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Database: UniProt
Entry: W5Q3N5_SHEEP
LinkDB: W5Q3N5_SHEEP
Original site: W5Q3N5_SHEEP 
ID   W5Q3N5_SHEEP            Unreviewed;       305 AA.
AC   W5Q3N5;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=cAMP-dependent protein kinase type II-alpha regulatory subunit {ECO:0000256|ARBA:ARBA00041039};
GN   Name=PRKAR2A {ECO:0000313|Ensembl:ENSOARP00000017324.1};
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000017324.1, ECO:0000313|Proteomes:UP000002356};
RN   [1] {ECO:0000313|Ensembl:ENSOARP00000017324.1, ECO:0000313|Proteomes:UP000002356}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000017324.1,
RC   ECO:0000313|Proteomes:UP000002356};
RX   PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
RA   Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
RA   Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., Wang J.,
RA   Wang W., Xun X.;
RT   "The sheep genome reference sequence: a work in progress.";
RL   Anim. Genet. 41:449-453(2010).
RN   [2] {ECO:0000313|Ensembl:ENSOARP00000017324.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Regulatory subunit of the cAMP-dependent protein kinases
CC       involved in cAMP signaling in cells. Type II regulatory chains mediate
CC       membrane association by binding to anchoring proteins, including the
CC       MAP2 kinase. {ECO:0000256|ARBA:ARBA00037198}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC   -!- SIMILARITY: Belongs to the cAMP-dependent kinase regulatory chain
CC       family. {ECO:0000256|ARBA:ARBA00005753}.
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DR   EMBL; AMGL01045668; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; W5Q3N5; -.
DR   SMR; W5Q3N5; -.
DR   STRING; 9940.ENSOARP00000017324; -.
DR   PaxDb; 9940-ENSOARP00000017324; -.
DR   Ensembl; ENSOART00000017569.1; ENSOARP00000017324.1; ENSOARG00000016132.1.
DR   eggNOG; KOG1113; Eukaryota.
DR   HOGENOM; CLU_018310_2_0_1; -.
DR   OMA; NPYERSK; -.
DR   Proteomes; UP000002356; Chromosome 19.
DR   Bgee; ENSOARG00000016132; Expressed in skeletal muscle tissue of biceps brachii and 55 other cell types or tissues.
DR   GO; GO:0005952; C:cAMP-dependent protein kinase complex; IEA:InterPro.
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; Jelly Rolls; 2.
DR   InterPro; IPR012198; cAMP_dep_PK_reg_su.
DR   InterPro; IPR018488; cNMP-bd_CS.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR018490; cNMP-bd_dom_sf.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   PANTHER; PTHR11635; CAMP-DEPENDENT PROTEIN KINASE REGULATORY CHAIN; 1.
DR   PANTHER; PTHR11635:SF153; CAMP-DEPENDENT PROTEIN KINASE TYPE II-ALPHA REGULATORY SUBUNIT; 1.
DR   Pfam; PF00027; cNMP_binding; 2.
DR   PIRSF; PIRSF000548; PK_regulatory; 1.
DR   PRINTS; PR00103; CAMPKINASE.
DR   SMART; SM00100; cNMP; 2.
DR   SUPFAM; SSF51206; cAMP-binding domain-like; 2.
DR   PROSITE; PS00888; CNMP_BINDING_1; 2.
DR   PROSITE; PS00889; CNMP_BINDING_2; 2.
DR   PROSITE; PS50042; CNMP_BINDING_3; 2.
PE   3: Inferred from homology;
KW   cAMP {ECO:0000256|ARBA:ARBA00023149, ECO:0000256|PIRSR:PIRSR000548-1};
KW   cAMP-binding {ECO:0000256|ARBA:ARBA00022566, ECO:0000256|PIRSR:PIRSR000548-
KW   1}; Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000548-1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002356}.
FT   DOMAIN          40..159
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   DOMAIN          162..289
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   BINDING         109
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000548-1"
FT   BINDING         118
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000548-1"
FT   BINDING         239
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000548-1"
FT   BINDING         248
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000548-1"
SQ   SEQUENCE   305 AA;  34652 MW;  73DC13A9256F160B CRC64;
     VCAETYNPDE EEEDTDPRVI HPKTDQQRCR LQEACKDILL FKNLDPEQLS QVLDAMFERT
     VKVDEHVIDQ GDDGDNFYVI ERGTYDILVT KDNQTRSVGQ YDNHGSFGEL ALMYNTPRAA
     TIVATSEGSL WGLDRVTFRR IIVKNNAKKR KMFESFIESV PLLKSLEVSE RMKIVDVIGE
     KVYKDGERII TQGEKADSFY IIESGEVSIL IKSKTKVNKD GENQEVEIAR CRKGQYFGEL
     ALVTNKPRAA SAYAVGDVKC LVMDVQAFER LLGPCMDIMK RNISHYEEQL VKMFGSSMDL
     IDPGQ
//
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