STK3_XENLA
ID STK3_XENLA Reviewed; 493 AA.
AC Q6IP06;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Serine/threonine-protein kinase 3;
DE EC=2.7.11.1;
DE Contains:
DE RecName: Full=Serine/threonine-protein kinase 3 36kDa subunit;
DE Short=MST2/N;
DE Contains:
DE RecName: Full=Serine/threonine-protein kinase 3 20kDa subunit;
DE Short=MST2/C;
GN Name=stk3;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Stress-activated, pro-apoptotic kinase which, following
CC caspase-cleavage, enters the nucleus and induces chromatin condensation
CC followed by internucleosomal DNA fragmentation. Key component of the
CC Hippo signaling pathway which plays a pivotal role in organ size
CC control and tumor suppression by restricting proliferation and
CC promoting apoptosis. The core of this pathway is composed of a kinase
CC cascade wherein stk3/mst2 and stk4/mst1, in complex with its regulatory
CC protein sav1, phosphorylates and activates lats1/2 in complex with its
CC regulatory protein mob1, which in turn phosphorylates and inactivates
CC yap1 oncoprotein and wwtr1/taz. Phosphorylation of yap1 by lats2
CC inhibits its translocation into the nucleus to regulate cellular genes
CC important for cell proliferation, cell death, and cell migration.
CC {ECO:0000250|UniProtKB:Q13188}.
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 -!- ACTIVITY REGULATION: Inhibited by the C-terminal non-catalytic region.
CC Activated by caspase-cleavage. Full activation also requires
CC homodimerization and autophosphorylation of Thr-179 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homodimer; mediated via the coiled-coil region. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13188}. Nucleus
CC {ECO:0000250|UniProtKB:Q13188}. Note=The caspase-cleaved form cycles
CC between nucleus and cytoplasm. {ECO:0000250|UniProtKB:Q13188}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC072113; AAH72113.1; -; mRNA.
DR RefSeq; NP_001085133.1; NM_001091664.1.
DR AlphaFoldDB; Q6IP06; -.
DR SMR; Q6IP06; -.
DR MaxQB; Q6IP06; -.
DR DNASU; 432210; -.
DR GeneID; 432210; -.
DR KEGG; xla:432210; -.
DR CTD; 432210; -.
DR Xenbase; XB-GENE-960737; stk3.S.
DR OMA; QRMANLD; -.
DR OrthoDB; 967913at2759; -.
DR Proteomes; UP000186698; Chromosome 6S.
DR Bgee; 432210; Expressed in blastula and 18 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; ISS:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0035329; P:hippo signaling; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0051262; P:protein tetramerization; IEA:InterPro.
DR Gene3D; 4.10.170.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR024205; Mst1_SARAH_domain.
DR InterPro; IPR036674; p53_tetramer_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR011524; SARAH_dom.
DR Pfam; PF11629; Mst1_SARAH; 1.
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; PS50951; SARAH; 1.
PE 2: Evidence at transcript level;
KW Apoptosis; ATP-binding; Coiled coil; Cytoplasm; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..493
FT /note="Serine/threonine-protein kinase 3"
FT /id="PRO_0000247766"
FT CHAIN 1..321
FT /note="Serine/threonine-protein kinase 3 36kDa subunit"
FT /id="PRO_0000413721"
FT CHAIN 322..493
FT /note="Serine/threonine-protein kinase 3 20kDa subunit"
FT /id="PRO_0000413722"
FT DOMAIN 26..277
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 439..486
FT /note="SARAH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00310"
FT REGION 303..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 286..327
FT /evidence="ECO:0000255"
FT COILED 444..477
FT /evidence="ECO:0000255"
FT COMPBIAS 398..414
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 145
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 32..40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT SITE 321..322
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000250"
FT MOD_RES 179
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 493 AA; 56505 MW; 03AA1935ECEBE72F CRC64;
MEQPAPKSKL KKLSEDSLTK QPEEVFDVLE KLGEGSYGSV FKAIHKESGQ VVAIKQVPVE
SDLQEIIKEI SIMQQCDSHY VVKYYGSYFK NTDLWIVMEY CGAGSVSDII RLRNKTLTED
EIATILRSTL KGLEYLHFMR KIHRDIKAGN ILLNTEGHAK LADFGVAGQL TDTMAKRNTV
IGTPFWMAPE VIQEIGYNCV ADIWSLGITS IEMAEGKPPY ADIHPMRAIF MIPTNPPPTF
RKPELWTDEF TDFVKKCLVK NPEQRATATQ LLQHPFIKNA KPVSILRDLI TEAMDIKAKR
HEELQRELEE EDENSEEDEL DSHTMVKTNS ESAGTMRAAS TMSEGAQTMI EHNSTMLESD
LGTMVINSDD EEEEEEEDGT MKRNATSPQG PRPSFMDYFD KQDSKNKPHD NCNQNLHEQY
HISKNVFPDN WKVPPDGDFD FLKNLSFEEL QMRLKALDPM MEREIEDLRQ RYNAKRQPIL
DAMDAKKRRQ QNF
