ID M3WFD5_FELCA Unreviewed; 86 AA.
AC M3WFD5;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 3.
DT 24-JAN-2024, entry version 58.
DE RecName: Full=cAMP-dependent protein kinase inhibitor {ECO:0000256|PIRNR:PIRNR001667};
GN Name=PKIB {ECO:0000313|Ensembl:ENSFCAP00000010762.4,
GN ECO:0000313|VGNC:VGNC:68875};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000010762.4, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000010762.4, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000010762.4,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000010762.4, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000010762.4,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000010762.4}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000010762.4};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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:0000256|ARBA:ARBA00002844}.
CC -!- SIMILARITY: Belongs to the PKI family. {ECO:0000256|ARBA:ARBA00006393,
CC ECO:0000256|PIRNR:PIRNR001667}.
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DR EMBL; AANG04000169; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; M3WFD5; -.
DR Ensembl; ENSFCAT00000011596.5; ENSFCAP00000010762.4; ENSFCAG00000011594.5.
DR VGNC; VGNC:68875; PKIB.
DR eggNOG; ENOG502S8BW; Eukaryota.
DR GeneTree; ENSGT00530000064264; -.
DR HOGENOM; CLU_163471_1_0_1; -.
DR Proteomes; UP000011712; Chromosome B2.
DR Bgee; ENSFCAG00000011594; Expressed in eyeball of camera-type eye and 11 other cell types or tissues.
DR GO; GO:0004862; F:cAMP-dependent protein kinase inhibitor activity; IEA:UniProtKB-UniRule.
DR InterPro; IPR004171; cAMP_dep_PKI.
DR PANTHER; PTHR15416:SF6; CAMP-DEPENDENT PROTEIN KINASE INHIBITOR BETA; 1.
DR PANTHER; PTHR15416; CAMP-DEPENDENT PROTEIN KINASE INHIBITOR/PKI; 1.
DR Pfam; PF02827; PKI; 1.
DR PIRSF; PIRSF001667; PKI; 1.
PE 3: Inferred from homology;
KW Protein kinase inhibitor {ECO:0000256|PIRNR:PIRNR001667};
KW Reference proteome {ECO:0000313|Proteomes:UP000011712}.
FT REGION 30..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 64..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 31
FT /note="Important for inhibition"
FT /evidence="ECO:0000256|PIRSR:PIRSR001667-1"
FT SITE 34
FT /note="Important for inhibition"
FT /evidence="ECO:0000256|PIRSR:PIRSR001667-1"
FT SITE 35
FT /note="Important for inhibition"
FT /evidence="ECO:0000256|PIRSR:PIRSR001667-1"
SQ SEQUENCE 86 AA; 9499 MW; 07A2C60A4AE48803 CRC64;
TRLCQYVAMR TDSSKMTDVE PVVNNFASSA RTGRRNAVPD IQGSAGTGGI SELPLRLEAL
SMEEDVKKKD EETTQCQLEK PPKEEK
//
