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cAMP-dependent protein kinase type I-alpha regulatory subunit [Cleaved into: cAMP-dependent protein kinase type I-alpha regulatory subunit, N-terminally processed]

 KAP0_BOVIN              Reviewed;         380 AA.
P00514; A5D9F4; Q17QP8;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
17-APR-2007, sequence version 2.
05-DEC-2018, entry version 172.
RecName: Full=cAMP-dependent protein kinase type I-alpha regulatory subunit;
Contains:
RecName: Full=cAMP-dependent protein kinase type I-alpha regulatory subunit, N-terminally processed;
Name=PRKAR1A;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=16305752; DOI=10.1186/1471-2164-6-166;
Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
"Characterization of 954 bovine full-CDS cDNA sequences.";
BMC Genomics 6:166-166(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford; TISSUE=Basal ganglia;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
[3]
PROTEIN SEQUENCE OF 2-380, AND ACETYLATION AT ALA-2.
PubMed=6487597; DOI=10.1021/bi00313a028;
Titani K., Sasagawa T., Ericsson L.H., Kumar S., Smith S.B.,
Krebs E.G., Walsh K.A.;
"Amino acid sequence of the regulatory subunit of bovine type I
adenosine cyclic 3',5'-phosphate dependent protein kinase.";
Biochemistry 23:4193-4199(1984).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 214-232.
PubMed=6190178; DOI=10.1073/pnas.80.12.3608;
Lee D.C., Carmichael D.F., Krebs E.G., McKnight G.S.;
"Isolation of a cDNA clone for the type I regulatory subunit of bovine
cAMP-dependent protein kinase.";
Proc. Natl. Acad. Sci. U.S.A. 80:3608-3612(1983).
[5]
3D-STRUCTURE MODELING.
PubMed=3030405; DOI=10.1021/bi00376a003;
Weber I.T., Steitz T.A., Bubis J., Taylor S.S.;
"Predicted structures of cAMP binding domains of type I and II
regulatory subunits of cAMP-dependent protein kinase.";
Biochemistry 26:343-351(1987).
[6]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 114-380.
PubMed=7638597; DOI=10.1126/science.7638597;
Su Y., Dostmann W.R., Herberg F.W., Durick K., Xuong N.H.,
ten Eyck L., Taylor S.S., Varughese K.I.;
"Regulatory subunit of protein kinase A: structure of deletion mutant
with cAMP binding domains.";
Science 269:807-813(1995).
[7]
DISULFIDE BONDS.
PubMed=3667618;
Bubis J., Vedvick T.S., Taylor S.S.;
"Antiparallel alignment of the two protomers of the regulatory subunit
dimer of cAMP-dependent protein kinase I.";
J. Biol. Chem. 262:14961-14966(1987).
-!- FUNCTION: Regulatory subunit of the cAMP-dependent protein kinases
involved in cAMP signaling in cells.
-!- SUBUNIT: The inactive holoenzyme is composed of two regulatory
chains and two catalytic chains. Activation by cAMP releases the
two active catalytic monomers and the regulatory dimer. PRKAR1A
also interacts with RFC2; the complex may be involved in cell
survival. Interacts with AKAP4. Interacts with RARA; the
interaction occurs in the presence of cAMP or FSH and regulates
RARA transcriptional activity (By similarity). Interacts with the
phosphorylated form of PJA2 (By similarity). Interacts with
CBFA2T3 (By similarity). Interacts with PRKX; regulates this cAMP-
dependent protein kinase (By similarity). Interacts with smAKAP;
this interaction may target PRKAR1A to the plasma membrane (By
similarity). Interacts with AICDA (By similarity). {ECO:0000250}.
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-1041635, EBI-1041635;
O43572:AKAP10 (xeno); NbExp=2; IntAct=EBI-1041635, EBI-752153;
P05132:Prkaca (xeno); NbExp=6; IntAct=EBI-1041635, EBI-400564;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}.
