SIK2_CHICK
ID SIK2_CHICK Reviewed; 798 AA.
AC Q9IA88;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Serine/threonine-protein kinase SIK2;
DE EC=2.7.11.1;
DE AltName: Full=Qin-induced kinase;
DE AltName: Full=Salt-inducible kinase 2;
DE Short=SIK-2;
DE AltName: Full=Serine/threonine-protein kinase SNF1-like kinase 2;
GN Name=SIK2; Synonyms=QIK, SNF1LK2;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAF28351.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=11027514; DOI=10.1006/bbrc.2000.3508;
RA Xia Y., Zhang Z., Kruse U., Vogt P.K., Li J.;
RT "The new serine-threonine kinase, Qik, is a target of the Qin oncogene.";
RL Biochem. Biophys. Res. Commun. 276:564-570(2000).
CC -!- FUNCTION: Phosphorylates IRS1 in insulin-stimulated adipocytes,
CC potentially modulating the efficiency of insulin signal transduction.
CC Inhibits CREB activity by phosphorylating and repressing the CREB-
CC specific coactivators, CRTC1-3 (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:11027514}.
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 Evidence={ECO:0000269|PubMed:11027514};
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; Evidence={ECO:0000269|PubMed:11027514};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:11027514};
CC -!- ACTIVITY REGULATION: Activated by phosphorylation on Thr-181.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11027514}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in embryonic tissue.
CC {ECO:0000269|PubMed:11027514}.
CC -!- PTM: Phosphorylated at Thr-181 by STK11/LKB1 in complex with STE20-
CC related adapter-alpha (STRADA) pseudo kinase and CAB39. {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; AF219232; AAF28351.1; -; mRNA.
DR PIR; JC7500; JC7500.
DR RefSeq; NP_990013.1; NM_204682.1.
DR AlphaFoldDB; Q9IA88; -.
DR SMR; Q9IA88; -.
DR STRING; 9031.ENSGALP00000026069; -.
DR PaxDb; Q9IA88; -.
DR GeneID; 395417; -.
DR KEGG; gga:395417; -.
DR CTD; 150094; -.
DR VEuPathDB; HostDB:geneid_395417; -.
DR eggNOG; KOG0586; Eukaryota.
DR InParanoid; Q9IA88; -.
DR OrthoDB; 1127668at2759; -.
DR PhylomeDB; Q9IA88; -.
DR PRO; PR:Q9IA88; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0050321; F:tau-protein kinase activity; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IDA:UniProtKB.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0046626; P:regulation of insulin receptor signaling pathway; 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; IPR017090; Ser/Thr_kinase_SIK1/2.
DR InterPro; IPR034672; SIK.
DR InterPro; IPR015940; UBA.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF037014; Ser/Thr_PK_SNF1-like; 1.
DR SMART; SM00220; S_TKc; 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; Cytoplasm; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..798
FT /note="Serine/threonine-protein kinase SIK2"
FT /id="PRO_0000086665"
FT DOMAIN 26..277
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 302..342
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT REGION 351..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 148
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q13131,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 32..40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13131,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9H0K1,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 181
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0K1"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 575
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 798 AA; 88866 MW; 31FE1AF0FAA136BE CRC64;
MVIMSEDASV PAPSAAQPRP LRVGFYDIER TLGKGNFAVV KLARHRVTKT QVAIKIIDKT
RLDPSNLEKI YREVQIMKLL NHPHIIKLYQ VMETKDMLYI VTEFAKNGEM FDHLTSNGHL
SESEARKKFW QILSAVEYCH SHHIVHRDLK TENLLLDANM NIKLADFGFG NFYKSGEPLS
TWCGSPPYAA PEVFEGKEYE GPHLDIWSLG VVLYVLVCGS LPFDGPNLPT LRQRVLEGRF
RIPYFMSEDC ETLIRRMLVV DPTKRITISQ IKQHKWMQAD PSLRQQQSLS FSMQNYNSNL
GDYNEQVLGI MQTLGIDRQR TVESLQNSSY NHFAAIYYLL LERLKEYRSS QLSSRPATGR
QQRPRSSEIS NAEMPQDSLT SETLRSSLLY QQPQSLIQPS LQAEMDCDMN NPLQPVFFPV
DPNFNGLFRN RSISPSSLLE TTISEEVRQE KELEDEIKAY DHPIRIPSNT SRRHTLAEVT
THFYQHAPPC IVISSSASPT EGTSSDSCLT SSSNDSSVAL SSCLAGQVMT GSPATARMTS
AFLASQSDAP VLQVQGCMGG ASLLPVSFQE GRRASDTSLT QGLKAFRQQL RKNARAKGFL
GLNKIKGFAR QVCQSSSSRA ARSAMSPFQH AQPNTCIYSS SGSSREGRNL LEEVLQQQRM
LQLQHHQLLQ PACPQTSQTS ATNGLPPSDS AGTCKASNSL LLSELQRENS FELAFGGNSQ
LLQPHFFGVS VSPVSSAAHL LDTHLYISSN VSPVGTTFSQ QQSFSAQSPS YDAVTLQHGD
CEMEDLTSNQ LGKFVLVK
