KCC2D_XENLA
ID KCC2D_XENLA Reviewed; 475 AA.
AC Q9DG02;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Calcium/calmodulin-dependent protein kinase type II delta chain;
DE Short=CaM kinase II subunit delta;
DE Short=CaM-kinase II delta chain;
DE Short=CaMK-II subunit delta;
DE EC=2.7.11.17;
GN Name=camk2d;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovary;
RX PubMed=11275554; DOI=10.1093/oxfordjournals.jbchem.a002890;
RA Stevens I., Rondelez E., Merlevede W., Goris J.;
RT "Cloning and differential expression of new calcium, calmodulin-dependent
RT protein kinase II isoforms in Xenopus laevis oocytes and several adult
RT tissues.";
RL J. Biochem. 129:551-560(2001).
CC -!- FUNCTION: CaM-kinase II (CAMK2) is a prominent kinase in the central
CC nervous system. {ECO:0000250}.
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 -!- 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;
CC -!- ACTIVITY REGULATION: Autophosphorylation of CAMK2 plays an important
CC role in the regulation of the kinase activity. {ECO:0000250}.
CC -!- SUBUNIT: CAMK2 is composed of four different chains: alpha, beta,
CC gamma, and delta. The different isoforms assemble into homo- or
CC heteromultimeric holoenzymes composed of 8 to 12 subunits (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. CaMK subfamily. {ECO:0000305}.
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DR EMBL; AF233629; AAG17554.1; -; mRNA.
DR RefSeq; NP_001083858.1; NM_001090389.1.
DR AlphaFoldDB; Q9DG02; -.
DR SMR; Q9DG02; -.
DR BioGRID; 100485; 1.
DR IntAct; Q9DG02; 1.
DR GeneID; 399160; -.
DR KEGG; xla:399160; -.
DR CTD; 399160; -.
DR Xenbase; XB-GENE-868304; camk2d.S.
DR OrthoDB; 330091at2759; -.
DR BRENDA; 2.7.11.17; 6725.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 399160; Expressed in brain and 19 other tissues.
DR GO; GO:0043226; C:organelle; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IEA:UniProtKB-EC.
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 2: Evidence at transcript level;
KW ATP-binding; Calmodulin-binding; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..475
FT /note="Calcium/calmodulin-dependent protein kinase type II
FT delta chain"
FT /id="PRO_0000277822"
FT DOMAIN 13..271
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 135
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 19..27
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 286
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 317
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 335
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 475 AA; 53933 MW; 7C312F4CB686A68A CRC64;
MASTTCTRFT DEYQLFEELG KGAFSVVRRC IKINIGQEYA AKIINTKKLS ARDHQKLERE
AKICRLLKHP NIVRLHDSIS EEGFHYLVFD LVTGGELFED IVAREYYSEA DASHCIQQIL
ESVNHCHLNG IVHRDLKPEN LLLASKLKGA AVKLADFGLA IEVQGDQQAW FGFAGTPGYL
SPEVLRKDPY GKPVDMWACG VILYILLVGY PPFWDEDQHR LYQQIKAGAY DFPSPEWDTV
TPEAKDLINK MLTINPAKRI NATEALRHPW ICQRSTVASM MHRQETVDCL KKFNARRKLK
GAILTTMLAT RNFSAKSLLK KPDGVKESTE SSNTTIEDED VKARKQEIIK VTEQLIEAIN
NGDFEAYTKI CDPGLTSFEP EALGNLVEGM DFHRFYFENA LSKSNKPVHT IILNPHVHLI
GEDAACIAYI RLTQYLDSAG MPKTMQSEET RVWHRRDGKW QNVHFHRSGS PTIPN
