12
Subcellular location	Cell membrane By similarity.
Post-translational modification	The pseudophosphorylation site binds to the substrate-binding region of the catalytic chain, resulting in the inhibition of its activity By similarity.
Miscellaneous	Two types of regulatory chains are found: type I, which predominates in skeletal muscle, and type II, which predominates in cardiac muscle By similarity.
Sequence similarities	Belongs to the cAMP-dependent kinase regulatory chain family. Contains 2 cyclic nucleotide-binding domains.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Domain	Repeat
Ligand	Nucleotide-binding cAMP cAMP-binding
PTM	Acetylation Disulfide bond Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cardiac muscle cell proliferation Inferred from mutant phenotype PubMed 18316483. Source: MGI female meiosis Inferred from electronic annotation. Source: Compara mesoderm formation Inferred from mutant phenotype PubMed 12004056. Source: MGI negative regulation of meiosis Inferred from electronic annotation. Source: Compara negative regulation of protein kinase activity Inferred from mutant phenotype PubMed 18316483. Source: MGI organ morphogenesis Traceable author statement PubMed 7775586. Source: MGI protein phosphorylation Traceable author statement PubMed 7775586. Source: MGI sarcomere organization Inferred from mutant phenotype PubMed 18316483. Source: MGI signal transduction Inferred from electronic annotation. Source: InterPro
Cellular_component	cAMP-dependent protein kinase complex Inferred from electronic annotation. Source: Compara cytoplasm Traceable author statement PubMed 1448119. Source: MGI neuromuscular junction Inferred from direct assay PubMed 8794865. Source: MGI plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	cAMP binding Inferred from electronic annotation. Source: UniProtKB-KW cAMP-dependent protein kinase regulator activity Inferred from direct assay PubMed 7775586. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 381	381	cAMP-dependent protein kinase type I-alpha regulatory subunit		PRO_0000205378
	Initiator methionine	1	1	Removed; alternate By similarity
	Chain	2 – 381	380	cAMP-dependent protein kinase type I-alpha regulatory subunit, N-terminally processed		PRO_0000421786
Regions
	Nucleotide binding	137 – 254	118	cAMP 1
	Nucleotide binding	255 – 381	127	cAMP 2
	Region	1 – 136	136	Dimerization and phosphorylation
	Motif	96 – 100	5	Pseudophosphorylation motif
Sites
	Binding site	202	1	cAMP 1
	Binding site	211	1	cAMP 1
	Binding site	326	1	cAMP 2
	Binding site	335	1	cAMP 2
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine By similarity
	Modified residue	2	1	N-acetylalanine Probable
	Modified residue	77	1	Phosphoserine Ref.6 Ref.8
	Modified residue	83	1	Phosphoserine Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11
	Modified residue	101	1	Phosphoserine Ref.5
	Disulfide bond	18		Interchain (with C-39) By similarity
	Disulfide bond	39		Interchain (with C-18) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9DBC7 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 08F164BB4528C63B	FASTA	381	43,185
	10 20 30 40 50 60 MASGSMATSE EERSLRECEL YVQKHNIQAL LKDSIVQLCT TRPERPMAFL REYFERLEKE 70 80 90 100 110 120 EARQIQCLQK TGIRTDSRED EISPPPPNPV VKGRRRRGAI SAEVYTEEDA ASYVRKVIPK 130 140 150 160 170 180 DYKTMAALAK AIEKNVLFSH LDDNERSDIF DAMFPVSFIA GETVIQQGDE GDNFYVIDQG 190 200 210 220 230 240 EMDVYVNNEW ATSVGEGGSF GELALIYGTP RAATVKAKTN VKLWGIDRDS YRRILMGSTL 250 260 270 280 290 300 RKRKMYEEFL SKVSILESLD KWERLTVADA LEPVQFEDGQ KIVVQGEPGD EFFIILEGTA 310 320 330 340 350 360 AVLQRRSENE EFVEVGRLGP SDYFGEIALL MNRPRAATVV ARGPLKCVKL DRPRFERVLG 370 380 PCSDILKRNI QQYNSFVSLS V

