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cAMP-dependent protein kinase type I-alpha regulatory subunit [Cleaved into: cAMP-dependent protein kinase type I-alpha regulatory subunit, N-terminally processed]

 KAP0_MOUSE              Reviewed;         381 AA.
Q9DBC7; Q3UKU7; Q9JHR5; Q9JHR6;
11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
12-SEP-2018, entry version 148.
RecName: Full=cAMP-dependent protein kinase type I-alpha regulatory subunit;
Contains:
RecName: Full=cAMP-dependent protein kinase type I-alpha regulatory subunit, N-terminally processed;
Name=Prkar1a;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Bone marrow, Kidney, Liver, and Placenta;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-60 AND 259-382.
PubMed=10913627; DOI=10.1016/S0014-5793(00)01653-7;
Barradeau S., Imaizumi-Scherrer T., Weiss M.C., Faust D.M.;
"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.";
FEBS Lett. 476:272-276(2000).
[4]
INTERACTION WITH AKAP4.
PubMed=9852104; DOI=10.1074/jbc.273.51.34384;
Miki K., Eddy E.M.;
"Identification of tethering domains for protein kinase A type Ialpha
regulatory subunits on sperm fibrous sheath protein FSC1.";
J. Biol. Chem. 273:34384-34390(1998).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic brain;
PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
"Phosphoproteomic analysis of the developing mouse brain.";
Mol. Cell. Proteomics 3:1093-1101(2004).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18630941; DOI=10.1021/pr800223m;
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
"Specific phosphopeptide enrichment with immobilized titanium ion
affinity chromatography adsorbent for phosphoproteome analysis.";
J. Proteome Res. 7:3957-3967(2008).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[10]
INTERACTION WITH CBFA2T3.
PubMed=20138877; DOI=10.1016/j.febslet.2010.02.007;
Fiedler S.E., Schillace R.V., Daniels C.J., Andrews S.F., Carr D.W.;
"Myeloid translocation gene 16b is a dual A-kinase anchoring protein
that interacts selectively with plexins in a phospho-regulated
manner.";
FEBS Lett. 584:873-877(2010).
-!- FUNCTION: Regulatory subunit of the cAMP-dependent protein kinases
involved in cAMP signaling in cells. {ECO:0000250}.
-!- SUBUNIT: 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). {ECO:0000250}.
-!- INTERACTION:
O54918-1:Bcl2l11; NbExp=2; IntAct=EBI-645677, EBI-526076;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}.
-!- PTM: The pseudophosphorylation site binds to the substrate-binding
region of the catalytic chain, resulting in the inhibition of its
activity. {ECO:0000250}.
-!- MISCELLANEOUS: Two types of regulatory chains are found: type I,
which predominates in skeletal muscle, and type II, which
predominates in cardiac muscle. {ECO:0000250}.
-!- SIMILARITY: Belongs to the cAMP-dependent kinase regulatory chain
family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AK005039; BAB23766.1; -; mRNA.
EMBL; AK027916; BAC25664.1; -; mRNA.
EMBL; AK051068; BAC34516.1; -; mRNA.
EMBL; AK145797; BAE26655.1; -; mRNA.
EMBL; AK145860; BAE26704.1; -; mRNA.
EMBL; AK147188; BAE27748.1; -; mRNA.
EMBL; AK150427; BAE29550.1; -; mRNA.
EMBL; AK151124; BAE30132.1; -; mRNA.
EMBL; AK153227; BAE31820.1; -; mRNA.
EMBL; BC003461; AAH03461.1; -; mRNA.
EMBL; BC005697; AAH05697.1; -; mRNA.
EMBL; AJ278427; CAB94778.1; -; Genomic_DNA.
EMBL; AJ278429; CAB94718.1; -; Genomic_DNA.
CCDS; CCDS25583.1; -.
RefSeq; NP_001300902.1; NM_001313973.1.
RefSeq; NP_001300903.1; NM_001313974.1.
RefSeq; NP_001300904.1; NM_001313975.1.
RefSeq; NP_001300905.1; NM_001313976.1.
RefSeq; NP_068680.1; NM_021880.3.
