KAP0_PONAB
ID KAP0_PONAB Reviewed; 381 AA.
AC Q5REL1; Q5R492; Q5R729;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=cAMP-dependent protein kinase type I-alpha regulatory subunit;
GN Name=PRKAR1A;
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: Regulatory subunit of the cAMP-dependent protein kinases
CC involved in cAMP signaling in cells. {ECO:0000250}.
CC -!- SUBUNIT: The inactive holoenzyme is composed of two regulatory chains
CC and two catalytic chains. Activation by cAMP releases the two active
CC catalytic monomers and the regulatory dimer. Interacts with PRKACA and
CC PRKACB (By similarity). PRKAR1A also interacts with RFC2; the complex
CC may be involved in cell survival. Interacts with AKAP4. Interacts with
CC RARA; the interaction occurs in the presence of cAMP or FSH and
CC regulates RARA transcriptional activity. Interacts with the
CC phosphorylated form of PJA2. Interacts with CBFA2T3. Interacts with
CC PRKX; regulates this cAMP-dependent protein kinase (By similarity).
CC Interacts with smAKAP; this interaction may target PRKAR1A to the
CC plasma membrane. Interacts with AICDA (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P10644}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}.
CC -!- PTM: The pseudophosphorylation site binds to the substrate-binding
CC region of the catalytic chain, resulting in the inhibition of its
CC activity. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cAMP-dependent kinase regulatory chain
CC family. {ECO:0000305}.
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DR EMBL; CR857513; CAH89796.1; -; mRNA.
DR EMBL; CR860291; CAH92431.1; -; mRNA.
DR EMBL; CR861364; CAH93424.1; -; mRNA.
DR RefSeq; NP_001124827.1; NM_001131355.1.
DR RefSeq; XP_009234925.1; XM_009236650.1.
DR RefSeq; XP_009234926.1; XM_009236651.1.
DR RefSeq; XP_009234927.1; XM_009236652.1.
DR AlphaFoldDB; Q5REL1; -.
DR SMR; Q5REL1; -.
DR STRING; 9601.ENSPPYP00000010056; -.
DR Ensembl; ENSPPYT00000010457; ENSPPYP00000010056; ENSPPYG00000008962.
DR GeneID; 100171685; -.
DR KEGG; pon:100171685; -.
DR CTD; 5573; -.
DR eggNOG; KOG1113; Eukaryota.
DR GeneTree; ENSGT00940000155148; -.
DR HOGENOM; CLU_018310_1_0_1; -.
DR InParanoid; Q5REL1; -.
DR OMA; DQWERAN; -.
DR OrthoDB; 1047290at2759; -.
DR TreeFam; TF314920; -.
DR Proteomes; UP000001595; Chromosome 17.
DR GO; GO:0005952; C:cAMP-dependent protein kinase complex; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030552; F:cAMP binding; IEA:UniProtKB-KW.
DR GO; GO:0008603; F:cAMP-dependent protein kinase regulator activity; IEA:InterPro.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IEA:InterPro.
DR CDD; cd00038; CAP_ED; 2.
DR Gene3D; 2.60.120.10; -; 2.
DR InterPro; IPR012198; cAMP_dep_PK_reg_su.
DR InterPro; IPR003117; cAMP_dep_PK_reg_su_I/II_a/b.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR018488; cNMP-bd_CS.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR Pfam; PF00027; cNMP_binding; 2.
DR Pfam; PF02197; RIIa; 1.
DR PIRSF; PIRSF000548; PK_regulatory; 1.
DR SMART; SM00100; cNMP; 2.
DR SMART; SM00394; RIIa; 1.
DR SUPFAM; SSF51206; SSF51206; 2.
DR PROSITE; PS00888; CNMP_BINDING_1; 2.
DR PROSITE; PS00889; CNMP_BINDING_2; 2.
DR PROSITE; PS50042; CNMP_BINDING_3; 2.
PE 2: Evidence at transcript level;
KW Acetylation; cAMP; cAMP-binding; Cell membrane; Disulfide bond; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..381
FT /note="cAMP-dependent protein kinase type I-alpha
FT regulatory subunit"
FT /id="PRO_0000293482"
FT REGION 1..135
FT /note="Dimerization and phosphorylation"
FT /evidence="ECO:0000250"
FT REGION 64..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 96..100
FT /note="Pseudophosphorylation motif"
FT BINDING 137..254
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT BINDING 202
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 211
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 255..381
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT BINDING 326
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 335
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P10644"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09456"
FT MOD_RES 75
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P10644"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10644"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10644"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBC7"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09456"
FT DISULFID 18
FT /note="Interchain (with C-39)"
FT /evidence="ECO:0000250"
FT DISULFID 39
FT /note="Interchain (with C-18)"
FT /evidence="ECO:0000250"
FT CONFLICT 12
FT /note="A -> V (in Ref. 1; CAH93424)"
FT /evidence="ECO:0000305"
FT CONFLICT 77
FT /note="S -> P (in Ref. 1; CAH89796)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="P -> S (in Ref. 1; CAH93424)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 381 AA; 42982 MW; 2D04F08CE8857A6D CRC64;
MESGSTAASE EARSLRECEL YVQKHNIQAL LKDSIVQLCT ARPERPMAFL REYFERLEKE
EAKQIQNLQK AGTRTDSRED EISPPPPNPV VKGRRRRGAI SAEVYTEEDA ASYVRKVIPK
DYKTMAALAK AIEKNVLFSH LDDNERSDIF DAMFSVSFIA GETVIQQGDE GDNFYVIDQG
ETDVYVNNEW ATSVGEGGSF GELALIYGTP RAATVKAKTN VKLWGIDRDS YRRILMGSTL
RKRKMYEEFL SKVSILESLD KWERLTVADA LEPVQFEDGQ KIVVQGEPGD EFFIILEGSA
AVLQRRSENE EFVEVGRLGP SDYFGEIALL MNRPRAATVV ARGPLKCVKL DRPRFERVLG
PCSDILKRNI QQYNSFVSLS V