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Bone marrow, Kidney, Liver and Placenta.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Mammary tumor.
[3]	"Alternative 5'-exons of the mouse cAMP-dependent protein kinase subunit RIalpha gene are conserved and expressed in both a ubiquitous and tissue-restricted fashion." Barradeau S., Imaizumi-Scherrer T., Weiss M.C., Faust D.M. FEBS Lett. 476:272-276(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-60 AND 259-382.
[4]	"Identification of tethering domains for protein kinase A type Ialpha regulatory subunits on sperm fibrous sheath protein FSC1." Miki K., Eddy E.M. J. Biol. Chem. 273:34384-34390(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH AKAP4.
[5]	"Phosphoproteomic analysis of the developing mouse brain." Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P. Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101, MASS SPECTROMETRY. Tissue: Embryonic brain.
[6]	"Comprehensive identification of phosphorylation sites in postsynaptic density preparations." Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L. Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77 AND SER-83, MASS SPECTROMETRY. Tissue: Brain.
[7]	"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, MASS SPECTROMETRY. Tissue: Liver.
[8]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77 AND SER-83, MASS SPECTROMETRY. Tissue: Liver.
[9]	"Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis." Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H. J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, MASS SPECTROMETRY. Tissue: Liver.
[10]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, MASS SPECTROMETRY. Tissue: Melanoma.
[11]	"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry." Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J. Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, MASS SPECTROMETRY. Tissue: Embryonic fibroblast.
[12]	"Myeloid translocation gene 16b is a dual A-kinase anchoring protein that interacts selectively with plexins in a phospho-regulated manner." Fiedler S.E., Schillace R.V., Daniels C.J., Andrews S.F., Carr D.W. FEBS Lett. 584:873-877(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CBFA2T3.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK005039 mRNA. Translation: BAB23766.1. AK027916 mRNA. Translation: BAC25664.1. AK051068 mRNA. Translation: BAC34516.1. AK145797 mRNA. Translation: BAE26655.1. AK145860 mRNA. Translation: BAE26704.1. AK147188 mRNA. Translation: BAE27748.1. AK150427 mRNA. Translation: BAE29550.1. AK151124 mRNA. Translation: BAE30132.1. AK153227 mRNA. Translation: BAE31820.1. BC003461 mRNA. Translation: AAH03461.1. BC005697 mRNA. Translation: AAH05697.1. AJ278427 Genomic DNA. Translation: CAB94778.1. AJ278429 Genomic DNA. Translation: CAB94718.1.
IPI	IPI00762049.
RefSeq	NP_068680.1. NM_021880.2.
UniGene	Mm.30039.
3D structure databases
ProteinModelPortal	Q9DBC7.
SMR	Q9DBC7. Positions 14-380.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9DBC7. 10 interactions.
2D gel databases
REPRODUCTION-2DPAGE	IPI00762049. Q9DBC7.
Proteomic databases
PaxDb	Q9DBC7.
PRIDE	Q9DBC7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000049527; ENSMUSP00000056500; ENSMUSG00000020612. ENSMUST00000106677; ENSMUSP00000102288; ENSMUSG00000020612.
GeneID	19084.
KEGG	mmu:19084.
Organism-specific databases
CTD	5573.
MGI	MGI:104878. Prkar1a.
Phylogenomic databases
eggNOG	COG0664.
GeneTree	ENSGT00530000062947.
HOVERGEN	HBG002025.
InParanoid	Q9DBC7.
KO	K04739.
OMA	KNILFSH.
OrthoDB	EOG4JQ3XP.
Gene expression databases
ArrayExpress	Q9DBC7.
Bgee	Q9DBC7.
Genevestigator	Q9DBC7.
GermOnline	ENSMUSG00000020612. Mus musculus.
Family and domain databases
Gene3D	2.60.120.10. 2 hits.
InterPro	IPR002373. cAMP/cGMP_kin. IPR012198. cAMP_dep_PK_reg_su. IPR003117. cAMP_dep_PK_reg_su_I/II_a/b. IPR018490. cNMP-bd-like. IPR018488. cNMP-bd_CS. IPR000595. cNMP-bd_dom. IPR014710. RmlC-like_jellyroll. [Graphical view]
Pfam	PF00027. cNMP_binding. 2 hits. PF02197. RIIa. 1 hit. [Graphical view]
PIRSF	PIRSF000548. PK_regulatory. 1 hit.
PRINTS	PR00103. CAMPKINASE.
SMART	SM00100. cNMP. 2 hits. SM00394. RIIa. 1 hit. [Graphical view]
SUPFAM	SSF47391. cAMP-dep_prot_kin_reg_I/II_a/b. 1 hit. SSF51206. cNMP_binding. 2 hits.
PROSITE	PS00888. CNMP_BINDING_1. 2 hits. PS00889. CNMP_BINDING_2. 2 hits. PS50042. CNMP_BINDING_3. 2 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	PRKAR1A. mouse.
NextBio	295622.
SOURCE	Search...

Entry information

Entry name

KAP0_MOUSE

Accession

Primary (citable) accession number: Q9DBC7
Secondary accession number(s): Q3UKU7, Q9JHR5, Q9JHR6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 98 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program