IPKA_MOUSE
ID IPKA_MOUSE Reviewed; 76 AA.
AC P63248; P27776; Q3UTL0;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=cAMP-dependent protein kinase inhibitor alpha;
DE Short=PKI-alpha;
DE AltName: Full=cAMP-dependent protein kinase inhibitor, muscle/brain isoform;
GN Name=Pkia;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=1710219; DOI=10.1016/s0021-9258(18)99142-8;
RA Olsen S.R., Uhler M.D.;
RT "Isolation and characterization of cDNA clones for an inhibitor protein of
RT cAMP-dependent protein kinase.";
RL J. Biol. Chem. 266:11158-11162(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain cortex;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Olfactory epithelium;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 6-25 IN COMPLEX WITH PRKACA.
RX PubMed=8443157; DOI=10.1021/bi00060a005;
RA Zheng J., Knighton D.R., ten Eyck L.F., Karlsson R., Xuong N.-H.,
RA Taylor S.S., Sowadski J.M.;
RT "Crystal structure of the catalytic subunit of cAMP-dependent protein
RT kinase complexed with MgATP and peptide inhibitor.";
RL Biochemistry 32:2154-2161(1993).
CC -!- FUNCTION: Extremely potent competitive inhibitor of cAMP-dependent
CC protein kinase activity, this protein interacts with the catalytic
CC subunit of the enzyme after the cAMP-induced dissociation of its
CC regulatory chains.
CC -!- INTERACTION:
CC P63248; P05132: Prkaca; NbExp=4; IntAct=EBI-2931786, EBI-400564;
CC -!- TISSUE SPECIFICITY: Present at high levels in skeletal muscle and brain
CC but is present at lower levels in heart, testis and liver.
CC -!- MISCELLANEOUS: The inhibitory site contains regions very similar to the
CC hinge regions (sites that directly interact with the enzyme active
CC site) and 'pseudosubstrate site' of the regulatory chains; but, unlike
CC these chains, PKI does not contain cAMP-binding sites. The arginine
CC residues within the inhibitory site are essential for inhibition and
CC recognition of the enzyme active site (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PKI family. {ECO:0000305}.
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DR EMBL; M63554; AAA39940.1; -; mRNA.
DR EMBL; AK139347; BAE23970.1; -; mRNA.
DR EMBL; CH466577; EDL05208.1; -; Genomic_DNA.
DR EMBL; CH466577; EDL05209.1; -; Genomic_DNA.
DR EMBL; BC048244; AAH48244.1; -; mRNA.
DR CCDS; CCDS38383.1; -.
DR PIR; A40536; A40536.
DR RefSeq; NP_032888.1; NM_008862.3.
DR PDB; 1APM; X-ray; 2.00 A; I=6-25.
DR PDB; 1ATP; X-ray; 2.20 A; I=6-25.
DR PDB; 2CPK; X-ray; 2.70 A; I=6-25.
DR PDB; 2GNF; X-ray; 2.28 A; I=6-25.
DR PDB; 2GNG; X-ray; 1.87 A; I=6-25.
DR PDB; 2QUR; X-ray; 2.50 A; B=6-25.
DR PDB; 3FJQ; X-ray; 1.60 A; I=6-25.
DR PDB; 3OW3; X-ray; 1.90 A; B=6-25.
DR PDB; 3QAL; X-ray; 1.70 A; I=6-23.
DR PDB; 3QAM; X-ray; 1.92 A; I=6-24.
DR PDB; 4DFX; X-ray; 1.35 A; I=6-25.
DR PDB; 4DFZ; X-ray; 2.00 A; I=6-25.
DR PDB; 4DG0; X-ray; 2.00 A; I=6-25.
DR PDB; 4DG2; X-ray; 2.00 A; I=6-25.
DR PDB; 4DG3; X-ray; 1.80 A; A=6-25.
DR PDB; 4DH1; X-ray; 2.00 A; I=6-25.
DR PDB; 4DH3; X-ray; 2.20 A; I=6-25.
DR PDB; 4DH5; X-ray; 2.20 A; I=6-25.
DR PDB; 4DH7; X-ray; 1.80 A; I=6-25.
DR PDB; 4DH8; X-ray; 2.30 A; I=6-25.
DR PDB; 4HPT; X-ray; 2.15 A; I=6-25.
DR PDB; 4HPU; X-ray; 1.55 A; I=6-25.
DR PDB; 6F14; X-ray; 1.87 A; B=6-25.
DR PDB; 6Y05; X-ray; 1.70 A; B=6-25.
DR PDB; 6Y0B; X-ray; 1.71 A; B=6-25.
DR PDB; 6Y2O; X-ray; 2.01 A; B=6-25.
DR PDB; 6Y2U; X-ray; 1.93 A; B=6-25.
DR PDB; 6Y89; X-ray; 1.56 A; B=6-25.
DR PDB; 6Y8C; X-ray; 1.76 A; B=6-25.
DR PDB; 6YNA; X-ray; 1.47 A; B=12-30.
DR PDB; 6YNB; X-ray; 1.72 A; B=12-30.
DR PDB; 6YNC; X-ray; 1.40 A; B=12-30.
DR PDB; 6YNR; X-ray; 1.90 A; B=6-25.
DR PDB; 6YNT; X-ray; 1.52 A; B=6-25.
DR PDB; 6YOT; X-ray; 1.96 A; B=6-25.
DR PDB; 6YPP; X-ray; 1.75 A; B=6-25.
DR PDB; 6YQI; X-ray; 1.42 A; B=12-30.
DR PDB; 6YQJ; X-ray; 1.58 A; B=12-30.
DR PDB; 6YQK; X-ray; 1.67 A; B=12-30.
DR PDB; 7AXT; X-ray; 1.86 A; B=6-25.
