KAP0_BOVIN
ID KAP0_BOVIN Reviewed; 380 AA.
AC P00514; A5D9F4; Q17QP8;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 193.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Basal ganglia;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 2-380, AND ACETYLATION AT ALA-2.
RX PubMed=6487597; DOI=10.1021/bi00313a028;
RA Titani K., Sasagawa T., Ericsson L.H., Kumar S., Smith S.B., Krebs E.G.,
RA Walsh K.A.;
RT "Amino acid sequence of the regulatory subunit of bovine type I adenosine
RT cyclic 3',5'-phosphate dependent protein kinase.";
RL Biochemistry 23:4193-4199(1984).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 214-232.
RX PubMed=6190178; DOI=10.1073/pnas.80.12.3608;
RA Lee D.C., Carmichael D.F., Krebs E.G., McKnight G.S.;
RT "Isolation of a cDNA clone for the type I regulatory subunit of bovine
RT cAMP-dependent protein kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:3608-3612(1983).
RN [5]
RP 3D-STRUCTURE MODELING.
RX PubMed=3030405; DOI=10.1021/bi00376a003;
RA Weber I.T., Steitz T.A., Bubis J., Taylor S.S.;
RT "Predicted structures of cAMP binding domains of type I and II regulatory
RT subunits of cAMP-dependent protein kinase.";
RL Biochemistry 26:343-351(1987).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 114-380.
RX PubMed=7638597; DOI=10.1126/science.7638597;
RA Su Y., Dostmann W.R., Herberg F.W., Durick K., Xuong N.H., ten Eyck L.,
RA Taylor S.S., Varughese K.I.;
RT "Regulatory subunit of protein kinase A: structure of deletion mutant with
RT cAMP binding domains.";
RL Science 269:807-813(1995).
RN [7]
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.
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 -!- INTERACTION:
CC P00514; P00514: PRKAR1A; NbExp=5; IntAct=EBI-1041635, EBI-1041635;
CC P00514; O43572: AKAP10; Xeno; NbExp=2; IntAct=EBI-1041635, EBI-752153;
CC P00514; P05132: Prkaca; Xeno; NbExp=6; IntAct=EBI-1041635, EBI-400564;
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. The physiological significance of the in vitro
CC phosphorylation of a proximal serine is unclear.
CC -!- SIMILARITY: Belongs to the cAMP-dependent kinase regulatory chain
CC family. {ECO:0000305}.
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DR EMBL; BT030573; ABQ13013.1; -; mRNA.
DR EMBL; BC118242; AAI18243.1; -; mRNA.
DR EMBL; K00833; AAA30708.1; -; mRNA.
DR PIR; A00617; OKBO1R.
DR PIR; I45957; I45957.
DR RefSeq; NP_001069826.1; NM_001076358.1.
DR PDB; 1NE4; X-ray; 2.40 A; A=95-377.
DR PDB; 1NE6; X-ray; 2.30 A; A=95-377.
DR PDB; 1RGS; X-ray; 2.80 A; A=93-380.
DR PDB; 1RL3; X-ray; 2.70 A; A/B=93-380.
DR PDB; 2EZW; NMR; -; A/B=13-62.
DR PDB; 2QCS; X-ray; 2.20 A; B=91-380.
DR PDB; 3FHI; X-ray; 2.00 A; B=92-245.
DR PDB; 3IIA; X-ray; 2.70 A; A=92-245.
DR PDB; 3IM3; X-ray; 2.00 A; A=13-62.
DR PDB; 3IM4; X-ray; 2.28 A; A/B=13-62.
DR PDB; 3PLQ; X-ray; 2.30 A; A=92-245.
DR PDB; 3PNA; X-ray; 1.50 A; A/B=92-245.
DR PDB; 3PVB; X-ray; 3.30 A; B=85-244.
DR PDB; 4JV4; X-ray; 2.95 A; A=93-380.
DR PDB; 4MX3; X-ray; 3.88 A; A/B=2-380.
DR PDB; 4X6R; X-ray; 2.40 A; B=91-380.
DR PDB; 5HVZ; X-ray; 2.00 A; A/B=13-62.
DR PDB; 5JR7; X-ray; 3.56 A; B/D=92-366.
