KAPR_CAEEL
ID KAPR_CAEEL Reviewed; 366 AA.
AC P30625; Q0MQ68; Q21820; Q95ZR1;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 3.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=cAMP-dependent protein kinase regulatory subunit;
GN Name=kin-2; Synonyms=kin-a; ORFNames=R07E4.6;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Bristol N2;
RX PubMed=2303451; DOI=10.1016/s0021-9258(19)39766-2;
RA Lu X., Gross R.E., Bagchi S., Rubin C.S.;
RT "Cloning, structure, and expression of the gene for a novel regulatory
RT subunit of cAMP-dependent protein kinase in Caenorhabditis elegans.";
RL J. Biol. Chem. 265:3293-3303(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION, AND MUTAGENESIS OF GLY-310.
RX PubMed=24086161; DOI=10.1371/journal.pgen.1003831;
RA Wang H., Sieburth D.;
RT "PKA controls calcium influx into motor neurons during a rhythmic
RT behavior.";
RL PLoS Genet. 9:E1003831-E1003831(2013).
CC -!- FUNCTION: Controls the rhythmic contraction of enteric muscles probably
CC by regulating G-protein coupled receptor aex-2-mediated calcium influx
CC in GABAergic DVB neurons. {ECO:0000269|PubMed:24086161}.
CC -!- SUBUNIT: Tetramer, composed of 2 regulatory (R) and 2 catalytic (C)
CC subunits. In the presence of cAMP it dissociates into 2 active
CC monomeric C subunits and an R dimer that binds four cAMP molecules.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:2303451}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=a {ECO:0000312|WormBase:R07E4.6a};
CC IsoId=P30625-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:R07E4.6b};
CC IsoId=P30625-2; Sequence=VSP_015952;
CC Name=c {ECO:0000312|WormBase:R07E4.6c};
CC IsoId=P30625-3; Sequence=VSP_057512;
CC -!- DEVELOPMENTAL STAGE: Expressed at a low level during embryogenesis.
CC Expression increases sharply approximately four hours before hatching
CC with levels peaking during the first larval stage. Levels then decrease
CC as development progresses to adulthood. {ECO:0000269|PubMed:2303451}.
CC -!- PTM: The pseudophosphorylation site binds to the substrate-binding
CC region of the catalytic chain but is not phosphorylated. The
CC physiological significance of phosphorylations by other kinases is
CC unclear.
CC -!- SIMILARITY: Belongs to the cAMP-dependent kinase regulatory chain
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA27980.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; J05220; AAA27980.1; ALT_INIT; mRNA.
DR EMBL; FO080885; CCD67512.1; -; Genomic_DNA.
DR EMBL; FO080885; CCD67513.1; -; Genomic_DNA.
DR EMBL; FO080885; CCD67514.1; -; Genomic_DNA.
DR PIR; A35076; OKKW1R.
DR PIR; T16701; T16701.
DR RefSeq; NP_001024842.1; NM_001029671.3. [P30625-2]
DR RefSeq; NP_001076771.1; NM_001083302.1. [P30625-3]
DR RefSeq; NP_508999.2; NM_076598.5.
DR AlphaFoldDB; P30625; -.
DR SMR; P30625; -.
DR BioGRID; 45796; 26.
DR DIP; DIP-26281N; -.
DR IntAct; P30625; 9.
DR STRING; 6239.R07E4.6c; -.
DR EPD; P30625; -.
DR PaxDb; P30625; -.
DR PeptideAtlas; P30625; -.
DR PRIDE; P30625; -.
DR EnsemblMetazoa; R07E4.6a.1; R07E4.6a.1; WBGene00002190. [P30625-1]
DR EnsemblMetazoa; R07E4.6b.1; R07E4.6b.1; WBGene00002190. [P30625-2]
DR EnsemblMetazoa; R07E4.6c.1; R07E4.6c.1; WBGene00002190. [P30625-3]
DR GeneID; 180864; -.
DR KEGG; cel:CELE_R07E4.6; -.
DR UCSC; R07E4.6a; c. elegans.
DR CTD; 180864; -.
DR WormBase; R07E4.6a; CE39609; WBGene00002190; kin-2. [P30625-1]
DR WormBase; R07E4.6b; CE28749; WBGene00002190; kin-2. [P30625-2]
DR WormBase; R07E4.6c; CE04821; WBGene00002190; kin-2. [P30625-3]
DR eggNOG; KOG1113; Eukaryota.
