KAP0_PIG
ID KAP0_PIG Reviewed; 380 AA.
AC P07802;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=cAMP-dependent protein kinase type I-alpha regulatory subunit;
DE Contains:
DE RecName: Full=cAMP-dependent protein kinase type I-alpha regulatory subunit, N-terminally processed;
GN Name=PRKAR1A;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Kidney;
RX PubMed=3040400; DOI=10.1111/j.1432-1033.1987.tb13300.x;
RA Nowak I., Seipel K., Schwarz M., Jans D.A., Hemmings B.A.;
RT "Isolation of a cDNA and characterization of the 5' flanking region of the
RT gene encoding the type I regulatory subunit of the cAMP-dependent protein
RT kinase.";
RL Eur. J. Biochem. 167:27-33(1987).
RN [2]
RP DISULFIDE BONDS.
RX PubMed=3667618; DOI=10.1016/s0021-9258(18)48122-7;
RA Bubis J., Vedvick T.S., Taylor S.S.;
RT "Antiparallel alignment of the two protomers of the regulatory subunit
RT dimer of cAMP-dependent protein kinase I.";
RL J. Biol. Chem. 262:14961-14966(1987).
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 -!- TISSUE SPECIFICITY: Four types of regulatory chains are found: I-alpha,
CC I-beta, II-alpha, and II-beta. Their expression varies among tissues
CC and is in some cases constitutive and in others inducible.
CC -!- PTM: The pseudophosphorylation site binds to the substrate-binding
CC region of the catalytic chain, resulting in the inhibition of its
CC activity.
CC -!- SIMILARITY: Belongs to the cAMP-dependent kinase regulatory chain
CC family. {ECO:0000305}.
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DR EMBL; X05942; CAA29375.1; -; mRNA.
DR PIR; S00083; OKPG1R.
DR RefSeq; NP_999191.1; NM_214026.1.
DR AlphaFoldDB; P07802; -.
DR SMR; P07802; -.
DR STRING; 9823.ENSSSCP00000018286; -.
DR PaxDb; P07802; -.
DR PeptideAtlas; P07802; -.
DR PRIDE; P07802; -.
DR GeneID; 397091; -.
DR KEGG; ssc:397091; -.
DR CTD; 5573; -.
DR eggNOG; KOG1113; Eukaryota.
DR InParanoid; P07802; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005952; C:cAMP-dependent protein kinase complex; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IMP:AgBase.
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:1903538; P:regulation of meiotic cell cycle process involved in oocyte maturation; IMP:AgBase.
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 1: Evidence at protein level;
KW Acetylation; cAMP; cAMP-binding; Cell membrane; Direct protein sequencing;
KW Disulfide bond; Membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..380
FT /note="cAMP-dependent protein kinase type I-alpha
FT regulatory subunit"
FT /id="PRO_0000205379"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00514"
FT CHAIN 2..380
FT /note="cAMP-dependent protein kinase type I-alpha
FT regulatory subunit, N-terminally processed"
FT /id="PRO_0000423217"
FT REGION 2..135
FT /note="Dimerization and phosphorylation"
FT REGION 64..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 95..99
FT /note="Pseudophosphorylation motif"
FT BINDING 136..253
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT BINDING 201
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT BINDING 210
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT BINDING 254..380
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT BINDING 325
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT BINDING 334
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P10644"
FT MOD_RES 2
FT /note="N-acetylalanine; in cAMP-dependent protein kinase
FT type I-alpha regulatory subunit, N-terminally processed"
FT /evidence="ECO:0000250|UniProtKB:P00514"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09456"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10644"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10644"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBC7"
FT MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09456"
FT DISULFID 17
FT /note="Interchain (with C-38)"
FT /evidence="ECO:0000269|PubMed:3667618"
FT DISULFID 38
FT /note="Interchain (with C-17)"
FT /evidence="ECO:0000269|PubMed:3667618"
SQ SEQUENCE 380 AA; 42922 MW; 748FACEFF3167A18 CRC64;
MASGSTASEE ERSLRECELY VQKHNIQALL KDSIVQLCTA RPERPMAFLR EYFERLEKEE
AKQIQNLQKA SARADSREDE ISPPPPNPVV KGRRRRGAIS AEVYTEEDAA SYVRKVIPKD
YKTMAALAKA IEKNVLFSHL DDNERSDIFD AMFPVSFIAG ETVIQQGDEG DNFYVIDQGE
MDVYVNNEWA TSVGEGGSFG ELALIYGTPR AATVKAKTNV KLWGNDRDSY RRILMGSTLR
KRKMYEEFLS KVSILESLDK WERLTVADAL EPVQFEDGQK IVVQGEPGDE FFIILEGSAA
VLQRRSENEE FVEVGRLGPS DYFGEIALLM NRPRAATVVA RGPLKCVKLD RPRFERVLGP
CSDILKRNIQ QYNSFVSLSV
