GWL_BOVIN
ID GWL_BOVIN Reviewed; 883 AA.
AC E1BFR5;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 61.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=19390049; DOI=10.1126/science.1169588;
RG The bovine genome sequencing and analysis consortium;
RT "The genome sequence of taurine cattle: a window to ruminant biology and
RT evolution.";
RL Science 324:522-528(2009).
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 62' and 'Ser-67', respectively. ARPP19 and ENSA are phosphatase
CC inhibitors that specifically inhibit the PPP2R2D (PR55-delta) subunit
CC of PP2A. Inactivation of PP2A during M phase is essential to keep
CC cyclin-B1-CDK1 activity high. Following DNA damage, it is also involved
CC in checkpoint recovery by being inhibited (By similarity).
CC {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-745 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; AAFC03049560; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; E1BFR5; -.
DR SMR; E1BFR5; -.
DR STRING; 9913.ENSBTAP00000022950; -.
DR PaxDb; E1BFR5; -.
DR eggNOG; KOG0606; Eukaryota.
DR HOGENOM; CLU_016048_0_0_1; -.
DR InParanoid; E1BFR5; -.
DR OrthoDB; 878671at2759; -.
DR Proteomes; UP000009136; 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 3: Inferred from homology;
KW Acetylation; ATP-binding; Cell cycle; Cell division; Cytoplasm;
KW Cytoskeleton; Kinase; Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..883
FT /note="Serine/threonine-protein kinase greatwall"
FT /id="PRO_0000408314"
FT DOMAIN 35..839
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 840..883
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 298..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 511..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 706..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..724
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 41..49
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 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q96GX5"
FT MOD_RES 209
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96GX5"
FT MOD_RES 224
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96GX5"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96GX5"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96GX5"
FT MOD_RES 456
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96GX5"
FT MOD_RES 523
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96GX5"
FT MOD_RES 556
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96GX5"
FT MOD_RES 560
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96GX5"
FT MOD_RES 635
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96GX5"
FT MOD_RES 661
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96GX5"
FT MOD_RES 672
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96GX5"
FT MOD_RES 726
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96GX5"
FT MOD_RES 729
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96GX5"
FT MOD_RES 745
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:Q96GX5"
FT MOD_RES 879
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96GX5"
FT MOD_RES 882
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96GX5"
SQ SEQUENCE 883 AA; 98072 MW; DCBA21113836A6A6 CRC64;
MEPTMGGEME SGGGAATGEC VNRIPVPRPP SIEEFTIVKP ISRGAFGKVY LGQKGNRLYA
VKVVKKADMI NKNMTHQVQA ERDALALSKS PFIVHLYYSL QSANNVYLVM EYLIGGDVKS
LLHIYGYFDE EMAVKYISEV ALALDYLHRH GIIHRDLKPD NMLISNEGHI KLTDFGLSKV
TLNRDIDINM MDILTTPSMA KPRQDYSRTP GQVLSLISSL GFHTPVAEGN HDTANVLSTQ
VSETSPLSQG LTCPMSVDQK DTTPYSSKLL KSCPEMVASH PRMPVKCLTS HLLQSRKRLA
TSSTSSPSHT FISSMESECH SSPRWEKDCQ ESDDAAGSTM MSWNTVEKPL CTKSVDAMET
KSFNERDLEL ALSPIHNSSV VPATGNSYVN LAKKCSSGEV SWEARELDVN NINMTADTSQ
YCFHESNQRA VDSGGMTEEH LGKRSCKRIF ELVDSSPRQG IIPNKKSCFE YECSNEMRDC
YATQRTGFAF EVQDLKLLVY RDQQNDCVNK ENVGSSFTDK HQTPEKSPVP MIEKNLMCEL
DDDCDKNSKK DYLSSSFLCS DGDRTPKSIH MDSDSSFPGI SIMESPLGGQ SLDPDKNIKE
SSLEESNIED LLPVSPSCQE STLPKGVECP TIQDSNQKML APSSEVLKPL TSKRNAVAFR
SFNSHINASN SSEPSKMSIT SLDMMDVSCA YSGSYPTAIT PTQRERSDMP YQQTPNQVKS
ETPYRTPKSV RRGAAPVDDG RILGTPDYLA PELLLARAHG PAVDWWALGV CLFEFLTGIP
PFNDETPQQV FQNILKRDIP WPEGEEKLSD NAQSAVDILL TIDDTKRAGM KELKHHPLFS
GVDWENLQHQ KMPFIPQPDD ETDTSYFEAR NNAQHLTVSG FSL