RefSeq; XP_017169829.1; XM_017314340.1.
UniGene; Mm.30039; -.
ProteinModelPortal; Q9DBC7; -.
SMR; Q9DBC7; -.
BioGrid; 202365; 4.
DIP; DIP-32450N; -.
IntAct; Q9DBC7; 16.
MINT; Q9DBC7; -.
STRING; 10090.ENSMUSP00000056500; -.
iPTMnet; Q9DBC7; -.
PhosphoSitePlus; Q9DBC7; -.
SwissPalm; Q9DBC7; -.
REPRODUCTION-2DPAGE; IPI00762049; -.
REPRODUCTION-2DPAGE; Q9DBC7; -.
EPD; Q9DBC7; -.
MaxQB; Q9DBC7; -.
PaxDb; Q9DBC7; -.
PRIDE; Q9DBC7; -.
Ensembl; ENSMUST00000049527; ENSMUSP00000056500; ENSMUSG00000020612.
Ensembl; ENSMUST00000106677; ENSMUSP00000102288; ENSMUSG00000020612.
GeneID; 19084; -.
KEGG; mmu:19084; -.
UCSC; uc007mcu.1; mouse.
CTD; 5573; -.
MGI; MGI:104878; Prkar1a.
eggNOG; KOG1113; Eukaryota.
eggNOG; COG0664; LUCA.
GeneTree; ENSGT00530000062947; -.
HOVERGEN; HBG002025; -.
InParanoid; Q9DBC7; -.
KO; K04739; -.
OMA; VQLCTVR; -.
OrthoDB; EOG091G0F1K; -.
TreeFam; TF314920; -.
Reactome; R-MMU-163615; PKA activation.
Reactome; R-MMU-164378; PKA activation in glucagon signalling.
Reactome; R-MMU-180024; DARPP-32 events.
Reactome; R-MMU-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
Reactome; R-MMU-5610787; Hedgehog 'off' state.
Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production.
ChiTaRS; Prkar1a; mouse.
PRO; PR:Q9DBC7; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000020612; Expressed in 324 organ(s), highest expression level in dentate gyrus of hippocampal formation.
ExpressionAtlas; Q9DBC7; baseline and differential.
Genevisible; Q9DBC7; MM.
GO; GO:0005930; C:axoneme; IEA:Ensembl.
GO; GO:0005952; C:cAMP-dependent protein kinase complex; ISO:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0001772; C:immunological synapse; IEA:Ensembl.
GO; GO:0031594; C:neuromuscular junction; IDA:MGI.
GO; GO:0031588; C:nucleotide-activated protein kinase complex; ISO:MGI.
GO; GO:0044853; C:plasma membrane raft; ISO:MGI.
GO; GO:0032991; C:protein-containing complex; ISO:MGI.
GO; GO:0030552; F:cAMP binding; ISO:MGI.
GO; GO:0004862; F:cAMP-dependent protein kinase inhibitor activity; ISO:MGI.
GO; GO:0008603; F:cAMP-dependent protein kinase regulator activity; IDA:MGI.
GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
GO; GO:0034236; F:protein kinase A catalytic subunit binding; ISO:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0009887; P:animal organ morphogenesis; TAS:MGI.
GO; GO:0060038; P:cardiac muscle cell proliferation; IMP:MGI.
GO; GO:0008283; P:cell proliferation; TAS:MGI.
GO; GO:0007143; P:female meiotic nuclear division; IEA:Ensembl.
GO; GO:0007507; P:heart development; IMP:MGI.
GO; GO:0001707; P:mesoderm formation; IMP:MGI.
GO; GO:0046007; P:negative regulation of activated T cell proliferation; ISO:MGI.
GO; GO:2000480; P:negative regulation of cAMP-dependent protein kinase activity; ISO:MGI.
GO; GO:0045835; P:negative regulation of meiotic nuclear division; IEA:Ensembl.
GO; GO:0006469; P:negative regulation of protein kinase activity; IMP:MGI.
GO; GO:0006468; P:protein phosphorylation; TAS:MGI.
GO; GO:0045859; P:regulation of protein kinase activity; ISO:MGI.