-!- TISSUE SPECIFICITY: Four types of regulatory chains are found: I-
alpha, I-beta, II-alpha, and II-beta. Their expression varies
among tissues and is in some cases constitutive and in others
inducible.
-!- PTM: The pseudophosphorylation site binds to the substrate-binding
region of the catalytic chain, resulting in the inhibition of its
activity. The physiological significance of the in vitro
phosphorylation of a proximal serine is unclear.
-!- SIMILARITY: Belongs to the cAMP-dependent kinase regulatory chain
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; BT030573; ABQ13013.1; -; mRNA.
EMBL; BC118242; AAI18243.1; -; mRNA.
EMBL; K00833; AAA30708.1; -; mRNA.
PIR; A00617; OKBO1R.
PIR; I45957; I45957.
RefSeq; NP_001069826.1; NM_001076358.1.
UniGene; Bt.10903; -.
PDB; 1APK; Model; -; A=2-380.
PDB; 1BPK; Model; -; A=2-380.
PDB; 1NE4; X-ray; 2.40 A; A=95-377.
PDB; 1NE6; X-ray; 2.30 A; A=95-377.
PDB; 1PVK; Model; -; A=114-245.
PDB; 1RGS; X-ray; 2.80 A; A=93-380.
PDB; 1RL3; X-ray; 2.70 A; A/B=93-380.
PDB; 2EZW; NMR; -; A/B=13-62.
PDB; 2QCS; X-ray; 2.20 A; B=91-380.
PDB; 3FHI; X-ray; 2.00 A; B=92-245.
PDB; 3IIA; X-ray; 2.70 A; A=92-245.
PDB; 3IM3; X-ray; 2.00 A; A=13-62.
PDB; 3IM4; X-ray; 2.28 A; A/B=13-62.
PDB; 3PLQ; X-ray; 2.30 A; A=92-245.
PDB; 3PNA; X-ray; 1.50 A; A/B=92-245.
PDB; 3PVB; X-ray; 3.30 A; B=85-244.
PDB; 4JV4; X-ray; 2.95 A; A=93-380.
PDB; 4MX3; X-ray; 3.88 A; A/B=2-380.
PDB; 4X6R; X-ray; 2.40 A; B=91-380.
PDB; 5HVZ; X-ray; 2.00 A; A/B=13-62.
PDB; 5JR7; X-ray; 3.56 A; B/D=92-366.
PDBsum; 1APK; -.
PDBsum; 1BPK; -.
PDBsum; 1NE4; -.
PDBsum; 1NE6; -.
PDBsum; 1PVK; -.
PDBsum; 1RGS; -.
PDBsum; 1RL3; -.
PDBsum; 2EZW; -.
PDBsum; 2QCS; -.
PDBsum; 3FHI; -.
PDBsum; 3IIA; -.
PDBsum; 3IM3; -.
PDBsum; 3IM4; -.
PDBsum; 3PLQ; -.
PDBsum; 3PNA; -.
PDBsum; 3PVB; -.
PDBsum; 4JV4; -.
PDBsum; 4MX3; -.
PDBsum; 4X6R; -.
PDBsum; 5HVZ; -.
PDBsum; 5JR7; -.
DisProt; DP00245; -.
ProteinModelPortal; P00514; -.
SMR; P00514; -.
DIP; DIP-36644N; -.
IntAct; P00514; 3.
MINT; P00514; -.
STRING; 9913.ENSBTAP00000011371; -.
BindingDB; P00514; -.
iPTMnet; P00514; -.
PaxDb; P00514; -.
PRIDE; P00514; -.
Ensembl; ENSBTAT00000011371; ENSBTAP00000011371; ENSBTAG00000008621.
GeneID; 615074; -.
KEGG; bta:615074; -.
CTD; 5573; -.
VGNC; VGNC:33324; PRKAR1A.
eggNOG; KOG1113; Eukaryota.
eggNOG; COG0664; LUCA.
GeneTree; ENSGT00940000155148; -.
HOGENOM; HOG000196669; -.