DR PDB; 6BYR; X-ray; 3.66 A; B/D=2-380.
DR PDB; 6BYS; X-ray; 4.75 A; B/D/F/H=2-380.
DR PDB; 6NO7; X-ray; 3.55 A; B/D/F/H=1-380.
DR PDB; 7LZ4; X-ray; 4.16 A; A/B/C/D/E/F/G/H=109-377.
DR PDBsum; 1NE4; -.
DR PDBsum; 1NE6; -.
DR PDBsum; 1RGS; -.
DR PDBsum; 1RL3; -.
DR PDBsum; 2EZW; -.
DR PDBsum; 2QCS; -.
DR PDBsum; 3FHI; -.
DR PDBsum; 3IIA; -.
DR PDBsum; 3IM3; -.
DR PDBsum; 3IM4; -.
DR PDBsum; 3PLQ; -.
DR PDBsum; 3PNA; -.
DR PDBsum; 3PVB; -.
DR PDBsum; 4JV4; -.
DR PDBsum; 4MX3; -.
DR PDBsum; 4X6R; -.
DR PDBsum; 5HVZ; -.
DR PDBsum; 5JR7; -.
DR PDBsum; 6BYR; -.
DR PDBsum; 6BYS; -.
DR PDBsum; 6NO7; -.
DR PDBsum; 7LZ4; -.
DR AlphaFoldDB; P00514; -.
DR SMR; P00514; -.
DR DIP; DIP-36644N; -.
DR IntAct; P00514; 3.
DR MINT; P00514; -.
DR STRING; 9913.ENSBTAP00000011371; -.
DR BindingDB; P00514; -.
DR iPTMnet; P00514; -.
DR PaxDb; P00514; -.
DR PRIDE; P00514; -.
DR Ensembl; ENSBTAT00000011371; ENSBTAP00000011371; ENSBTAG00000008621.
DR GeneID; 615074; -.
DR KEGG; bta:615074; -.
DR CTD; 5573; -.
DR VEuPathDB; HostDB:ENSBTAG00000008621; -.
DR VGNC; VGNC:33324; PRKAR1A.
DR eggNOG; KOG1113; Eukaryota.
DR GeneTree; ENSGT00940000155148; -.
DR HOGENOM; CLU_018310_1_0_1; -.
DR InParanoid; P00514; -.
DR OMA; DQWERAN; -.
DR OrthoDB; 1047290at2759; -.
DR TreeFam; TF314920; -.
DR EvolutionaryTrace; P00514; -.
DR PRO; PR:P00514; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000008621; Expressed in prefrontal cortex and 106 other tissues.
DR ExpressionAtlas; P00514; baseline and differential.
DR GO; GO:0005930; C:axoneme; IEA:Ensembl.
DR GO; GO:0005952; C:cAMP-dependent protein kinase complex; IMP:CAFA.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IDA:CAFA.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0001772; C:immunological synapse; IEA:Ensembl.
DR GO; GO:0005771; C:multivesicular body; IEA:Ensembl.
DR GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
DR GO; GO:0031588; C:nucleotide-activated protein kinase complex; IEA:Ensembl.
DR GO; GO:0044853; C:plasma membrane raft; IEA:Ensembl.
DR GO; GO:0097224; C:sperm connecting piece; IEA:Ensembl.
DR GO; GO:0030552; F:cAMP binding; IBA:GO_Central.
DR GO; GO:0004862; F:cAMP-dependent protein kinase inhibitor activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0034236; F:protein kinase A catalytic subunit binding; IPI:CAFA.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0060038; P:cardiac muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0001707; P:mesoderm formation; IEA:Ensembl.
DR GO; GO:0046007; P:negative regulation of activated T cell proliferation; IEA:Ensembl.
DR GO; GO:2000480; P:negative regulation of cAMP-dependent protein kinase activity; IBA:GO_Central.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:0045214; P:sarcomere organization; IEA:Ensembl.
DR CDD; cd00038; CAP_ED; 2.
DR DisProt; DP00245; -.
