IPKA_PIG
ID IPKA_PIG Reviewed; 76 AA.
AC Q71U53;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=cAMP-dependent protein kinase inhibitor alpha;
DE Short=PKI-alpha;
GN Name=PKIA;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Myocardium;
RA Knoell R., Nevescanin K., Schulze K., Hummel M., Zimmermann R., Stein H.,
RA Schaper W., Schultheiss H.P.;
RT "PKI alpha cDNA sequence.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000250}.
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; AF132737; AAF34733.1; -; mRNA.
DR RefSeq; NP_999369.1; NM_214204.1.
DR PDB; 1Q24; X-ray; 2.60 A; I=6-25.
DR PDB; 1Q61; X-ray; 2.10 A; I=6-25.
DR PDB; 2F7X; X-ray; 1.90 A; I=6-25.
DR PDBsum; 1Q24; -.
DR PDBsum; 1Q61; -.
DR PDBsum; 2F7X; -.
DR AlphaFoldDB; Q71U53; -.
DR SMR; Q71U53; -.
DR STRING; 9823.ENSSSCP00000006574; -.
DR PaxDb; Q71U53; -.
DR PeptideAtlas; Q71U53; -.
DR GeneID; 397408; -.
DR KEGG; ssc:397408; -.
DR CTD; 5569; -.
DR eggNOG; ENOG502S6JP; Eukaryota.
DR InParanoid; Q71U53; -.
DR OrthoDB; 1648219at2759; -.
DR EvolutionaryTrace; Q71U53; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0004862; F:cAMP-dependent protein kinase inhibitor activity; IEA:InterPro.
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_0000154534"
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..13
FT /evidence="ECO:0007829|PDB:2F7X"
SQ SEQUENCE 76 AA; 7989 MW; BDCE072810435951 CRC64;
MTDVETTYAD FIASGRTGRR NAIHDILVSS ASGNSNELAL KLAGLDINKT EGEEDAQRSS
TEQSGEAQGE AAKSES
