ID H2ML66_ORYLA Unreviewed; 1530 AA.
AC H2ML66;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=MAST1 {ECO:0000313|Ensembl:ENSORLP00000019439.3};
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000019439.3, ECO:0000313|Proteomes:UP000001038};
RN [1] {ECO:0000313|Ensembl:ENSORLP00000019439.3, ECO:0000313|Proteomes:UP000001038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000019439.3,
RC ECO:0000313|Proteomes:UP000001038};
RX PubMed=17554307; DOI=10.1038/nature05846;
RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT "The medaka draft genome and insights into vertebrate genome evolution.";
RL Nature 447:714-719(2007).
RN [2] {ECO:0000313|Ensembl:ENSORLP00000019439.3}
RP IDENTIFICATION.
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000019439.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00001433};
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:0000256|ARBA:ARBA00000775};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000256|ARBA:ARBA00009903}.
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DR STRING; 8090.ENSORLP00000019439; -.
DR Ensembl; ENSORLT00000019440.3; ENSORLP00000019439.3; ENSORLG00000015521.3.
DR eggNOG; KOG0606; Eukaryota.
DR GeneTree; ENSGT00940000157700; -.
DR HOGENOM; CLU_000288_9_0_1; -.
DR InParanoid; H2ML66; -.
DR TreeFam; TF313149; -.
DR Proteomes; UP000001038; Chromosome 8.
DR Bgee; ENSORLG00000015521; Expressed in bone element and 4 other cell types or tissues.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0007010; P:cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00992; PDZ_signaling; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 1.20.1480.20; MAST3 pre-PK domain-like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR015022; MAST_pre-PK_dom.
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 PANTHER; PTHR24356:SF150; MICROTUBULE-ASSOCIATED SERINE_THREONINE-PROTEIN KINASE 1; 1.
DR PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF08926; DUF1908; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF140482; MAST3 pre-PK domain-like; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001038};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 287..571
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 572..640
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 865..953
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 96..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 826..854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 961..1038
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1088..1147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1190..1530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 832..853
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..992
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 994..1038
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1107..1127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1204..1218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1219..1261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1286..1324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1325..1348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1405..1421
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1477..1491
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1530 AA; 168811 MW; 656CB5C7F326DBBF CRC64;
PTLPRPHSPL PLPGHLGSSP LDSPRNFSPS NPAHFSFASS RRADGRRWSL ASLPSSGYGT
NTPSSTSSSS SQERLHQLPF QPTMDELHFL SKHFGSTESI TDDDGGRCSP HMRPRSRSLS
PGRSSSCYDN EIVMMNHVYK ERFPKATAQM EERLAEFIQA FSPENVLPLA DGVLSFIHHQ
IAELARDCLT KSREGLITSV YFFELQENLE KLLQDAFERS ESSEVAFVTE LVKKLLIIIA
RPARLLECLE FNPEEFYHLL EAAEDHAKEG HLVKTDIPRY IISQLGLTRD PIEGENLRGK
LCTALKINEK DTFASSDLTK LAVYLVRHLE SQQRFAMKKI NKQNLILRNQ IQQAFVERDI
LTFAENPFVV SMFCSFETRR HLCMVMEYVE GKHLMICHNI KISRSSVDVS LARTLLSPIS
LTDSRLLLIT SIGHIKLTDF GLSKMGLMSL TTNLYEGHIE KDTREFLDKQ VCGTPEYIAP
EVILRQGYGK PVDWWAMGII LYEFLVGCVP FFGDTPEELF GQVITDDIEW PDEDDALPVD
VQHLISSLLQ RNPLARLGTG GTFEVKQHSF FTEVDWNSLL RQKAEFVPHL ESEEDTSYFD
TRSERYHHVQ AYEEDDTNDD EPVEIHRFSS CSPRFSKVYS SMEHLSQLEH KPPPVTLREH
KAPREDRVGK RESLGSVTLR EKSWRTGSPE MKRLSCSETF FTECDSSLAS GARRRFSALM
DTQRFASPLE LDFEPPVPGK HTPIKTRGAS LEGAMGFVSP HGDLRTFLKD VNSGSRGATT
DLVLRRARHQ QLSAEGDKPN SRPGTKVIKS ASATALSVMI PAVEQHGASP LPSPMSPRSL
SSNPSSRDSS PSRDCCPVVN VLHSPITIHR SGKKYGFTLR AIRVYMGDSD VYSVHHMVWH
VEDGGPAQEA GLRAGDLITH VNGESVHGLV HTEVVELILK SGNKVTVTTT PFENTSIKVG
PARKSSYKSK MARRSKKPGV KEGQDKKRSS LFRKITKQSN LLHTSRSLSS LNRSLSSGDS
LPGSPTHSLT ARSPTQTYRS SLETSYLGYR LSPNIGKTAS HHMRPSSLHG LSPKLHRQYR
SARCKSAGNI PLSPLAHTPS PTTSSPPPLS GHTVGSSNTT QTFPAKLHSS PPVARPRPKS
AEPPRSPLLQ RVQSAEKLGH SLEVTHGDYR RESFHCEHSL QSLLEIEGEN GPIGGLKPVR
RLGRQESPLS RDTLITKDKD SQTAASDITG RQARNATATF DKTRTAASTA ETDLSRTSGE
LKPRTSLEET KLNPENKPPN PRVLGSEATF TKSKPSEKTS NTSRSLQQED TKQQNVQTEN
GPATKAQEKT EEKEKCSAGR DKSNTRKSSG MEQTKQPIGP ETPEKGVIRV SDKTADTTKV
KGPAPPVPAQ VQTQPPTRNR VEKSTSSCRG VKEERAHLEV LEESPTSPSP RAASPCSGKS
RPISPGEKAS FVTQLTSVAK TVLGPMKGGP QEAGKAKDVA KTSEEKRGGT LAKADTLSGG
IRRGAHSTAP TTAGTAHSGR GNGRGFKHQS
//