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 3D-structure; Acetylation; cAMP; cAMP-binding; Cell membrane;
KW Direct protein sequencing; Disulfide bond; Membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..380
FT /note="cAMP-dependent protein kinase type I-alpha
FT regulatory subunit"
FT /id="PRO_0000423216"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000269|PubMed:6487597"
FT CHAIN 2..380
FT /note="cAMP-dependent protein kinase type I-alpha
FT regulatory subunit, N-terminally processed"
FT /id="PRO_0000205376"
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:0000269|PubMed:6487597"
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-37)"
FT /evidence="ECO:0000269|PubMed:3667618"
FT DISULFID 38
FT /note="Interchain (with C-16)"
FT /evidence="ECO:0000269|PubMed:3667618"
FT CONFLICT 230
FT /note="Y -> N (in Ref. 4; AAA30708)"
FT /evidence="ECO:0000305"
FT HELIX 14..23
FT /evidence="ECO:0007829|PDB:3IM3"
FT HELIX 26..40
FT /evidence="ECO:0007829|PDB:3IM3"
FT HELIX 45..61
FT /evidence="ECO:0007829|PDB:3IM3"
FT HELIX 106..109
FT /evidence="ECO:0007829|PDB:3FHI"
FT HELIX 121..133
FT /evidence="ECO:0007829|PDB:3PNA"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:3PNA"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:3IIA"
FT HELIX 142..151
FT /evidence="ECO:0007829|PDB:3PNA"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:3PNA"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:3PNA"
FT STRAND 172..179
FT /evidence="ECO:0007829|PDB:3PNA"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:3PNA"
FT STRAND 188..193
FT /evidence="ECO:0007829|PDB:3PNA"
FT HELIX 202..206
FT /evidence="ECO:0007829|PDB:3PNA"
FT STRAND 211..218
FT /evidence="ECO:0007829|PDB:3PNA"
FT STRAND 220..226
FT /evidence="ECO:0007829|PDB:3PNA"
FT HELIX 227..233
FT /evidence="ECO:0007829|PDB:3PNA"
FT HELIX 235..240
FT /evidence="ECO:0007829|PDB:3PNA"
FT HELIX 246..250
FT /evidence="ECO:0007829|PDB:1RL3"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:2QCS"
FT HELIX 260..269
FT /evidence="ECO:0007829|PDB:2QCS"
FT STRAND 271..275
FT /evidence="ECO:0007829|PDB:2QCS"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:1RL3"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:2QCS"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:1NE4"
FT STRAND 290..304
FT /evidence="ECO:0007829|PDB:2QCS"
FT STRAND 305..309
FT /evidence="ECO:0007829|PDB:1NE4"
FT STRAND 311..317
FT /evidence="ECO:0007829|PDB:2QCS"
FT STRAND 322..324
FT /evidence="ECO:0007829|PDB:1RGS"
FT HELIX 326..328
FT /evidence="ECO:0007829|PDB:2QCS"
FT STRAND 335..350
FT /evidence="ECO:0007829|PDB:2QCS"
FT HELIX 351..358
FT /evidence="ECO:0007829|PDB:2QCS"
FT HELIX 361..365
FT /evidence="ECO:0007829|PDB:2QCS"
FT HELIX 369..375
FT /evidence="ECO:0007829|PDB:2QCS"
SQ SEQUENCE 380 AA; 42893 MW; B086A291809422F4 CRC64;
MASGTTASEE ERSLRECELY VQKHNIQALL KDSIVQLCTA RPERPMAFLR EYFEKLEKEE
AKQIQNLQKA GSRADSREDE ISPPPPNPVV KGRRRRGAIS AEVYTEEDAA SYVRKVIPKD
YKTMAALAKA IEKNVLFSHL DDNERSDIFD AMFPVSFIAG ETVIQQGDEG DNFYVIDQGE
MDVYVNNEWA TSVGEGGSFG ELALIYGTPR AATVKAKTNV KLWGIDRDSY RRILMGSTLR
KRKMYEEFLS KVSILESLDK WERLTVADAL EPVQFEDGQK IVVQGEPGDE FFIILEGSAA
VLQRRSENEE FVEVGRLGPS DYFGEIALLM NRPRAATVVA RGPLKCVKLD RPRFERVLGP
CSDILKRNIQ QYNSFVSLSV
