ID F1QGL7_DANRE Unreviewed; 554 AA.
AC F1QGL7; A0A8M3AYA9;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 2.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=calcium/calmodulin-dependent protein kinase {ECO:0000256|ARBA:ARBA00012434};
DE EC=2.7.11.17 {ECO:0000256|ARBA:ARBA00012434};
GN Name=camk2d2 {ECO:0000313|Ensembl:ENSDARP00000044895,
GN ECO:0000313|RefSeq:XP_009304932.1,
GN ECO:0000313|ZFIN:ZDB-GENE-040718-277};
GN Synonyms=camk2d {ECO:0000313|RefSeq:XP_009304932.1}, camk2da
GN {ECO:0000313|RefSeq:XP_009304932.1}, wu:fq17a12
GN {ECO:0000313|RefSeq:XP_009304932.1}, zgc:92792
GN {ECO:0000313|RefSeq:XP_009304932.1};
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 {ECO:0000313|Ensembl:ENSDARP00000044895};
RN [1] {ECO:0000313|Ensembl:ENSDARP00000044895}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000044895};
RG Ensembl;
RL Submitted (JUL-2011) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSDARP00000044895, ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000044895};
RX PubMed=23594743; DOI=10.1038/nature12111;
RG Genome Reference Consortium Zebrafish;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3] {ECO:0000313|RefSeq:XP_009304932.1}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:XP_009304932.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00000902};
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:0000256|ARBA:ARBA00000517};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. CaMK subfamily. {ECO:0000256|ARBA:ARBA00005354}.
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DR EMBL; CR388002; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT826376; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_009304932.1; XM_009306657.3.
DR Ensembl; ENSDART00000044896; ENSDARP00000044895; ENSDARG00000014273.
DR Ensembl; ENSDART00000044896.9; ENSDARP00000044895.7; ENSDARG00000014273.11.
DR GeneID; 436815; -.
DR AGR; ZFIN:ZDB-GENE-040718-277; -.
DR CTD; 436815; -.
DR ZFIN; ZDB-GENE-040718-277; camk2d2.
DR OMA; HPNIXVT; -.
DR OrthoDB; 1121238at2759; -.
DR TreeFam; TF315229; -.
DR Proteomes; UP000000437; Chromosome 1.
DR Bgee; ENSDARG00000014273; Expressed in cardiac ventricle and 23 other cell types or tissues.
DR GO; GO:0043226; C:organelle; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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: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:SF365; CALCIUM_CALMODULIN-DEPENDENT PROTEIN KINASE TYPE II SUBUNIT DELTA; 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 1: Evidence at protein level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW Kinase {ECO:0000313|RefSeq:XP_009304932.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Proteomics identification {ECO:0007829|PeptideAtlas:F1QGL7};
KW Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW Transferase {ECO:0000313|RefSeq:XP_009304932.1}.
FT DOMAIN 13..271
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
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 BINDING 42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 554 AA; 62414 MW; 2FB05592F85E51DE 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 TAAEALKHPW 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 VPIK
//
