IPKA_BOVIN
ID IPKA_BOVIN Reviewed; 76 AA.
AC Q3SX13;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=cAMP-dependent protein kinase inhibitor alpha;
DE Short=PKI-alpha;
GN Name=PKIA;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) 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; BC104561; AAI04562.1; -; mRNA.
DR RefSeq; NP_001032709.1; NM_001037620.1.
DR PDB; 2GNJ; X-ray; 2.28 A; I=6-25.
DR PDB; 2UZT; X-ray; 2.10 A; B=6-25.
DR PDB; 2UZU; X-ray; 2.40 A; I=6-25.
DR PDB; 2UZV; X-ray; 2.50 A; 2=6-25.
DR PDB; 2UZW; X-ray; 2.20 A; I=6-25.
DR PDB; 3E8C; X-ray; 2.20 A; G/H/I/J/K/L=6-25.
DR PDB; 3E8E; X-ray; 2.00 A; C/F/G/J/N/Q=6-25.
DR PDB; 3ZO1; X-ray; 2.00 A; I=6-23.
DR PDB; 3ZO2; X-ray; 1.98 A; I=6-25.
DR PDB; 3ZO3; X-ray; 2.10 A; I=6-23.
DR PDB; 3ZO4; X-ray; 1.65 A; I=6-25.
DR PDB; 4C33; X-ray; 1.70 A; I=6-23.
DR PDB; 4C34; X-ray; 1.78 A; I=6-23.
DR PDB; 4C35; X-ray; 2.19 A; I=6-23.
DR PDB; 4C36; X-ray; 1.98 A; I=6-25.
DR PDB; 4C37; X-ray; 1.70 A; I=6-25.
DR PDB; 4C38; X-ray; 1.58 A; I=6-25.
DR PDB; 4YXR; X-ray; 2.00 A; I=6-25.
DR PDB; 5VHB; X-ray; 1.61 A; B=6-23.
DR PDB; 5VI9; X-ray; 1.95 A; B=6-23.
DR PDB; 5VIB; X-ray; 2.37 A; B=6-23.
DR PDBsum; 2GNJ; -.
DR PDBsum; 2UZT; -.
DR PDBsum; 2UZU; -.
DR PDBsum; 2UZV; -.
DR PDBsum; 2UZW; -.
DR PDBsum; 3E8C; -.
DR PDBsum; 3E8E; -.
DR PDBsum; 3ZO1; -.
DR PDBsum; 3ZO2; -.
DR PDBsum; 3ZO3; -.
DR PDBsum; 3ZO4; -.
DR PDBsum; 4C33; -.
DR PDBsum; 4C34; -.
DR PDBsum; 4C35; -.
DR PDBsum; 4C36; -.
DR PDBsum; 4C37; -.
DR PDBsum; 4C38; -.
DR PDBsum; 4YXR; -.
DR PDBsum; 5VHB; -.
DR PDBsum; 5VI9; -.
DR PDBsum; 5VIB; -.
DR AlphaFoldDB; Q3SX13; -.
DR BMRB; Q3SX13; -.
DR SMR; Q3SX13; -.
DR STRING; 9913.ENSBTAP00000010711; -.
DR PaxDb; Q3SX13; -.
DR PRIDE; Q3SX13; -.
DR Ensembl; ENSBTAT00000074880; ENSBTAP00000068262; ENSBTAG00000008150.
DR GeneID; 613524; -.
DR KEGG; bta:613524; -.
DR CTD; 5569; -.
DR VEuPathDB; HostDB:ENSBTAG00000008150; -.
DR VGNC; VGNC:32940; PKIA.
DR eggNOG; ENOG502S6JP; Eukaryota.
DR GeneTree; ENSGT00530000064276; -.
DR HOGENOM; CLU_163471_2_0_1; -.
DR InParanoid; Q3SX13; -.
DR OrthoDB; 1468806at2759; -.
DR TreeFam; TF330809; -.
DR EvolutionaryTrace; Q3SX13; -.
DR Proteomes; UP000009136; Chromosome 14.
DR Bgee; ENSBTAG00000008150; Expressed in gluteus medius and 102 other tissues.
DR ExpressionAtlas; Q3SX13; baseline.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004862; F:cAMP-dependent protein kinase inhibitor activity; IBA:GO_Central.
DR GO; GO:2000480; P:negative regulation of cAMP-dependent protein kinase activity; IBA:GO_Central.
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_0000154531"
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:4C38"
SQ SEQUENCE 76 AA; 8016 MW; BDDBDD1810435951 CRC64;
MTDVETTYAD FIASGRTGRR NAIHDILVSS ASGNSNELAL KLAGLDINKT EGEEDAQRNS
TEQSGEAQGE AAKSES