DR GeneTree; ENSGT00940000157513; -.
DR HOGENOM; CLU_018310_1_0_1; -.
DR InParanoid; P30625; -.
DR OMA; DQWERAN; -.
DR OrthoDB; 1047290at2759; -.
DR Reactome; R-CEL-163615; PKA activation.
DR Reactome; R-CEL-164378; PKA activation in glucagon signalling.
DR Reactome; R-CEL-180024; DARPP-32 events.
DR Reactome; R-CEL-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR Reactome; R-CEL-442720; CREB1 phosphorylation through the activation of Adenylate Cyclase.
DR Reactome; R-CEL-5610787; Hedgehog 'off' state.
DR Reactome; R-CEL-9634597; GPER1 signaling.
DR Reactome; R-CEL-983231; Factors involved in megakaryocyte development and platelet production.
DR PRO; PR:P30625; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00002190; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005952; C:cAMP-dependent protein kinase complex; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:WormBase.
DR GO; GO:0016020; C:membrane; IDA:WormBase.
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:0008603; F:cAMP-dependent protein kinase regulator activity; ISS:WormBase.
DR GO; GO:0034236; F:protein kinase A catalytic subunit binding; IBA:GO_Central.
DR GO; GO:0072375; P:medium-term memory; IMP:WormBase.
DR GO; GO:2000480; P:negative regulation of cAMP-dependent protein kinase activity; IBA:GO_Central.
DR GO; GO:1900194; P:negative regulation of oocyte maturation; IMP:WormBase.
DR GO; GO:0090038; P:negative regulation of protein kinase C signaling; IGI:WormBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:2000114; P:regulation of establishment of cell polarity; IGI:WormBase.
DR CDD; cd00038; CAP_ED; 2.
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 Alternative splicing; cAMP; cAMP-binding; Cytoplasm; Disulfide bond;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..366
FT /note="cAMP-dependent protein kinase regulatory subunit"
FT /id="PRO_0000205394"
FT REGION 1..121
FT /note="Dimerization and phosphorylation"
FT REGION 55..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 82..86
FT /note="Pseudophosphorylation motif"
FT BINDING 122..239
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT BINDING 187
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT BINDING 196
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT BINDING 240..366
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT BINDING 311
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT BINDING 320
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT DISULFID 13
FT /note="Interchain (with C-34)"
FT /evidence="ECO:0000250"
FT DISULFID 34
FT /note="Interchain (with C-13)"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..58
FT /note="MSGGNEEDQLAQCQAYVQRHNIQQLVKEAIVVLCIHKPDNPVLFLKDHFEKL
FT NEQRAQ -> MGQQLSNRRNSQSVGATKNAKTPKPK (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_015952"
FT VAR_SEQ 1
FT /note="M -> MNNYSGDIVFM (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_057512"
FT MUTAGEN 310
FT /note="G->D: Loss of cAMP binding which may prevent
FT dissociation from kin-1. Contraction of enteric muscles is
FT partially impaired."
FT /evidence="ECO:0000269|PubMed:24086161"
FT CONFLICT 204
FT /note="T -> I (in Ref. 1; AAA27980)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="A -> V (in Ref. 1; AAA27980)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 366 AA; 41468 MW; 8EE6AF7111A58C0E CRC64;
MSGGNEEDQL AQCQAYVQRH NIQQLVKEAI VVLCIHKPDN PVLFLKDHFE KLNEQRAQEG
GNPDAADDDD IIVEPPKRSG GRRTGISAEP IKEDDTEYKK VVIPKDDATR RSLESAMRKN
LLFAHLEEDE QKTMYDAMFP VEKSAGETII EQGEEGDNFY VIDKGTVDVY VNHEYVLTIN
EGGSFGELAL IYGTPRAATV IAKTDVKLWA IDRLTYRRIL MGSVTKKRKM YDEFLSKVQI
LADLDQWERA NVADALERCD FEPGTHVVEQ GQPGDEFFII LEGEANVLQK RSDDAPFDVV
GHLGMSDYFG EIALLLDRPR AATVVAKTHL KCIKLDRNRF ERVMGPVREI LKRDVSNYNS
YVKLMT
