SIK3_DANRE
ID SIK3_DANRE Reviewed; 1187 AA.
AC Q6NSM8; Q6PHV1;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Serine/threonine-protein kinase SIK3 homolog;
DE EC=2.7.11.1;
DE AltName: Full=Serine/threonine-protein kinase QSK homolog;
GN ORFNames=zgc:66101;
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].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
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=2.7.11.1;
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=2.7.11.1;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. SNF1 subfamily. {ECO:0000305}.
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DR EMBL; BC056316; AAH56316.1; -; mRNA.
DR EMBL; BC070022; AAH70022.1; -; mRNA.
DR RefSeq; NP_956835.1; NM_200541.1.
DR AlphaFoldDB; Q6NSM8; -.
DR SMR; Q6NSM8; -.
DR PaxDb; Q6NSM8; -.
DR PRIDE; Q6NSM8; -.
DR GeneID; 393513; -.
DR KEGG; dre:393513; -.
DR CTD; 23387; -.
DR ZFIN; ZDB-GENE-140106-203; sik3.
DR eggNOG; KOG0586; Eukaryota.
DR InParanoid; Q6NSM8; -.
DR OrthoDB; 1127668at2759; -.
DR PhylomeDB; Q6NSM8; -.
DR PRO; PR:Q6NSM8; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0050321; F:tau-protein kinase activity; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR CDD; cd14071; STKc_SIK; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR034672; SIK.
DR InterPro; IPR015940; UBA.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00165; UBA; 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.
DR PROSITE; PS50030; UBA; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..1187
FT /note="Serine/threonine-protein kinase SIK3 homolog"
FT /id="PRO_0000252259"
FT DOMAIN 59..310
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 337..377
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1060..1092
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..753
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..776
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1073..1087
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 181
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 65..73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 88
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 214
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT CONFLICT 31
FT /note="Q -> QQQ (in Ref. 1; AAH56316)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="V -> G (in Ref. 1; AAH56316)"
FT /evidence="ECO:0000305"
FT CONFLICT 358
FT /note="Q -> H (in Ref. 1; AAH56316)"
FT /evidence="ECO:0000305"
FT CONFLICT 1021
FT /note="A -> T (in Ref. 1; AAH56316)"
FT /evidence="ECO:0000305"
FT CONFLICT 1080
FT /note="T -> A (in Ref. 1; AAH56316)"
FT /evidence="ECO:0000305"
FT CONFLICT 1148
FT /note="V -> A (in Ref. 1; AAH56316)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1187 AA; 130967 MW; 4B01A32E53F77176 CRC64;
MAAVSSGAAA AAGIPNPNPN RERPQQQQQQ QPASAALHPV AHRSAAAACR PPLARVGYYE
MERTIGKGNF AVVKLATHMI TKAKVAIKIV DKTQLDDENL KKIFREVQIM KMLRHPHIIR
LYQVMETERM IYLVTEYASG GEIFDHLVAH GRMAEKDARR KFKQIVAAVY FCHCRSIVHR
DLKAENLLLD HNLNIKIADF GFSNLFSRGQ LLKTWCGSPP YAAPELFEGK EYDGPKVDIW
SLGVVLYVLV CGALPFDGST LQNLRARVLS GKFRIPFFMS TDCEYLIRHM LILEPSRRLS
MEQICKNKWM RQGDPDPEFD RLIVECEQVK VERETELINE QVLMAMAEMG FDRERTLQSL
HADSYDHYSA TYSLLSDKLK RHKNLCVAPP TPRPLYPLQD QSNAVSMTVP QVQLINPENQ
IVETDGPMAL DSDEGEEPSP EAMARYLSMR RHTVGVPDPR AEMQEDLQKL APGFPRVAPQ
APFPPLMPAL AQMQLMPTPS LQPGQQLEYK EQSLLQPPTL QLLNGMGPLG RRASDGGANI
QLHTQQLLKR PRGQSPLVTS PHPIPAVAPV DEEGSDAEPD PEAVQRSSYK DCNTLHLPME
RFSPVRRFSD GAATIQAYKT QLENNSLIRQ LKQECEQLQK MYAAPQDERL MEHTQQQHVL
YQQEQQILHQ QIQALSLGHG ENQPSSHLTY QLQRLRIQPS SPPPTHPSNH LFRPANQSSP
PPPGGGAGLM QTHGGPSAVQ YQHGSALYQS PSDSPPPTSL PRMALANQQP SVPPGSARTL
AQTLPQQQVT IQVQEVELGG GAQRQSFLAT PCHRVLGKQL SADNAETHSR SLSRFHTSAY
EQLTAQLLGE SVMGSYNPYL QGASLKVPGL EGYGLSYGGP SALQQALLSP TPLEYRPPPQ
VTPTLQGLLS PRHSLTGHAD PRLPPQELAA LLKRHSRPAP PTAPPTIPQD YGEMLLLQQL
GQAAESLDSA PPQATPTQHY HHLLQIRTPP ECPAPSLPHS ESMEEDEMPA YHEGLLAKAA
APCTEAHELL APPLGSTPPY SSPTHRHAYL RSATATRESC ADAADAGMES DHNGYGSRST
QSDSYRPRGA LQRHHTIQTC DDAYEQVEPM SGMSLLAGKA LSSARMSDIL SQSSLTGSQQ
LQQREGPVCD VDADVHSSSC YPSSCTTDML LSYKTPDLQY SVEQAGV
