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Database: UniProt
Entry: A8XKP2_CAEBR
LinkDB: A8XKP2_CAEBR
Original site: A8XKP2_CAEBR 
ID   A8XKP2_CAEBR            Unreviewed;       366 AA.
AC   A8XKP2;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 2.
DT   27-MAR-2024, entry version 93.
DE   SubName: Full=Protein CBR-KIN-2 {ECO:0000313|EMBL:CAP33216.2};
GN   Name=kin-2 {ECO:0000313|WormBase:CBG14791};
GN   Synonyms=Cbr-kin-2 {ECO:0000313|EMBL:CAP33216.2};
GN   ORFNames=CBG14791 {ECO:0000313|WormBase:CBG14791}, CBG_14791
GN   {ECO:0000313|EMBL:CAP33216.2};
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238 {ECO:0000313|EMBL:CAP33216.2, ECO:0000313|Proteomes:UP000008549};
RN   [1] {ECO:0000313|EMBL:CAP33216.2, ECO:0000313|Proteomes:UP000008549}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16 {ECO:0000313|EMBL:CAP33216.2,
RC   ECO:0000313|Proteomes:UP000008549};
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- SIMILARITY: Belongs to the cAMP-dependent kinase regulatory chain
CC       family. {ECO:0000256|ARBA:ARBA00005753}.
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DR   EMBL; HE600983; CAP33216.2; -; Genomic_DNA.
DR   AlphaFoldDB; A8XKP2; -.
DR   STRING; 6238.A8XKP2; -.
DR   EnsemblMetazoa; CBG14791.1; CBG14791.1; WBGene00035185.
DR   WormBase; CBG14791; CBP32511; WBGene00035185; Cbr-kin-2.
DR   eggNOG; KOG1113; Eukaryota.
DR   HOGENOM; CLU_018310_1_1_1; -.
DR   InParanoid; A8XKP2; -.
DR   OMA; DQWERAN; -.
DR   OrthoDB; 55978at2759; -.
DR   Proteomes; UP000008549; Unassembled WGS sequence.
DR   GO; GO:0005952; C:cAMP-dependent protein kinase complex; IEA:EnsemblMetazoa.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IEA:EnsemblMetazoa.
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:0072375; P:medium-term memory; IEA:EnsemblMetazoa.
DR   GO; GO:1900194; P:negative regulation of oocyte maturation; IEA:EnsemblMetazoa.
DR   GO; GO:0090038; P:negative regulation of protein kinase C signaling; IEA:EnsemblMetazoa.
DR   GO; GO:0010628; P:positive regulation of gene expression; IEA:EnsemblMetazoa.
DR   GO; GO:2000114; P:regulation of establishment of cell polarity; IEA:EnsemblMetazoa.
DR   GO; GO:0001932; P:regulation of protein phosphorylation; IEA:InterPro.
DR   CDD; cd00038; CAP_ED; 2.
DR   CDD; cd12097; DD_RI_PKA; 1.
DR   Gene3D; 1.20.890.10; cAMP-dependent protein kinase regulatory subunit, dimerization-anchoring domain; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 2.
DR   InterPro; IPR012198; cAMP_dep_PK_reg_su.
DR   InterPro; IPR003117; cAMP_dep_PK_reg_su_I/II_a/b.
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:SF126; CAMP-DEPENDENT PROTEIN KINASE TYPE I-BETA REGULATORY SUBUNIT; 1.
DR   Pfam; PF00027; cNMP_binding; 2.
DR   Pfam; PF02197; RIIa; 1.
DR   PIRSF; PIRSF000548; PK_regulatory; 1.
DR   PRINTS; PR00103; CAMPKINASE.
DR   SMART; SM00100; cNMP; 2.
DR   SMART; SM00394; RIIa; 1.
DR   SUPFAM; SSF51206; cAMP-binding domain-like; 2.
DR   SUPFAM; SSF47391; Dimerization-anchoring domain of cAMP-dependent PK regulatory subunit; 1.
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}; Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000548-1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008549};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          122..237
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   DOMAIN          240..361
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   REGION          55..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         187
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         196
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         311
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         320
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   366 AA;  41497 MW;  BF407D4235027943 CRC64;
     MSGGNEEDQL AQCQAYVQRH NVQQLVKEAI VVLCIHKPDN PVLFLKDHFE KLNEQRSQEG
     GNPDTVDDDD IIVEPPKRSG GRRTGISAEP IKEDDTEYKK VVIPKDDATR KSLEAAMRKN
     LLFAHLEEDE QKTMYDAMFP VEKNGGETII EQGEEGDNFY VIDKGTVDVY VNHEYVLTIN
     EGGSFGELAL IYGTPRAATV IAKTDVKLWA IDRLTYRRIL MGSVTKKRKM YDEFLSKVQI
     LADLDQWERA NVADALERCD FEPGTHVVEQ GQPGDEFFII LEGEANVLQK RSDDAPFDVV
     GHLGMSDYFG EIALLLDRPR AATVVAKTHL KCIKLDRNRF ERVMGPVREI LKRDVSNYNS
     YVKLMT
//
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