HOVERGEN; HBG002025; -.
InParanoid; P00514; -.
KO; K04739; -.
OMA; VQLCTVR; -.
OrthoDB; EOG091G0F1K; -.
TreeFam; TF314920; -.
Reactome; R-BTA-163615; PKA activation.
Reactome; R-BTA-164378; PKA activation in glucagon signalling.
Reactome; R-BTA-180024; DARPP-32 events.
Reactome; R-BTA-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
Reactome; R-BTA-5610787; Hedgehog 'off' state.
Reactome; R-BTA-983231; Factors involved in megakaryocyte development and platelet production.
EvolutionaryTrace; P00514; -.
PRO; PR:P00514; -.
Proteomes; UP000009136; Chromosome 19.
Bgee; ENSBTAG00000008621; Expressed in 9 organ(s), highest expression level in testis.
GO; GO:0005930; C:axoneme; IEA:Ensembl.
GO; GO:0005952; C:cAMP-dependent protein kinase complex; IMP:CAFA.
GO; GO:0005737; C:cytoplasm; IDA:CAFA.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
GO; GO:0001772; C:immunological synapse; IEA:Ensembl.
GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
GO; GO:0031588; C:nucleotide-activated protein kinase complex; IEA:Ensembl.
GO; GO:0044853; C:plasma membrane raft; IEA:Ensembl.
GO; GO:0047555; F:3',5'-cyclic-GMP phosphodiesterase activity; IBA:GO_Central.
GO; GO:0030552; F:cAMP binding; IEA:UniProtKB-KW.
GO; GO:0004862; F:cAMP-dependent protein kinase inhibitor activity; IEA:Ensembl.
GO; GO:0008603; F:cAMP-dependent protein kinase regulator activity; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
GO; GO:0034236; F:protein kinase A catalytic subunit binding; IPI:CAFA.
GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
GO; GO:0060038; P:cardiac muscle cell proliferation; IEA:Ensembl.
GO; GO:0019934; P:cGMP-mediated signaling; IBA:GO_Central.
GO; GO:0001707; P:mesoderm formation; IEA:Ensembl.
GO; GO:0046007; P:negative regulation of activated T cell proliferation; IEA:Ensembl.
GO; GO:2000480; P:negative regulation of cAMP-dependent protein kinase activity; IEA:Ensembl.
GO; GO:0045214; P:sarcomere organization; IEA:Ensembl.
CDD; cd00038; CAP_ED; 2.
Gene3D; 2.60.120.10; -; 2.
InterPro; IPR012198; cAMP_dep_PK_reg_su.
InterPro; IPR003117; cAMP_dep_PK_reg_su_I/II_a/b.
InterPro; IPR018490; cNMP-bd-like.
InterPro; IPR018488; cNMP-bd_CS.
InterPro; IPR000595; cNMP-bd_dom.
InterPro; IPR014710; RmlC-like_jellyroll.
Pfam; PF00027; cNMP_binding; 2.
Pfam; PF02197; RIIa; 1.
PIRSF; PIRSF000548; PK_regulatory; 1.
SMART; SM00100; cNMP; 2.
SMART; SM00394; RIIa; 1.
SUPFAM; SSF51206; SSF51206; 2.
PROSITE; PS00888; CNMP_BINDING_1; 2.
PROSITE; PS00889; CNMP_BINDING_2; 2.
PROSITE; PS50042; CNMP_BINDING_3; 2.
1: Evidence at protein level;
3D-structure; Acetylation; cAMP; cAMP-binding; Cell membrane;
Complete proteome; Direct protein sequencing; Disulfide bond;
Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome;
Repeat.
CHAIN 1 380 cAMP-dependent protein kinase type I-
alpha regulatory subunit.
/FTId=PRO_0000423216.
INIT_MET 1 1 Removed; alternate.
{ECO:0000269|PubMed:6487597}.
CHAIN 2 380 cAMP-dependent protein kinase type I-
alpha regulatory subunit, N-terminally
processed.
