ID   IPKB_RAT                Reviewed;          71 AA.
AC   P27775;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 109.
DE   RecName: Full=cAMP-dependent protein kinase inhibitor beta;
DE   AltName: Full=PKI-beta;
DE   AltName: Full=cAMP-dependent protein kinase inhibitor, testis isoform;
GN   Name=Pkib;
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], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Testis;
RX   PubMed=2052616; DOI=10.1073/pnas.88.12.5383;
RA   van Patten S.M., Ng D.C., Th'Ng J.P.H., Angelos K.L., Smith A.J.,
RA   Walsh D.A.;
RT   "Molecular cloning of a rat testis form of the inhibitor protein of cAMP-
RT   dependent protein kinase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:5383-5387(1991).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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: Testis.
CC   -!- SIMILARITY: Belongs to the PKI family. {ECO:0000305}.
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DR   EMBL; M64092; AAA41879.1; -; mRNA.
DR   PIR; A40962; A40962.
DR   AlphaFoldDB; P27775; -.
DR   STRING; 10116.ENSRNOP00000001075; -.
DR   iPTMnet; P27775; -.
DR   PhosphoSitePlus; P27775; -.
DR   PaxDb; P27775; -.
DR   RGD; 3335; Pkib.
DR   eggNOG; ENOG502S8BW; Eukaryota.
DR   InParanoid; P27775; -.
DR   PRO; PR:P27775; -.
DR   Proteomes; UP000002494; Unplaced.
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; ISO:RGD.
DR   GO; GO:2000480; P:negative regulation of cAMP-dependent protein kinase activity; ISO:RGD.
DR   GO; GO:0051973; P:positive regulation of telomerase activity; ISO:RGD.
DR   GO; GO:1904355; P:positive regulation of telomere capping; ISO:RGD.
DR   GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; 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   Direct protein sequencing; Phosphoprotein; Protein kinase inhibitor;
KW   Reference proteome.
FT   CHAIN           1..71
FT                   /note="cAMP-dependent protein kinase inhibitor beta"
FT                   /id="PRO_0000154540"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          51..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
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="Blocked amino end (Thr)"
FT   MOD_RES         35
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   71 AA;  7585 MW;  63FB306AD91398D2 CRC64;
     MTDVESVISS FASSARAGRR NALPDIQSSL ATGGSPDLAL KLEALAVKED AKMKNEEKDQ
     GQPKKPLDED K