KC2D1_DANRE
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 03-AUG-2022, entry version 140.
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
RC Olfactory epithelium {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 -!- 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}.
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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.ENSDARP00000056465; -.
DR PaxDb; Q6DEH3; -.
DR PRIDE; Q6DEH3; -.
DR Ensembl; ENSDART00000142259; ENSDARP00000119349; ENSDARG00000043010. [Q6DEH3-2]
DR Ensembl; ENSDART00000166198; ENSDARP00000131013; ENSDARG00000043010. [Q6DEH3-1]
DR GeneID; 445208; -.
DR KEGG; dre:445208; -.
DR CTD; 445208; -.
DR ZFIN; ZDB-GENE-040801-121; camk2d1.
DR eggNOG; KOG0033; Eukaryota.
DR GeneTree; ENSGT00940000155150; -.
DR HOGENOM; CLU_000288_71_3_1; -.
DR InParanoid; Q6DEH3; -.
DR OrthoDB; 330091at2759; -.
DR PhylomeDB; Q6DEH3; -.
DR TreeFam; TF315229; -.
DR PRO; PR:Q6DEH3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 7.
DR Bgee; ENSDARG00000043010; Expressed in zone of skin and 32 other 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: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..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
