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Database: UniProt
Entry: P00514
LinkDB: P00514
Original site: P00514 
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   10-FEB-2021, entry version 187.
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;
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. PRKAR1A also interacts
CC       with RFC2; the complex may be involved in cell survival. Interacts with
CC       AKAP4. Interacts with RARA; the interaction occurs in the presence of
CC       cAMP or FSH and regulates RARA transcriptional activity (By
CC       similarity). Interacts with the phosphorylated form of PJA2 (By
CC       similarity). Interacts with CBFA2T3 (By similarity). 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 (By similarity). Interacts with AICDA (By similarity).
CC       {ECO:0000250}.
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; 1APK; Model; -; A=2-380.
DR   PDB; 1BPK; Model; -; A=2-380.
DR   PDB; 1NE4; X-ray; 2.40 A; A=95-377.
DR   PDB; 1NE6; X-ray; 2.30 A; A=95-377.
DR   PDB; 1PVK; Model; -; A=114-245.
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   PDBsum; 1APK; -.
DR   PDBsum; 1BPK; -.
DR   PDBsum; 1NE4; -.
DR   PDBsum; 1NE6; -.
DR   PDBsum; 1PVK; -.
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   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   VGNC; VGNC:33324; PRKAR1A.
DR   eggNOG; KOG1113; Eukaryota.
DR   GeneTree; ENSGT00940000155148; -.
DR   HOGENOM; CLU_018310_1_0_1; -.
DR   InParanoid; P00514; -.
DR   OMA; YELYMNA; -.
DR   OrthoDB; 1047290at2759; -.
DR   TreeFam; TF314920; -.
DR   EvolutionaryTrace; P00514; -.
DR   PRO; PR:P00514; -.
DR   Proteomes; UP000009136; Chromosome 19.
DR   Bgee; ENSBTAG00000008621; Expressed in testis and 18 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; IEA:UniProtKB-KW.
DR   GO; GO:0004862; F:cAMP-dependent protein kinase inhibitor activity; IEA:Ensembl.
DR   GO; GO:0008603; F:cAMP-dependent protein kinase regulator 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:0043949; P:regulation of cAMP-mediated signaling; IBA:GO_Central.
DR   GO; GO:0010738; P:regulation of protein kinase A signaling; IBA:GO_Central.
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   NP_BIND         136..253
FT                   /note="cAMP 1"
FT   NP_BIND         254..380
FT                   /note="cAMP 2"
FT   REGION          2..135
FT                   /note="Dimerization and phosphorylation"
FT   MOTIF           95..99
FT                   /note="Pseudophosphorylation motif"
FT   BINDING         201
FT                   /note="cAMP 1"
FT   BINDING         210
FT                   /note="cAMP 1"
FT   BINDING         325
FT                   /note="cAMP 2"
FT   BINDING         334
FT                   /note="cAMP 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:0000244|PDB:3IM3"
FT   HELIX           26..40
FT                   /evidence="ECO:0000244|PDB:3IM3"
FT   HELIX           45..61
FT                   /evidence="ECO:0000244|PDB:3IM3"
FT   HELIX           106..109
FT                   /evidence="ECO:0000244|PDB:3FHI"
FT   HELIX           121..133
FT                   /evidence="ECO:0000244|PDB:3PNA"
FT   HELIX           135..137
FT                   /evidence="ECO:0000244|PDB:3PNA"
FT   STRAND          138..140
FT                   /evidence="ECO:0000244|PDB:3IIA"
FT   HELIX           142..151
FT                   /evidence="ECO:0000244|PDB:3PNA"
FT   STRAND          153..157
FT                   /evidence="ECO:0000244|PDB:3PNA"
FT   STRAND          162..164
FT                   /evidence="ECO:0000244|PDB:3PNA"
FT   STRAND          172..179
FT                   /evidence="ECO:0000244|PDB:3PNA"
FT   STRAND          181..185
FT                   /evidence="ECO:0000244|PDB:3PNA"
FT   STRAND          188..193
FT                   /evidence="ECO:0000244|PDB:3PNA"
FT   HELIX           202..206
FT                   /evidence="ECO:0000244|PDB:3PNA"
FT   STRAND          211..218
FT                   /evidence="ECO:0000244|PDB:3PNA"
FT   STRAND          220..226
FT                   /evidence="ECO:0000244|PDB:3PNA"
FT   HELIX           227..233
FT                   /evidence="ECO:0000244|PDB:3PNA"
FT   HELIX           235..240
FT                   /evidence="ECO:0000244|PDB:3PNA"
FT   HELIX           246..250
FT                   /evidence="ECO:0000244|PDB:1RL3"
FT   HELIX           253..255
FT                   /evidence="ECO:0000244|PDB:2QCS"
FT   HELIX           260..269
FT                   /evidence="ECO:0000244|PDB:2QCS"
FT   STRAND          271..275
FT                   /evidence="ECO:0000244|PDB:2QCS"
FT   STRAND          277..279
FT                   /evidence="ECO:0000244|PDB:1RL3"
FT   STRAND          280..282
FT                   /evidence="ECO:0000244|PDB:2QCS"
FT   STRAND          284..286
FT                   /evidence="ECO:0000244|PDB:1NE4"
FT   STRAND          290..304
FT                   /evidence="ECO:0000244|PDB:2QCS"
FT   STRAND          305..309
FT                   /evidence="ECO:0000244|PDB:1NE4"
FT   STRAND          311..317
FT                   /evidence="ECO:0000244|PDB:2QCS"
FT   STRAND          322..324
FT                   /evidence="ECO:0000244|PDB:1RGS"
FT   HELIX           326..328
FT                   /evidence="ECO:0000244|PDB:2QCS"
FT   STRAND          335..350
FT                   /evidence="ECO:0000244|PDB:2QCS"
FT   HELIX           351..358
FT                   /evidence="ECO:0000244|PDB:2QCS"
FT   HELIX           361..365
FT                   /evidence="ECO:0000244|PDB:2QCS"
FT   HELIX           369..375
FT                   /evidence="ECO:0000244|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
//
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