GWL_XENTR
ID GWL_XENTR Reviewed; 890 AA.
AC B1WAR9;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Serine/threonine-protein kinase greatwall;
DE Short=GW;
DE Short=GWL;
DE EC=2.7.11.1;
DE AltName: Full=Microtubule-associated serine/threonine-protein kinase-like;
DE Short=MAST-L;
GN Name=mastl; Synonyms=gw, gwl;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Serine/threonine kinase that plays a key role in M phase by
CC acting as a regulator of mitosis entry and maintenance. Acts by
CC promoting the inactivation of protein phosphatase 2A (PP2A) during M
CC phase: does not directly inhibit PP2A but acts by mediating
CC phosphorylation and subsequent activation of arpp19 and ensa at 'Ser-
CC 67', 2 phosphatase inhibitors that specifically inhibit the ppp2r2d
CC (PR55-delta) subunit of PP2A. Inactivation of PP2A during M phase is
CC essential to keep cyclin-B1-CDK1 activity high. Following DNA damage,
CC it is also involved in checkpoint recovery by being inhibited (By
CC similarity). {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250}. Nucleus. Note=During interphase is
CC mainly nuclear, upon nuclear envelope breakdown localizes at the
CC cytoplasm and during mitosis at the centrosomes. {ECO:0000250}.
CC -!- PTM: Phosphorylation at Thr-752 by CDK1 during M phase activates its
CC kinase activity. Maximum phosphorylation occurs in prometaphase (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; BC161476; AAI61476.1; -; mRNA.
DR RefSeq; NP_001120546.1; NM_001127074.1.
DR AlphaFoldDB; B1WAR9; -.
DR SMR; B1WAR9; -.
DR STRING; 8364.ENSXETP00000040639; -.
DR PaxDb; B1WAR9; -.
DR GeneID; 100145700; -.
DR KEGG; xtr:100145700; -.
DR CTD; 84930; -.
DR Xenbase; XB-GENE-964548; mastl.
DR eggNOG; KOG0606; Eukaryota.
DR InParanoid; B1WAR9; -.
DR OrthoDB; 878671at2759; -.
DR Reactome; R-XTR-2465910; MASTL Facilitates Mitotic Progression.
DR Proteomes; UP000008143; Chromosome 6.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0032154; C:cleavage furrow; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0051721; F:protein phosphatase 2A 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:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0032515; P:negative regulation of phosphoprotein phosphatase activity; ISS:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR CDD; cd05610; STKc_MASTL; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR037638; MASTL_STKc.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Kinase;
KW Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..890
FT /note="Serine/threonine-protein kinase greatwall"
FT /id="PRO_0000408319"
FT DOMAIN 33..846
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 847..890
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 324..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..592
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 156
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 MOD_RES 752
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 890 AA; 98557 MW; BE52901D415DFCF8 CRC64;
MGVVVAETSQ NGDISLLSEK KFTVPQPPSI EEFSIVKPIS RGAFGKVYLA RRKNNNKLFA
VKVVKKADMI NKNMVQQVQA ERDALALSKS PFIVHLYYSL QSANNIYLIM EYLIGGDVKS
LLHIYGYFDE EMAVKYISEV ALALDYLHRH GIIHRDLKPD NMLISNEGHI KLTDFGLSKV
TLKRELSMMD ILTTPSMAKP KRDYSRTPGQ VLSLISSLGF NTPVGGRTQG SIAQQTEGMR
GNASTPLLMK KKENSVKGNK LMISCPEAGL SSPSMPVKCL TPNLLKCRTP FTTSSTSSQS
RICLSSLESE CGMSPRWENC SQDAEAPPYL NSSRVKDCSS EQARSKKPMG SSASQNLKHL
EFAFSPIVDR RTGKKAGFQD ETGELSDTPL ATLGAKGVIR KCLYDNNAQE KHKDLGKDDQ
GELEKLTISP DSPPWLANGS VAPIQFNDDE IIEKMGIKRN YDLVEKSPEQ EVLQDKKTNT
DYKRGCTITG YPVSQSTGLT MEINSLFLSE LRSSTNNYAS DRKSEDDYIS APRTHENLGS
GNTIAKNLLC ELDDNCERDG EANSNSGCEE GENQKESLNQ DSESSSADMS VTENQIEREL
CQVDKSIKEL SFEESPSESN EETTPENKGM AFMAENDALK REPNRSVLPE TLHNVLASPA
PTSAMAHPRR KPMVAFRSYN SPINGSNLSE PSRISMNSAD KIHFSLGCTG SFPMAVTPAQ
KKVQGLTETP YRTPKTVRRG GLQAENERIL GTPDYLAPEL LLGKSHGPAV DWWALGVCLF
EFLTGIPPFN DETPSQVFQN ILNRDIPWPE EEETLSVNAQ SAIEILLAID QTKRAGLKDL
KAHHLFHAIE WDDLQNLPMP FIPQPDDETD TTYFEARNNA QHLKVSGFSL
