ID A0A384C3V9_URSMA Unreviewed; 2351 AA.
AC A0A384C3V9;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 03-AUG-2022, sequence version 2.
DT 27-MAR-2024, entry version 25.
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=MAST4 {ECO:0000313|RefSeq:XP_008689566.2};
OS Ursus maritimus (Polar bear) (Thalarctos maritimus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=29073 {ECO:0000313|Proteomes:UP000261680, ECO:0000313|RefSeq:XP_008689566.2};
RN [1] {ECO:0000313|RefSeq:XP_008689566.2}
RP IDENTIFICATION.
RC TISSUE=Whole blood {ECO:0000313|RefSeq:XP_008689566.2};
RG RefSeq;
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 RefSeq; XP_008689566.2; XM_008691344.2.
DR KEGG; umr:103663623; -.
DR OrthoDB; 2915765at2759; -.
DR Proteomes; UP000261680; Unplaced.
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:SF224; MICROTUBULE-ASSOCIATED SERINE_THREONINE-PROTEIN KINASE 4; 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, ECO:0000313|RefSeq:XP_008689566.2};
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:UP000261680};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 376..649
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 650..722
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 880..968
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 26..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 724..882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 966..1001
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1028..1220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1277..1302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1392..1412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1554..2112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2124..2351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..777
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 788..809
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 822..841
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..882
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 982..998
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1028..1084
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1119..1133
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1134..1156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1191..1219
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1277..1295
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1569..1583
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1709..1723
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1783..1799
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1835..1854
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2178..2206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2244..2261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2330..2351
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2351 AA; 255622 MW; F1EA0F029303D6CE CRC64;
MDMSDPNFWT VLSNFTLPHL RSGNRLRRTQ SCRTSNRKSL IGNGQSPALP RPHSPLSAHA
GNSPQDSPRN FSPSASAHFS FARRTDGRRW SLASLPSSGY GTNTPSSTVS SSSSSQEKLH
QLPYQPTPDE LHFLSKHFCT TESIATENRC RNTPMRPRSR SLSPGRSPAC CDHEIIMMNH
VYKERFPKAT AQMEERLKEI ITSYSPDHVL PLADGVLSFT HHQIIELARD CLDKSHQGLI
TSRYFLELQH KLDKLLQEAH DRSESGELAF IKQLVRKILI VIARPARLLE CLEFDPEEFY
YLLEAAEGHA KEGQGIKTDI PRYIISQLGL NKDPLEEMAQ LGNYDSGTAE TPETDESVSS
SNASLKLQRK PRESDFETIK LISNGAYGAV YFVRHKESRQ RFAMKKINKQ NLILRNQIQQ
AFVERDILTF AENPFVVSMY CSFETRRHLC MVMEYVEGGD CATLMKNMGP LPVDMARMYF
AETVLALEYL HNYGIVHRDL KPDNLLVTSM GHIKLTDFGL SKVGLMSMTT NLYEGHIEKD
AREFLDKQVC GTPEYIAPEV ILRQGYGKPV DWWAMGIILY EFLVGCVPFF GDTPEELFGQ
VISDEINWPE KDEAPPPDAQ DLITLLLRQN PLERLGTGGA YEVKQHRFFR SLDWNSLLRQ
KAEFIPQLES EDDTSYFDTR SEKYHHMETE EEDDTNDEDF NVEIRQFSSC SHRFSKVFSS
VDRITQNSGE EKEDPGDKTK STALPSTETF SWSSEYSEMQ QFSTSNSSDT ESNRRKLSSG
PLPKLAISTE AEKDEAAPCP RDLPEEPEKP VLPPAESAQE EPEVTTPAST ISSSTLSDMF
AVSPLGSPMS PHSLSSDPSS SRDSSPSRDS SAASASPHQP VVIHSSGKNY GFTIRAIRVY
VGDSDIYTVH HIVWNVEEGS PACQAGLKAG DLITHINGEP VHGLVHTEVI ELLLKSGNKV
SITTTPFENT SIKTGPARRN SYKSRMVRRS KKSKKKESLE RRRSLFKKLA KQPSPLLHTS
RSFSCLNRSL SSGESLPGSP THSLSPRSPT PSYRSTPDFP SGTNSSQSSS PSSSAPNSPA
GSGHIRPSTL HGLAPKLSGQ RYRSGRRKSA GSIPLSPLAR TPSPTPQPTS PQRSPSPLLG
HSLGNSKITQ AFPSKMHSPP TIVRHIVRPK SAEPPRSPLL KRVQSEEKLS PSYGSDKKHL
CSRKHSLEVT QEEVQREQPQ REVTLQSLEE NVCDAPSLSR ARPVEQGCLK RPVSRKLGRQ
ESVDELDREK LKAKVVVKKP DGFPEKQEPH QKSHGLGSDL ENLSTYRLEE REKKIYPKAL
ERSNHFENKG ALQETQSLGS LLKGALHKQV SIRASEGVTS EGAATGHVLA PGDHSQGISD
FKRTSVPSTL QDTLCHSTDR SSSVKGENLE KAPQAKECLR CEKLDSKLAN IDYLRKKMSL
EDKDDSLCPV LKPKMTSSAH ESLPGNPVRA IGGQQEALPA SESRAFVNSA HPAQISSVSF
VPLKALASRV DAGVEKPGLV APESPVRKSP SEYKLEGRSV SCLKPIEGTL DIALLSGPQA
SKTELPSPEP TQSPSPASDV GPSVPPALPS SGGMRGDTAG QREPSPAGFR MTKSYLLESR
FPPSSRGLQN SPATPLPDPE VKRDRKASHA ARSPMTVMES DPQQREGGPS KHQDHSPDTK
LLPFLGQNPH SADPSRSRSL LPPEGTPSRE KLSGRESSER APSAARSERS AMRANSRRDP
SVELCPPEAA KTSDNSRNLP CGGRPRPDFH TQPHPMEKAW GPCGKTSHRD GRVEVRPLAR
EDSSFPSAGT SERELGRGRG GMEPQPEAPP ARWSLQPPST ENGKGDQLSG FPSFQKDSPK
ELERKEQLLQ KHVSSSSQPV PVTKELPSPA ARPHCSSPSH SSGREPAGKP CAAEPSLGLQ
GPPKPTAAHS ESSSHKPRPG PDPSPPKSKH PDRALSSQKP SGGPAASKEP GAQPPVGPSR
EEKGGSKGVL DAFPALPGSQ NTANDAMSQG GGGPSVPLHT EGALLDTKMK PASAGRPPEV
LEKPTHLPWQ GHSGADESVD QKPATVSEKQ NLSPKHPKPS TVKDCPALCK QTEKSPSSQA
TATPDRKSEG KKCTEALYVA ADSGKLEASL SLAPGEARPK GPERPAAAVG KGLPEAKGKG
LSPQKPLTEA GKPSGMKRSP SATGQSSLRS AALPEKSLSS SSSFPEARPG AREATASGSD
SSSAKASGAA AKALPGGDGR THMTKSDSMP SFRSPTVTLE LQHPGPSVAG GAGHRDRAMS
VTATIGETKG KEPVPAPPSQ TRKQNAGREV TKVSPAPNPD RPIALSSEKD FVVRQRRGKE
SLRSSPHKKA S
//
