KCC2D_CAEBR
ID KCC2D_CAEBR Reviewed; 533 AA.
AC A8WXF6;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Calcium/calmodulin-dependent protein kinase type II {ECO:0000250|UniProtKB:O62305};
DE Short=CaM kinase II {ECO:0000250|UniProtKB:O62305};
DE EC=2.7.11.17;
DE AltName: Full=Uncoordinated protein 43;
GN Name=unc-43 {ECO:0000312|EMBL:CAP25104.1}; ORFNames=CBG04391;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1] {ECO:0000312|EMBL:CAP25104.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
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.A., 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.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: Role in locomotion and neuronal cell fate specification.
CC Required for the regulation of synaptic density, egg laying,
CC defecation, and meiotic maturation. Required for viability under
CC chronic osmotic stress in which it acts downstream of osr-1. Regulates
CC the synaptic trafficking of glr-1. Bidirectional modulator of
CC neurotransmitter release with negative modulatory effects mainly
CC mediated via slo-1 activation. May suppress the functional response to
CC an internal pacemaker, perhaps by modulating the activity of the IP3
CC receptor (By similarity). {ECO:0000250|UniProtKB:O62305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.17;
CC Evidence={ECO:0000250|UniProtKB:O62305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.17; Evidence={ECO:0000250|UniProtKB:O62305};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:O62305};
CC -!- ACTIVITY REGULATION: Ca(2+)/calmodulin binding removes an
CC autoinhibitory regulatory segment located C-terminal to the kinase
CC domain. This releases the catalytic activity of the enzyme and makes
CC accessible a regulatory residue Thr-284. Phosphorylation of Thr-284 by
CC another kinase domain within the oligomeric holoenzyme keeps CaMKII
CC active in the absence of Ca(2+)/calmodulin by preventing the rebinding
CC of the regulatory segment to the kinase domain and by increasing the
CC affinity of calmodulin for the enzyme. Can respond to high-frequency
CC Ca(2+) pulses to become Ca(2+) independent (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Dodecamer. Subunits are tightly packed around a central ring-
CC shaped scaffold with extensive contacts between the regulatory segment
CC of one kinase and the catalytic domain of another enabling cooperative
CC activation of a subunit by the adjacent molecule. Interacts with and
CC phosphorylates daf-16; the interaction promotes daf-16 nuclear
CC localization. Interacts with egl-2 and tir-1. Interacts with nsy-1.
CC {ECO:0000250|UniProtKB:O62305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O62305}. Cell
CC projection, axon {ECO:0000250|UniProtKB:O62305}. Perikaryon
CC {ECO:0000250|UniProtKB:O62305}. Note=Localizes at or near the Golgi
CC apparatus. Localizes to post-synaptic regions and is enriched in
CC punctate structures in axons of AWC neurons where it co-localizes with
CC tir-1. Localization is regulated by tir-1.
CC {ECO:0000250|UniProtKB:O62305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. CaMK subfamily. {ECO:0000255}.
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DR EMBL; HE601251; CAP25104.1; -; Genomic_DNA.
DR RefSeq; XP_002634394.1; XM_002634348.1.
DR AlphaFoldDB; A8WXF6; -.
DR SMR; A8WXF6; -.
DR STRING; 6238.CBG04391; -.
DR PRIDE; A8WXF6; -.
DR EnsemblMetazoa; CBG04391a.1; CBG04391a.1; WBGene00027073.
DR GeneID; 8576389; -.
DR KEGG; cbr:CBG_04391; -.
DR CTD; 8576389; -.
DR WormBase; CBG04391a; CBP01170; WBGene00027073; Cbr-unc-43.
DR eggNOG; KOG0033; Eukaryota.
DR HOGENOM; CLU_000288_71_0_1; -.
DR InParanoid; A8WXF6; -.
DR OMA; CIAYTRL; -.
DR OrthoDB; 330091at2759; -.
DR Proteomes; UP000008549; Chromosome IV.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
DR GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR013543; Ca/CaM-dep_prot_kinase-assoc.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF08332; CaMKII_AD; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF54427; SSF54427; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding; Calmodulin-binding; Cell projection; Cytoplasm; Kinase;
KW Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Stress response;
KW Transferase.
FT CHAIN 1..533
FT /note="Calcium/calmodulin-dependent protein kinase type II"
FT /id="PRO_0000396644"
FT REGION 316..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 134
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 18..26
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O62305,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 284
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:O62305"
SQ SEQUENCE 533 AA; 59583 MW; D2D3A61B344A0106 CRC64;
MMNACTKFSD NYDVKEELGK GAFSVVRRCV HKTTGLEFAA KIINTKKLSA RDFQKLEREA
RICRKLQHPN IVRLHDSIQE ESFHYLVFDL VTGGELFEDI VAREFYSEAD ASHCIQQILE
SIAYCHSNGV VHRDLKPENL LLASKAKGAA VKLADFGLAI EVNDSEAWHG FAGTPGYLSP
EVLKKDPYSK PVDIWACGVI LYILLVGYPP FWDEDQHRLY AQIKAGAYDY PSPEWDTVTP
EAKSLIDSML TVNPKKRITA DQALKVPWIC NRERVASAIH RQDTVDCLKK FNARRKLKAA
ISAVKMVTRM SGVLRTSDST GSVASNGSTT HDTSQIAGTS SQPTSPAAEG AILTTMIATR
NLSNLGRNLL NKKEQGPPST IKESSESSQT IDDNDSEKAQ KQDIVRVTQT LLDAISCKDF
DTYTRLCDTS MTCFEPEALG NLIEGIEFHR FYFDGNRKNQ VHTTMLNPNV HIIGEDAACV
AYVKLTQFLD RNGEAHTRQS QESRVWSKKQ GRWLCVHVHR STQPSTNTTV SEF
