ID KC2D1_DANRE Reviewed; 491 AA. AC Q6DEH3; A8KBP0; DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot. DT 14-OCT-2008, sequence version 2. DT 27-MAR-2024, entry version 147. DE RecName: Full=Calcium/calmodulin-dependent protein kinase type II delta 1 chain {ECO:0000303|PubMed:17103413}; DE EC=2.7.11.17; DE AltName: Full=Calcium/calmodulin-dependent protein kinase type II delta-B chain; DE Short=CaM kinase II subunit delta-B; DE Short=CaM-kinase II delta-B chain; DE Short=CaMK-II subunit delta-B; GN Name=camk2d1 {ECO:0000303|PubMed:17103413}; GN Synonyms=camk2db {ECO:0000312|EMBL:AAH77143.1}; GN ORFNames=zgc:101001, zgc:173815; 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] {ECO:0000305, ECO:0000312|EMBL:AAH77143.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS E AND G). RC TISSUE=Embryo {ECO:0000312|EMBL:AAH77143.1}, and Olfactory epithelium RC {ECO:0000312|EMBL:AAI54190.1}; RG NIH - Zebrafish Gene Collection (ZGC) project; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [MRNA] OF 301-383 (ISOFORMS E AND G), 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|UniProtKB:Q13557, CC ECO:0000250|UniProtKB:Q6PHZ2}. 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:0000305}; 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:0000305}; CC -!- ACTIVITY REGULATION: Autophosphorylation of CAMK2 plays an important CC role in the regulation of the kinase activity. CC {ECO:0000250|UniProtKB:Q13557}. 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|UniProtKB:Q13557}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=E {ECO:0000269|PubMed:17103413}; CC IsoId=Q6DEH3-1; Sequence=Displayed; CC Name=G {ECO:0000269|PubMed:17103413}; CC IsoId=Q6DEH3-2; Sequence=VSP_035558; CC -!- TISSUE SPECIFICITY: First detected at the 18-somite stage where CC expression is restricted to somite boundaries. At 24 hpf, expression is CC elevated in epidermal tissue and in the hatching gland. After 24 hpf, CC expression dimishes, but persists at low levels along the dorsal trunk. CC At 48 hpf, expression is restricted at a low level to the forebrain. At CC 72 hpf, weak expression reappears along the entire dorsal trunk in CC discrete cell bodies. {ECO:0000269|PubMed:17103413}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr CC protein kinase family. CaMK subfamily. {ECO:0000255}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC077143; AAH77143.1; -; mRNA. DR EMBL; BC154189; AAI54190.1; -; mRNA. DR RefSeq; NP_001003602.1; NM_001003602.2. [Q6DEH3-2] DR RefSeq; NP_001108180.1; NM_001114708.2. [Q6DEH3-1] DR AlphaFoldDB; Q6DEH3; -. DR SMR; Q6DEH3; -. DR STRING; 7955.ENSDARP00000119349; -. DR PaxDb; 7955-ENSDARP00000056465; -. DR GeneID; 445208; -. DR KEGG; dre:445208; -. DR AGR; ZFIN:ZDB-GENE-040801-121; -. DR CTD; 445208; -. DR ZFIN; ZDB-GENE-040801-121; camk2d1. DR eggNOG; KOG0033; Eukaryota. DR HOGENOM; CLU_000288_71_3_1; -. DR InParanoid; Q6DEH3; -. DR OMA; QGVAHTH; -. DR OrthoDB; 1121238at2759; -. DR PhylomeDB; Q6DEH3; -. DR TreeFam; TF315229; -. DR PRO; PR:Q6DEH3; -. DR Proteomes; UP000000437; Chromosome 7. DR Bgee; ENSDARG00000043010; Expressed in zone of skin and 32 other cell types or tissues. DR ExpressionAtlas; Q6DEH3; baseline and differential. 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:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd14086; STKc_CaMKII; 1. DR Gene3D; 3.10.450.50; -; 1. DR Gene3D; 6.10.140.620; -; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. 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 PANTHER; PTHR24347:SF431; CALCIUM_CALMODULIN-DEPENDENT PROTEIN KINASE TYPE II DELTA 1 CHAIN; 1. DR PANTHER; PTHR24347; SERINE/THREONINE-PROTEIN KINASE; 1. DR Pfam; PF08332; CaMKII_AD; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF54427; NTF2-like; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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..491 FT /note="Calcium/calmodulin-dependent protein kinase type II FT delta 1 chain" FT /id="PRO_0000296340" FT DOMAIN 13..271 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 315..354 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 330..346 FT /note="Polar 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|UniProtKB:Q6PHZ2" FT MOD_RES 314 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q13557" FT MOD_RES 350 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q6PHZ2" FT VAR_SEQ 326..340 FT /note="Missing (in isoform G)" FT /evidence="ECO:0000303|PubMed:17103413, ECO:0000303|Ref.1" FT /id="VSP_035558" SQ SEQUENCE 491 AA; 55829 MW; ADCFD717E279AF15 CRC64; MASTTCTRFT DEYQLYEELG KGAFSVVRRC MKISTGQEYA AKIINTKKLS ARDHQKLERE ARICRLLKHA NIVRLHDSIS EEGVHYLVFD LVTGGELFED IVAREYYSEA DASHCIQQIL EAVLHCHQMG VVHRDLKPEN LLLASKLKGA AVKLADFGLA IEVQGDQQAW FGFAGTPGYL SPEVLRKEPY GKPVDMWACG VILYILLVGY PPFWDEDQHR LYQQIKAGAY DFPSPEWDTV TPEAKDLINK MLTINPAKRI TAAEALKHPW ICQRSTVASM MHRQETVECL KKFNARRKLK GAILTTMLAT RNFSSKNPYK KPDGVKEPQT TVIHNPTDGN KESSESTNTT IEDEDIKARK QEIIKVTELL IEAINNGEFE AYTKICDPGL TSFEPEALGN LVEGTDFHRF YFENSLSKGH KPIHTILLNP HVHLIGEDAA CIAYIRLTQY MDVNNMPRTM QSEETRVWHR RDGKWQNIHF HRSGSPTVPT K //