ID W5KT35_ASTMX Unreviewed; 1797 AA.
AC W5KT35;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 53.
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=MAST2 {ECO:0000313|Ensembl:ENSAMXP00000010747.2};
OS Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Characidae; Astyanax.
OX NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000010747.2, ECO:0000313|Proteomes:UP000018467};
RN [1] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA Jeffery W., Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX PubMed=25329095; DOI=10.1038/ncomms6307;
RA McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA Yoshizawa M., Warren W.C.;
RT "The cavefish genome reveals candidate genes for eye loss.";
RL Nat. Commun. 5:5307-5307(2014).
RN [3] {ECO:0000313|Ensembl:ENSAMXP00000010747.2}
RP IDENTIFICATION.
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; 7994.ENSAMXP00000010747; -.
DR Ensembl; ENSAMXT00000010747.2; ENSAMXP00000010747.2; ENSAMXG00000010437.2.
DR eggNOG; KOG0606; Eukaryota.
DR GeneTree; ENSGT00940000155705; -.
DR HOGENOM; CLU_000288_9_2_1; -.
DR InParanoid; W5KT35; -.
DR Proteomes; UP000018467; Unassembled WGS sequence.
DR Bgee; ENSAMXG00000010437; Expressed in brain and 13 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; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00992; PDZ_signaling; 1.
DR CDD; cd05609; STKc_MAST; 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; IPR037711; MAST.
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 InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24356:SF136; MICROTUBULE-ASSOCIATED SERINE_THREONINE-PROTEIN KINASE 2; 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 SMART; SM00220; S_TKc; 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.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000018467};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 429..702
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 703..771
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 1010..1098
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 728..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 776..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 825..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 858..923
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 969..1001
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1103..1275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1321..1797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..212
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..427
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 728..743
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 860..874
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..923
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 979..1001
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1123..1137
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1140..1220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1375..1401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1454..1514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1521..1552
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1580..1606
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1625..1643
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1664..1694
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1698..1713
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1750..1764
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1772..1788
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1797 AA; 196536 MW; E904848BC9C150D5 CRC64;
GKTKLQRQLS QDDGRARRSS MASGLTGKQL LPLSSSMHSG VSQLAWQQQT GEPNNLVRMR
SQSLGQSAPS LTAGLKELSL PRRGSFCRTS NRKSLIVTSS TSPTLPRPHS PLHGHTGSSP
LDSPRNFSPN TAAHFSFVPA RRTDGRRWSL ASLPSSGYGT NTPSSTVSSS CSSQEKLHQL
PFQPTADELH FLTKHFSSES ITDEEGRRSP AMRPRSRSLS PGRSPISFDH EIVMMNHVYK
ERFPKATAQM EERLAEFMSS SAPEKVMPLA DGVLSFIHHQ VIELSRDCLD KSREGLITSR
YFYELQENLE KLLQDAHERS ESVEVTFVTQ LVKKLMIIIA RPARLLECLE FDPEEFYHLL
EAAEGHAKEG QGIKSDIPRY IISQLGLTRD PLEEMAQLSS YDSGNPETPE TEDSSEPQPK
TKTPREEDFE TIKLISNGAY GAVFLVRHKE TRQRFAMKKI NKQNLILRNQ IQQAFVERDI
LTFAENPFVV SMFCSFETRR HLCMVMEYVE GGDCATLLKH IGALPVDMAR MYFAETVLAL
EYLHNYGIVH RDLKPDNLLI TSMGHIKLTD FGLSKIGLMS LTTNLYEGHI EKDAREFLDK
QVCGTPEYIA PEVILRQGYG KPVDWWAMGV ILYEFLVGCA PFFGDTPEEL FGQVISDEII
WPEEDEALPP DAQDLISKLL RQNPLERLGT GSAFEVKQHR FFTDLDWNSL LRQKAEFIPQ
LESEDDTSYF DTRSDRYHHL DSDEEEDTND DEHVEMRQFS SCSPRFNKVY SSMERLTLHE
EKRTPPPTKR SLSEEGAERI DSLSGLKSRD RSWLVGSPEI LRKRLSVSES SHTESDSSPP
LTVRRRCCSA IIEMPRFAIS SEEESSRKTP VRGPRSEELP SAIPELPVER ELKLDESPTT
PGSTSSRATL TRYTDGSDNS TPKAISDLAA RRARHRLLSG DTEKHTSRPL NKVIKSASAT
TLSLMIPADH HGASPLASPM SPHSMSSNPS SRDSSPSRDL SPAVCSVKPA IVIHRAGKKY
GFTLRAIRVY MGDTDIYTVH HMVWHVEEGG PAHEAGLREG DLITHVNGEP VHGLVHTEVV
ELILKSGTKV SISATPFENT SIKVGPARKT SSKSKMARRN KKTKTKEGQD SKKRNSLFRK
ITKQASLLHT SRSLSSLNRS VSSGESVPGS PTHMSPRSPT QGYRSTPDSA HSVGGNSSQS
SSPSSSVPNS PASSGQIRPS SLHGLAPKLQ RQYRSPRRKS AGNIPLSPLA RTPSPTPQST
SPQRSPSPLP SHALVSSSIG QSFPVKLHSS PPLVRQIARP KSADPPRSPL LKRVQSAEKL
ASLQESASET LLGGRVSPAE KGSLQKHSAR KLSRQEGPDS GTGSLGLAPG KSKLKDKLSA
IRQDRAERRE SLQKQDAIHE VDSSEDETDE GSEDSQDGRR TTFVPPSHVL RPTTVMGSPH
AIRMGPAALP SLSVTPSMVA QPGSPHLSQG LQAQQTQHTP LAQSQPEAKA SEQKLSQTPV
STPIPASTSA LAEDSSERGG RMLDSVSSSK TNTPLSSPLI SNISTPGSAF TTVSKDPFVK
PTVPPLDRRT SKAVEPRAKV SSKQESSTVP TAARESPVST TPTGGITKEM KEADNRRQAA
AAAAAAAATS STSTPTESGV DKVVSQLATV AKSVLGPVKL NIPGTKDAHE RSKEPRTLSD
GNPKSKDPRL ERSDSPDTSF PFVASASQTG RLPLPPSRQP PAKSEPPSTS QRPVELHSGA
PKKPSAPKDC SQTAGEQQDR PGTPRSSAPL RPGAEAQSQS QAKPSSSKPQ DKSSKKT
//
