KC2D2_DANRE
ID KC2D2_DANRE Reviewed; 554 AA.
AC Q6DGS3; A8WGM2;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Calcium/calmodulin-dependent protein kinase type II delta 2 chain;
DE EC=2.7.11.17;
DE AltName: Full=Calcium/calmodulin-dependent protein kinase type II delta-A chain;
DE Short=CaM kinase II subunit delta-A;
DE Short=CaM-kinase II delta-A chain;
DE Short=CaMK-II subunit delta-A;
GN Name=camk2d2; Synonyms=camk2d, camk2da; ORFNames=zgc:92792;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM E).
RC TISSUE=Brain, and Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 301-446 (ISOFORMS A; E AND O), ALTERNATIVE
RP SPLICING, AND TISSUE SPECIFICITY.
RX PubMed=17103413; DOI=10.1002/dvdy.21005;
RA Rothschild S.C., Lister J.A., Tombes R.M.;
RT "Differential expression of CaMK-II genes during early zebrafish
RT embryogenesis.";
RL Dev. Dyn. 236:295-305(2007).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=O;
CC IsoId=Q6DGS3-1; Sequence=Displayed;
CC Name=A;
CC IsoId=Q6DGS3-2; Sequence=VSP_035557;
CC Name=E;
CC IsoId=Q6DGS3-3; Sequence=VSP_035556, VSP_035557;
CC -!- TISSUE SPECIFICITY: First detected at 18 hpf. At 24 hpf, expressed in
CC discrete anterior locations and along either side of the midline. At 48
CC hpf, expression is predominantly in the forebrain, and then accumulates
CC in the forebrain, hindbrain, and retinal epithelium at 72 hpf.
CC {ECO:0000269|PubMed:17103413}.
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; BC076266; AAH76266.1; -; mRNA.
DR EMBL; BC154768; AAI54769.1; -; mRNA.
DR RefSeq; NP_001002542.1; NM_001002542.1. [Q6DGS3-3]
DR AlphaFoldDB; Q6DGS3; -.
DR SMR; Q6DGS3; -.
DR STRING; 7955.ENSDARP00000044895; -.
DR PaxDb; Q6DGS3; -.
DR PRIDE; Q6DGS3; -.
DR GeneID; 436815; -.
DR KEGG; dre:436815; -.
DR CTD; 436815; -.
DR ZFIN; ZDB-GENE-040718-277; camk2d2.
DR eggNOG; KOG0033; Eukaryota.
DR InParanoid; Q6DGS3; -.
DR PhylomeDB; Q6DGS3; -.
DR Reactome; R-DRE-3371571; HSF1-dependent transactivation.
DR Reactome; R-DRE-438066; Unblocking of NMDA receptors, glutamate binding and activation.
DR Reactome; R-DRE-5576892; Phase 0 - rapid depolarisation.
DR Reactome; R-DRE-5578775; Ion homeostasis.
DR Reactome; R-DRE-5673000; RAF activation.
DR Reactome; R-DRE-5673001; RAF/MAP kinase cascade.
DR Reactome; R-DRE-877300; Interferon gamma signaling.
DR Reactome; R-DRE-936837; Ion transport by P-type ATPases.
DR PRO; PR:Q6DGS3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IBA:GO_Central.
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 Alternative splicing; ATP-binding; Calmodulin-binding; Kinase;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..554
FT /note="Calcium/calmodulin-dependent protein kinase type II
FT delta 2 chain"
FT /id="PRO_0000277821"
FT DOMAIN 13..271
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 324..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 318
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 372
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 329..348
FT /note="Missing (in isoform E)"
FT /evidence="ECO:0000303|PubMed:17103413, ECO:0000303|Ref.1"
FT /id="VSP_035556"
FT VAR_SEQ 379..419
FT /note="Missing (in isoform A and isoform E)"
FT /evidence="ECO:0000303|PubMed:17103413, ECO:0000303|Ref.1"
FT /id="VSP_035557"
FT CONFLICT 266
FT /note="P -> L (in Ref. 1; AAI54769)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 554 AA; 62384 MW; 2CC541C7B3C02832 CRC64;
MALTICTRFT DEYQLFEELG KGAFSVVRRC VKISSGQEYA AKIINTKKLS ARDHQKLERE
ARICRLLKHP NIVRLHDSIS EEGFHYLVFD LVTGGELFED IVAREYYSEA DASHCIQQIL
ESVHHCHVNG IVHRDLKPEN LLLASKMKGA AVKLADFGLA IEVQGDQQAW FGFAGTPGYL
SPEVLRKDPY GKPVDMWACG VILYILLVGY PPFWDEDQHR LYQQIKAGAY DFPSPEWDTV
TPEAKDLINK MLTINPSKRI TAAEAPKHPW ICQRSTVASM MHRQETVECL KKFNARRKLK
GAILTTLLVT RNFSAAKSLL NKKPDGVKVN NKTNLASSPK DTGPAPALEP QTTVIHNPVD
RNKESTESAN TTIEDEDLKA RRFGNLSINS IWQPSVGRPQ NSEPKQAPNS SVQTCQVINK
ARKQEIIKVT EQLIESINNG DFEAYAKICD PGLTSFEPEA LGNLVEGHDF HRFYFENALS
KGNKPVHTIL LNPHVHLIGE DAACIAYIRL TQYMDGSGMP RTMQSEETRV WHRRDGKWLN
IHFHRSGAPS VPIN
