ID   ARP21_PONAB             Reviewed;          89 AA.
AC   Q5R6X9;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=cAMP-regulated phosphoprotein 21;
DE            Short=ARPP-21;
GN   Name=ARPP21;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May act as a competitive inhibitor of calmodulin-dependent
CC       enzymes such as calcineurin in neurons. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with CALM1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- PTM: Phosphorylation at Ser-56 favors interaction with CALM1.
CC       {ECO:0000250}.
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DR   EMBL; CR860347; CAH92481.1; -; mRNA.
DR   RefSeq; NP_001126463.1; NM_001132991.2.
DR   RefSeq; XP_009237508.1; XM_009239233.1.
DR   RefSeq; XP_009237509.1; XM_009239234.1.
DR   RefSeq; XP_009237510.1; XM_009239235.1.
DR   AlphaFoldDB; Q5R6X9; -.
DR   STRING; 9601.ENSPPYP00000015689; -.
DR   Ensembl; ENSPPYT00000040679; ENSPPYP00000035104; ENSPPYG00000014027.
DR   GeneID; 100173450; -.
DR   KEGG; pon:100173450; -.
DR   CTD; 10777; -.
DR   eggNOG; KOG2953; Eukaryota.
DR   GeneTree; ENSGT00940000160796; -.
DR   InParanoid; Q5R6X9; -.
DR   Proteomes; UP000001595; Chromosome 3.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
PE   3: Inferred from homology;
KW   Acetylation; Calmodulin-binding; Cytoplasm; Phosphoprotein;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q7M2N1"
FT   CHAIN           2..89
FT                   /note="cAMP-regulated phosphoprotein 21"
FT                   /id="PRO_0000064684"
FT   REGION          1..89
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..28
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..59
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7M2N1"
FT   MOD_RES         33
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UBL0"
FT   MOD_RES         56
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9DCB4"
SQ   SEQUENCE   89 AA;  9674 MW;  94654817C61B4C94 CRC64;
     MSEQGDLNQA IAEEGGTEQE TATPENGIVK SESLDEEEKL ELQRRLEAQN QERRKSKSGA
     GKGKLTRSLA VCEESSARPG GESLQDQTL