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Database: UniProt
Entry: P63248
LinkDB: P63248
Original site: P63248 
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   07-APR-2021, entry version 117.
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;
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; 1PVK; Model; -; 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; 6Y2O; X-ray; 2.01 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; 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   PDBsum; 1APM; -.
DR   PDBsum; 1ATP; -.
DR   PDBsum; 1PVK; -.
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; 6Y2O; -.
DR   PDBsum; 6Y8C; -.
DR   PDBsum; 6YNA; -.
DR   PDBsum; 6YNB; -.
DR   PDBsum; 6YNC; -.
DR   PDBsum; 6YNR; -.
DR   PDBsum; 6YNT; -.
DR   PDBsum; 6YQI; -.
DR   PDBsum; 6YQJ; -.
DR   PDBsum; 6YQK; -.
DR   BMRB; P63248; -.
DR   SMR; P63248; -.
DR   BioGRID; 202207; 4.
DR   DIP; DIP-6087N; -.
DR   IntAct; P63248; 3.
DR   MINT; P63248; -.
DR   STRING; 10090.ENSMUSP00000028999; -.
DR   PhosphoSitePlus; P63248; -.
DR   PaxDb; P63248; -.
DR   PeptideAtlas; P63248; -.
DR   PRIDE; P63248; -.
DR   ProteomicsDB; 269496; -.
DR   Antibodypedia; 52148; 58 antibodies.
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   eggNOG; ENOG502S6JP; Eukaryota.
DR   GeneTree; ENSGT00530000064276; -.
DR   HOGENOM; CLU_163471_2_0_1; -.
DR   InParanoid; P63248; -.
DR   OMA; GREMPLT; -.
DR   OrthoDB; 1468806at2759; -.
DR   PhylomeDB; P63248; -.
DR   TreeFam; TF330809; -.
DR   BioGRID-ORCS; 18767; 0 hits in 53 CRISPR screens.
DR   EvolutionaryTrace; P63248; -.
DR   PRO; PR:P63248; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; P63248; protein.
DR   Bgee; ENSMUSG00000027499; Expressed in extra-ocular muscle and 311 other tissues.
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   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:0007744|PDB:4DFX"
SQ   SEQUENCE   76 AA;  7960 MW;  FCCE07281498788A CRC64;
     MTDVETTYAD FIASGRTGRR NAIHDILVSS ASGNSNELAL KLAGLDINKT EGEDDGQRSS
     TEQSGEAQGE AAKSES
//
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