IPKA_RAT
ID IPKA_RAT Reviewed; 76 AA.
AC P63249; P27776;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 100.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1491692; DOI=10.1210/mend.6.12.1491692;
RA van Patten S.M., Howard P., Walsh D.A., Maurer R.A.;
RT "The alpha- and beta-isoforms of the inhibitor protein of the 3',5'-cyclic
RT adenosine monophosphate-dependent protein kinase: characteristics and
RT tissue- and developmental-specific expression.";
RL Mol. Endocrinol. 6:2114-2122(1992).
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 -!- TISSUE SPECIFICITY: Highest expression in muscle (both skeletal and
CC cardiac) and brain.
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; L02615; AAA40867.1; -; mRNA.
DR RefSeq; NP_446224.1; NM_053772.2.
DR RefSeq; XP_006232217.1; XM_006232155.3.
DR RefSeq; XP_006232218.1; XM_006232156.3.
DR RefSeq; XP_008759079.1; XM_008760857.2.
DR PDB; 1L3R; X-ray; 2.00 A; I=6-25.
DR PDB; 1Q62; X-ray; 2.30 A; I=6-25.
DR PDB; 1Q8U; X-ray; 1.90 A; B=6-25.
DR PDB; 1SVH; X-ray; 2.30 A; B=6-25.
DR PDB; 1YDS; X-ray; 2.20 A; I=6-25.
DR PDB; 1YDT; X-ray; 2.30 A; I=6-25.
DR PDBsum; 1L3R; -.
DR PDBsum; 1Q62; -.
DR PDBsum; 1Q8U; -.
DR PDBsum; 1SVH; -.
DR PDBsum; 1YDS; -.
DR PDBsum; 1YDT; -.
DR AlphaFoldDB; P63249; -.
DR BMRB; P63249; -.
DR SMR; P63249; -.
DR STRING; 10116.ENSRNOP00000016567; -.
DR PaxDb; P63249; -.
DR GeneID; 114906; -.
DR KEGG; rno:114906; -.
DR UCSC; RGD:621021; rat.
DR CTD; 5569; -.
DR RGD; 621021; Pkia.
DR VEuPathDB; HostDB:ENSRNOG00000012095; -.
DR eggNOG; ENOG502S6JP; Eukaryota.
DR HOGENOM; CLU_163471_2_0_1; -.
DR InParanoid; P63249; -.
DR OMA; HYKNHFS; -.
DR OrthoDB; 1468806at2759; -.
DR PhylomeDB; P63249; -.
DR TreeFam; TF330809; -.
DR EvolutionaryTrace; P63249; -.
DR PRO; PR:P63249; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000012095; Expressed in quadriceps femoris and 19 other tissues.
DR Genevisible; P63249; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0004862; F:cAMP-dependent protein kinase inhibitor activity; ISO:RGD.
DR GO; GO:0034236; F:protein kinase A catalytic subunit binding; ISO:RGD.
DR GO; GO:2000480; P:negative regulation of cAMP-dependent protein kinase activity; ISO:RGD.
DR GO; GO:0043086; P:negative regulation of catalytic activity; ISO:RGD.
DR GO; GO:0042308; P:negative regulation of protein import into nucleus; ISO:RGD.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; ISO:RGD.
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_0000154536"
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:1Q8U"
SQ SEQUENCE 76 AA; 7960 MW; FCCE07281498788A CRC64;
MTDVETTYAD FIASGRTGRR NAIHDILVSS ASGNSNELAL KLAGLDINKT EGEDDGQRSS
TEQSGEAQGE AAKSES
