ID   MAST3_XENLA             Reviewed;        1482 AA.
AC   Q6AX33;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Microtubule-associated serine/threonine-protein kinase 3;
DE            EC=2.7.11.1;
GN   Name=mast3;
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=Eye;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. {ECO:0000305}.
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DR   EMBL; BC079780; AAH79780.1; -; mRNA.
DR   RefSeq; NP_001087433.1; NM_001093964.1.
DR   AlphaFoldDB; Q6AX33; -.
DR   SMR; Q6AX33; -.
DR   GeneID; 447257; -.
DR   KEGG; xla:447257; -.
DR   CTD; 447257; -.
DR   Xenbase; XB-GENE-5928389; mast3.L.
DR   OrthoDB; 323328at2759; -.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 447257; Expressed in blastula and 18 other tissues.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
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:0006468; P:protein phosphorylation; IEA:InterPro.
DR   CDD; cd05609; STKc_MAST; 1.
DR   Gene3D; 1.20.1480.20; -; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR015022; MA_Ser/Thr_Kinase_dom.
DR   InterPro; IPR037711; MAST.
DR   InterPro; IPR023142; MAST_pre-PK_dom_sf.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR041489; PDZ_6.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF08926; DUF1908; 1.
DR   Pfam; PF17820; PDZ_6; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF140482; SSF140482; 1.
DR   SUPFAM; SSF50156; SSF50156; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Magnesium; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..1482
FT                   /note="Microtubule-associated serine/threonine-protein
FT                   kinase 3"
FT                   /id="PRO_0000277824"
FT   DOMAIN          399..672
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          673..745
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT   DOMAIN          968..1058
FT                   /note="PDZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   REGION          1..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          116..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          163..191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          755..810
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          830..915
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          936..965
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1061..1266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1449..1482
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..87
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        118..143
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        163..178
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        759..789
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        790..810
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        832..846
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        861..883
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        891..905
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        936..964
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1072..1088
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1099..1139
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1153..1184
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1205..1227
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1245..1260
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        522
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         405..413
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         428
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   1482 AA;  164805 MW;  7B29CCB04489E8F8 CRC64;
     MKSRRDKLKI PSLTLDLSPN NQSPTLLSPC SPCSPNSPLQ TLHPWSCRSS NRKSLVVGSP
     SPTLSRPLSP LSVPTAGSSP LDSPRNFSTS ASVNFPFARS HGPRADRADG RRWSLASLPS
     SGYGTNTPSS TLSSSSSSQE RLHQLPFQPT ADELHFLSKH FRSTESVTDD DGRRSPCMRP
     RSRSLSPGRA SSNFDNEIIM MNHVYKERFP KATAQMEERL QDIITHFCPS QTLPLADGVL
     GFIHHQIIEL ARDCLDKSKG ALITSRYFLE LQEKLEKMLQ DAHNRSESEE VMFINHLARK
     LLMVIARPGR LLECLEFDPE QFYHLLEAAE GQAKVGQGIK TDIPRYIISQ LGLTKDPLEE
     IVQLDHYDTE SSLQLDQEDY HDPYIPSTPS RKKPCESDFE TIKLISNGAY GAVYLVRHKE
     TRQRFAMKKI NKQNLILRNQ IHQVFVERDI LTFAENPFVV SMFCSFETRR HLCMVMEYVE
     GGDCATLLKN MGPLPVDMSR MYFAETVLAL EYLHNYGIVH RDLKPDNLLI TSLGHIKLTD
     FGLSKVGLMN MTTNLYEGHI EKDTREFLDK QVCGTPEYIA PEVILRQGYG KPVDWWAMGI
     ILYEFLVGCV PFFGDTPEEL FGQVISDDII WPGGEEALPA DSQDLITRLL RQNSLERLGT
     GGAQEVKQHT FFLSLDWNGL LRQKAEFVPQ LEADDDTSYF DTRSERYHHL ASEEDEETND
     DESSVEIRQF SSCSHRFSKV YSSSEHLATQ LNLSFSSTER SHSDEKEEHG DRWERTLSTE
     EEKNRLGAET RLRSWTSSGS SHHSWLSERS ASPNVLTSTC SLDTMPRFAF SSEEESSDHK
     PERPTFTLGE IKGTPPKPTS LCDIVSLSRT RLRSNSTGAK NSTPRPLEAG VSRRLRGHRE
     TPEKQSSSTG SRVPKSASVS ALSLIITSDD FGSGSLASPI SPRSLSSNPS SRDSSPSRES
     SVAVSSLRPP IIIHSSGKKY GFTLRAIRVY MGESDVYTVH HMVWNVEDGS PAHEAGLRAG
     DLITHVNGES VLGLVHMDVV ELLLKSGSKV SLRTTPLENT SIKIGPARKN SCKGRMARRT
     KKSRKRENQD RKRSLFKKIS KQSTVLQTSR SFSSGLHQSL SSSESLPASP THSLSPGPIT
     PSRSPAPDAA GDAVSPQSTS PCSSTPSSPA GHIRPSSLQC LTPKLSGQRY KVGRRKSTSS
     IPPSPLACTP SPVPQQPSSP QRSPSPLLPS HPRSGHCGLQ GKTLSPPTIV RQSSRNRATE
     APRSPLLKRV QSVEKMAAYL SSGRKASPVD IQHWEDTVDA LEAMSESRNR DWGAEKHERD
     TEVVVMRRLN LSERRDSFKK QEAVQEVSFD EPDAGAVELV PEDKKTARCS GLWERLPHQT
     SWIQARTGIS TPVTTEQETS CRLVPQIAVQ TSESDEQEKS QGVWECQGFY PLQLSGKDKC
     PLVTLLSEPT GATSDRSQLK SEKISECPAP FALSSKRDSK KN