ST17B_RAT
ID ST17B_RAT Reviewed; 371 AA.
AC Q91XS8;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Serine/threonine-protein kinase 17B;
DE EC=2.7.11.1;
DE AltName: Full=DAP kinase-related apoptosis-inducing protein kinase 2;
GN Name=Stk17b; Synonyms=Drak2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000312|EMBL:BAB63368.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH CHP1, TISSUE
RP SPECIFICITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-62.
RC TISSUE=Brain {ECO:0000312|EMBL:BAB63368.1};
RX PubMed=11481038; DOI=10.1093/oxfordjournals.jbchem.a002975;
RA Matsumoto M., Miyake Y., Nagita M., Inoue H., Shitakubo D., Takemoto K.,
RA Ohtsuka C., Murakami H., Nakamura N., Kanazawa H.;
RT "A serine/threonine kinase which causes apoptosis-like cell death interacts
RT with a calcineurin B-like protein capable of binding Na+/H+ exchanger.";
RL J. Biochem. 130:217-225(2001).
RN [2]
RP FUNCTION AS A MYOSIN LIGHT CHAIN KINASE, AUTOPHOSPHORYLATION, AND
RP MUTAGENESIS OF LYS-62.
RX PubMed=12966074; DOI=10.1093/jb/mvg137;
RA Kuwahara H., Kamei J., Nakamura N., Matsumoto M., Inoue H., Kanazawa H.;
RT "The apoptosis-inducing protein kinase DRAK2 is inhibited in a calcium-
RT dependent manner by the calcium-binding protein CHP.";
RL J. Biochem. 134:245-250(2003).
CC -!- FUNCTION: Acts as a positive regulator of apoptosis. Phosphorylates
CC myosin light chains. {ECO:0000269|PubMed:11481038,
CC ECO:0000269|PubMed:12966074}.
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:11481038};
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:11481038};
CC -!- SUBUNIT: Interacts with CHP1; the interaction induces CHP1 to
CC translocate from the Golgi to the nucleus.
CC {ECO:0000269|PubMed:11481038}.
CC -!- INTERACTION:
CC Q91XS8; P61023: Chp1; NbExp=6; IntAct=EBI-77460, EBI-917838;
CC Q91XS8; Q9Z1Y0: Rhov; NbExp=2; IntAct=EBI-77460, EBI-77480;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11481038}. Cell
CC membrane {ECO:0000269|PubMed:11481038}. Endoplasmic reticulum-Golgi
CC intermediate compartment {ECO:0000269|PubMed:11481038}.
CC Note=Colocalizes with STK17B at the plasma membrane.
CC -!- TISSUE SPECIFICITY: Highly expressed in thymus, spleen, and testis,
CC lower levels present in the brain. {ECO:0000269|PubMed:11481038}.
CC -!- PTM: Autophosphorylated.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. DAP kinase subfamily. {ECO:0000305}.
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DR EMBL; AB070349; BAB63368.1; -; mRNA.
DR PIR; JC7733; JC7733.
DR RefSeq; NP_596883.1; NM_133392.1.
DR RefSeq; XP_006244970.1; XM_006244908.2.
DR AlphaFoldDB; Q91XS8; -.
DR SMR; Q91XS8; -.
DR IntAct; Q91XS8; 2.
DR STRING; 10116.ENSRNOP00000016857; -.
DR iPTMnet; Q91XS8; -.
DR PhosphoSitePlus; Q91XS8; -.
DR PaxDb; Q91XS8; -.
DR Ensembl; ENSRNOT00000016856; ENSRNOP00000016857; ENSRNOG00000012502.
DR GeneID; 170904; -.
DR KEGG; rno:170904; -.
DR UCSC; RGD:620457; rat.
DR CTD; 9262; -.
DR RGD; 620457; Stk17b.
DR eggNOG; KOG0032; Eukaryota.
DR GeneTree; ENSGT00940000154014; -.
DR HOGENOM; CLU_000288_63_0_1; -.
DR InParanoid; Q91XS8; -.
DR OMA; FYMLESK; -.
DR OrthoDB; 1156450at2759; -.
DR PhylomeDB; Q91XS8; -.
DR TreeFam; TF314166; -.
DR PRO; PR:Q91XS8; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000012502; Expressed in thymus and 20 other tissues.
DR Genevisible; Q91XS8; RN.
DR GO; GO:0015629; C:actin cytoskeleton; IMP:UniProtKB.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; 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:0006915; P:apoptotic process; IMP:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IDA:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:2000271; P:positive regulation of fibroblast apoptotic process; ISS:UniProtKB.
DR GO; GO:0012501; P:programmed cell death; IDA:RGD.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR CDD; cd14198; STKc_DRAK2; 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; IPR042763; ST17B_STKc.
DR Pfam; PF00069; Pkinase; 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.
PE 1: Evidence at protein level;
KW Apoptosis; ATP-binding; Cell membrane; Kinase; Membrane;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..371
FT /note="Serine/threonine-protein kinase 17B"
FT /id="PRO_0000086708"
FT DOMAIN 33..293
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 308..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 158
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 39..47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 62
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MUTAGEN 62
FT /note="K->A: Inhibits kinase activity."
FT /evidence="ECO:0000269|PubMed:11481038,
FT ECO:0000269|PubMed:12966074"
SQ SEQUENCE 371 AA; 42133 MW; 7BD4E83D98896F4F CRC64;
MSRRRFDCRS ISGLLTTTPQ TPMKTENFNN FYTLTPKELG RGKFAVVRQC ISKSTGQEYA
AKFLKKRRRG QDCRAEILHE IAVLELARSC PHVINLHEVY ETATEIILVL EYAAGGEIFN
LCLPELAEMV SENDVIRLIK QILEGVHYLH QNNIVHLDLK PQNILLSSIY PLGDIKIVDF
GMSRKIGNAS ELREIMGTPE YLAPEILNYD PITTATDMWN IGIIAYMLLT HTSPFVGEDN
QETYLNISQV NVDYSEEMFS SVSQLATDFI QSLLVKNPEK RPTAESCLSH SWLQQWDFGS
LFHPEETSES SQTQDLSLRS SEDKTPKSCN GSCGDREDKE NIPEDDSLLS KRFRFDDSLP
SPHELVPDLF C