GO; GO:0045214; P:sarcomere organization; IMP:MGI.
CDD; cd00038; CAP_ED; 2.
Gene3D; 2.60.120.10; -; 2.
InterPro; IPR012198; cAMP_dep_PK_reg_su.
InterPro; IPR003117; cAMP_dep_PK_reg_su_I/II_a/b.
InterPro; IPR018490; cNMP-bd-like.
InterPro; IPR018488; cNMP-bd_CS.
InterPro; IPR000595; cNMP-bd_dom.
InterPro; IPR014710; RmlC-like_jellyroll.
Pfam; PF00027; cNMP_binding; 2.
Pfam; PF02197; RIIa; 1.
PIRSF; PIRSF000548; PK_regulatory; 1.
SMART; SM00100; cNMP; 2.
SMART; SM00394; RIIa; 1.
SUPFAM; SSF51206; SSF51206; 2.
PROSITE; PS00888; CNMP_BINDING_1; 2.
PROSITE; PS00889; CNMP_BINDING_2; 2.
PROSITE; PS50042; CNMP_BINDING_3; 2.
1: Evidence at protein level;
Acetylation; cAMP; cAMP-binding; Cell membrane; Complete proteome;
Disulfide bond; Membrane; Nucleotide-binding; Phosphoprotein;
Reference proteome; Repeat.
CHAIN 1 381 cAMP-dependent protein kinase type I-
alpha regulatory subunit.
/FTId=PRO_0000421786.
INIT_MET 1 1 Removed; alternate.
{ECO:0000250|UniProtKB:P00514}.
CHAIN 2 381 cAMP-dependent protein kinase type I-
alpha regulatory subunit, N-terminally
processed.
/FTId=PRO_0000205378.
NP_BIND 137 254 cAMP 1.
NP_BIND 255 381 cAMP 2.
REGION 2 136 Dimerization and phosphorylation.
MOTIF 96 100 Pseudophosphorylation motif.
BINDING 202 202 cAMP 1.
BINDING 211 211 cAMP 1.
BINDING 326 326 cAMP 2.
BINDING 335 335 cAMP 2.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P10644}.
MOD_RES 2 2 N-acetylalanine; in cAMP-dependent
protein kinase type I-alpha regulatory
subunit, N-terminally processed.
{ECO:0000250|UniProtKB:P00514}.
MOD_RES 3 3 Phosphoserine.
{ECO:0000250|UniProtKB:P09456}.
MOD_RES 75 75 Phosphothreonine.
{ECO:0000250|UniProtKB:P10644}.
MOD_RES 77 77 Phosphoserine.
{ECO:0000250|UniProtKB:P10644}.
MOD_RES 83 83 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:21183079}.
MOD_RES 101 101 Phosphoserine.
{ECO:0000244|PubMed:15345747}.
MOD_RES 258 258 Phosphoserine.
{ECO:0000250|UniProtKB:P09456}.
DISULFID 18 18 Interchain (with C-39). {ECO:0000250}.
DISULFID 39 39 Interchain (with C-18). {ECO:0000250}.
SEQUENCE 381 AA; 43185 MW; 08F164BB4528C63B CRC64;
MASGSMATSE EERSLRECEL YVQKHNIQAL LKDSIVQLCT TRPERPMAFL REYFERLEKE
EARQIQCLQK TGIRTDSRED EISPPPPNPV VKGRRRRGAI SAEVYTEEDA ASYVRKVIPK
DYKTMAALAK AIEKNVLFSH LDDNERSDIF DAMFPVSFIA GETVIQQGDE GDNFYVIDQG
EMDVYVNNEW ATSVGEGGSF GELALIYGTP RAATVKAKTN VKLWGIDRDS YRRILMGSTL
RKRKMYEEFL SKVSILESLD KWERLTVADA LEPVQFEDGQ KIVVQGEPGD EFFIILEGTA
AVLQRRSENE EFVEVGRLGP SDYFGEIALL MNRPRAATVV ARGPLKCVKL DRPRFERVLG
PCSDILKRNI QQYNSFVSLS V


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