DR PDB; 7AXV; X-ray; 1.79 A; B=6-25.
DR PDB; 7AXW; X-ray; 1.69 A; B=6-25.
DR PDB; 7BAQ; X-ray; 1.54 A; B=6-23.
DR PDB; 7BB0; X-ray; 1.75 A; B=6-25.
DR PDBsum; 1APM; -.
DR PDBsum; 1ATP; -.
DR PDBsum; 2CPK; -.
DR PDBsum; 2GNF; -.
DR PDBsum; 2GNG; -.
DR PDBsum; 2QUR; -.
DR PDBsum; 3FJQ; -.
DR PDBsum; 3OW3; -.
DR PDBsum; 3QAL; -.
DR PDBsum; 3QAM; -.
DR PDBsum; 4DFX; -.
DR PDBsum; 4DFZ; -.
DR PDBsum; 4DG0; -.
DR PDBsum; 4DG2; -.
DR PDBsum; 4DG3; -.
DR PDBsum; 4DH1; -.
DR PDBsum; 4DH3; -.
DR PDBsum; 4DH5; -.
DR PDBsum; 4DH7; -.
DR PDBsum; 4DH8; -.
DR PDBsum; 4HPT; -.
DR PDBsum; 4HPU; -.
DR PDBsum; 6F14; -.
DR PDBsum; 6Y05; -.
DR PDBsum; 6Y0B; -.
DR PDBsum; 6Y2O; -.
DR PDBsum; 6Y2U; -.
DR PDBsum; 6Y89; -.
DR PDBsum; 6Y8C; -.
DR PDBsum; 6YNA; -.
DR PDBsum; 6YNB; -.
DR PDBsum; 6YNC; -.
DR PDBsum; 6YNR; -.
DR PDBsum; 6YNT; -.
DR PDBsum; 6YOT; -.
DR PDBsum; 6YPP; -.
DR PDBsum; 6YQI; -.
DR PDBsum; 6YQJ; -.
DR PDBsum; 6YQK; -.
DR PDBsum; 7AXT; -.
DR PDBsum; 7AXV; -.
DR PDBsum; 7AXW; -.
DR PDBsum; 7BAQ; -.
DR PDBsum; 7BB0; -.
DR AlphaFoldDB; P63248; -.
DR BMRB; P63248; -.
DR SMR; P63248; -.
DR BioGRID; 202207; 4.
DR DIP; DIP-6087N; -.
DR IntAct; P63248; 2.
DR STRING; 10090.ENSMUSP00000028999; -.
DR PhosphoSitePlus; P63248; -.
DR PaxDb; P63248; -.
DR PeptideAtlas; P63248; -.
DR PRIDE; P63248; -.
DR ProteomicsDB; 269496; -.
DR Antibodypedia; 52148; 63 antibodies from 17 providers.
DR DNASU; 18767; -.
DR Ensembl; ENSMUST00000028999; ENSMUSP00000028999; ENSMUSG00000027499.
DR Ensembl; ENSMUST00000193330; ENSMUSP00000141466; ENSMUSG00000027499.
DR GeneID; 18767; -.
DR KEGG; mmu:18767; -.
DR UCSC; uc008oof.1; mouse.
DR CTD; 5569; -.
DR MGI; MGI:104747; Pkia.
DR VEuPathDB; HostDB:ENSMUSG00000027499; -.
DR eggNOG; ENOG502S6JP; Eukaryota.
DR GeneTree; ENSGT00530000064276; -.
DR HOGENOM; CLU_163471_2_0_1; -.
DR InParanoid; P63248; -.
DR OMA; HYKNHFS; -.
DR OrthoDB; 1468806at2759; -.
DR PhylomeDB; P63248; -.
DR TreeFam; TF330809; -.
DR BioGRID-ORCS; 18767; 0 hits in 72 CRISPR screens.
DR EvolutionaryTrace; P63248; -.
DR PRO; PR:P63248; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P63248; protein.
DR Bgee; ENSMUSG00000027499; Expressed in barrel cortex and 254 other tissues.
DR ExpressionAtlas; P63248; baseline and differential.
DR Genevisible; P63248; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0004862; F:cAMP-dependent protein kinase inhibitor activity; IDA:MGI.
DR GO; GO:0034236; F:protein kinase A catalytic subunit binding; IPI:CAFA.
DR GO; GO:2000480; P:negative regulation of cAMP-dependent protein kinase activity; ISO:MGI.
DR GO; GO:0043086; P:negative regulation of catalytic activity; IDA:MGI.
DR GO; GO:0042308; P:negative regulation of protein import into nucleus; IDA:MGI.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IDA:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; IMP:MGI.
DR InterPro; IPR004171; cAMP_dep_PKI.
DR PANTHER; PTHR15416; PTHR15416; 1.
DR Pfam; PF02827; PKI; 1.
DR PIRSF; PIRSF001667; PKI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Protein kinase inhibitor; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P61925"
FT CHAIN 2..76
FT /note="cAMP-dependent protein kinase inhibitor alpha"
FT /id="PRO_0000154533"
FT REGION 49..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 16
FT /note="Important for inhibition"
FT /evidence="ECO:0000250"
FT SITE 19
FT /note="Important for inhibition"
FT /evidence="ECO:0000250"
FT SITE 20
FT /note="Important for inhibition"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000250|UniProtKB:P61925"
FT HELIX 7..12
FT /evidence="ECO:0007829|PDB:4DFX"
SQ SEQUENCE 76 AA; 7960 MW; FCCE07281498788A CRC64;
MTDVETTYAD FIASGRTGRR NAIHDILVSS ASGNSNELAL KLAGLDINKT EGEDDGQRSS
TEQSGEAQGE AAKSES