/FTId=PRO_0000205376.
NP_BIND 136 253 cAMP 1.
NP_BIND 254 380 cAMP 2.
REGION 2 135 Dimerization and phosphorylation.
MOTIF 95 99 Pseudophosphorylation motif.
BINDING 201 201 cAMP 1.
BINDING 210 210 cAMP 1.
BINDING 325 325 cAMP 2.
BINDING 334 334 cAMP 2.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P10644}.
MOD_RES 2 2 N-acetylalanine; in cAMP-dependent
protein kinase type I-alpha regulatory
subunit, N-terminally processed.
{ECO:0000269|PubMed:6487597}.
MOD_RES 3 3 Phosphoserine.
{ECO:0000250|UniProtKB:P09456}.
MOD_RES 76 76 Phosphoserine.
{ECO:0000250|UniProtKB:P10644}.
MOD_RES 82 82 Phosphoserine.
{ECO:0000250|UniProtKB:P10644}.
MOD_RES 100 100 Phosphoserine.
{ECO:0000250|UniProtKB:Q9DBC7}.
MOD_RES 257 257 Phosphoserine.
{ECO:0000250|UniProtKB:P09456}.
DISULFID 17 17 Interchain (with C-37).
{ECO:0000269|PubMed:3667618}.
DISULFID 38 38 Interchain (with C-16).
{ECO:0000269|PubMed:3667618}.
CONFLICT 230 230 Y -> N (in Ref. 4; AAA30708).
{ECO:0000305}.
HELIX 14 23 {ECO:0000244|PDB:3IM3}.
HELIX 26 40 {ECO:0000244|PDB:3IM3}.
HELIX 45 61 {ECO:0000244|PDB:3IM3}.
HELIX 106 109 {ECO:0000244|PDB:3FHI}.
HELIX 121 133 {ECO:0000244|PDB:3PNA}.
HELIX 135 137 {ECO:0000244|PDB:3PNA}.
STRAND 138 140 {ECO:0000244|PDB:3IIA}.
HELIX 142 151 {ECO:0000244|PDB:3PNA}.
STRAND 153 157 {ECO:0000244|PDB:3PNA}.
STRAND 162 164 {ECO:0000244|PDB:3PNA}.
STRAND 172 179 {ECO:0000244|PDB:3PNA}.
STRAND 181 185 {ECO:0000244|PDB:3PNA}.
STRAND 188 193 {ECO:0000244|PDB:3PNA}.
HELIX 202 206 {ECO:0000244|PDB:3PNA}.
STRAND 211 218 {ECO:0000244|PDB:3PNA}.
STRAND 220 226 {ECO:0000244|PDB:3PNA}.
HELIX 227 233 {ECO:0000244|PDB:3PNA}.
HELIX 235 240 {ECO:0000244|PDB:3PNA}.
HELIX 246 250 {ECO:0000244|PDB:1RL3}.
HELIX 253 255 {ECO:0000244|PDB:2QCS}.
HELIX 260 269 {ECO:0000244|PDB:2QCS}.
STRAND 271 275 {ECO:0000244|PDB:2QCS}.
STRAND 277 279 {ECO:0000244|PDB:1RL3}.
STRAND 280 282 {ECO:0000244|PDB:2QCS}.
STRAND 284 286 {ECO:0000244|PDB:1NE4}.
STRAND 290 304 {ECO:0000244|PDB:2QCS}.
STRAND 305 309 {ECO:0000244|PDB:1NE4}.
STRAND 311 317 {ECO:0000244|PDB:2QCS}.
STRAND 322 324 {ECO:0000244|PDB:1RGS}.
HELIX 326 328 {ECO:0000244|PDB:2QCS}.
STRAND 335 350 {ECO:0000244|PDB:2QCS}.
HELIX 351 358 {ECO:0000244|PDB:2QCS}.
HELIX 361 365 {ECO:0000244|PDB:2QCS}.
HELIX 369 375 {ECO:0000244|PDB:2QCS}.
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


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