ID A0A287DBI4_ICTTR Unreviewed; 2463 AA.
AC A0A287DBI4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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|Ensembl:ENSSTOP00000030856.1};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000030856.1, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000030856.1}
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 EMBL; AGTP01013999; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01014000; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01014001; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01014002; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01014003; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01014004; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01014005; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01014006; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01014007; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01014008; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 43179.ENSSTOP00000030856; -.
DR Ensembl; ENSSTOT00000042415.1; ENSSTOP00000030856.1; ENSSTOG00000023790.2.
DR GeneTree; ENSGT00940000156399; -.
DR InParanoid; A0A287DBI4; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000005215};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 90..111
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 410..683
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 684..756
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 982..1070
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 378..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 759..922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 947..984
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1068..1103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1130..1522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1544..1585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1614..1641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1654..1838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1890..2212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2224..2463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..811
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..907
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..922
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 949..984
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1084..1100
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1130..1186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1221..1235
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1293..1321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1322..1336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1355..1431
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1504..1522
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1670..1684
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1693..1713
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1755..1772
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1784..1800
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1811..1825
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1961..1976
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1977..2008
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2057..2087
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2277..2305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2349..2380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2442..2463
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2463 AA; 268090 MW; 23E0AF53A8765287 CRC64;
MQTNTTLPCG GFTSLSSALQ TVTLLHTVFC LIGFPPYPPG TASHTKTLIL CPPSHSSQTL
NPWLVGHTSC ALCRSLVSVP FSLLYSPLKL VFLLNIVSAI FSLKTVFFFL FDSCRTSNRK
SLIGNGQSPA LPRPHSPLSA HAVLSSCSSQ EKLHQLPYQP TPDELHFLSK HFCTTESIAT
ENRCRNTPMR PRSRSLSPGR SPACCDHEII MMNHVYKERF PKATAQMEER LKEIITSYSP
DNVLPLADGV LSFTHHQIIE LARDCLDKSH QGLITSRYFL ELQHKLDKLL QEAHDRSESG
ELAFIKQLVR KILIVIARPA RLLECLEFDP EEFYYLLEAA EGHAKEGQGI KTDIPRYIIS
QLGLNKDPLE EMAQLGNYDS GTAETPETDE SVGSSNASLK LRRKPRESDF ETIKLISNGA
YGAVYFVRHK ESRQRFAMKK INKQNLILRN QIQQAFVERD ILTFAENPFV VSMYCSFETR
RHLCMVMEYV EGGDCATLMK NMGPLPVDMA RMYFAETVLA LEYLHNYGIV HRDLKPDNLL
VTSMGHIKLT DFGLSKVGLM SMTTNLYEGH IEKDAREFLD KQVCGTPEYI APEVILRQGY
GKPVDWWAMG IILYEFLVGC VPFFGDTPEE LFGQVISDEI NWPEKDEAPP PDAQDLITLL
LRQNPLERLG TGGAYEVKQH RFFRSLDWNS LLRQKAEFIP QLESEDDTSY FDTRSEKYHH
METEEEDDTN DEDFNVEIRQ FSSCSHRFSK VFSSIDRITQ NSGEEKEDSG DKTKSTTLPS
TETLSWSSEY SEVQQLSTSN SSDTESNRHK LSSGLLPKLA ISAEGEQDEA TPCPGDPHGE
PGKPALPPEE CAQEEPEVTT PASTISSSTL SVGSFSEHLD QINGRSECVD STDNSSKPSS
EPASHMARQR LESTEKKKIS GKVTKSLSAS ALSLMIPGDM FAVSPLGSPM SPHSLSSDPS
SSRDSSPSRD SSSTAAPSPH QPIVIHSSGK NYGFTIRAIR VYVGDSDIYT VHHIVWNVEE
GSPAYQAGLK AGDLITHING EPVHGLVHTE VIELLLKSGN KVSITTTPFE NTSIKTGPAR
RNSYKSRMVR RSKKSKKKES LERRRSLFKK LAKQPSPLLH TSRSFSCLNR SLSSGESLPG
SPTHSLSPRS PTPSYRSTPD FPSGTNSSQS SSPSSSAPNS PAGSGHIRPS TLHGLAPKLS
GQRYRSGRRK SAGSIPLSPL ARTPSPTPQP TSPQRSPSPL LGHSLGNAKI AQAFPSKMHS
PPTIVRHIVR PKSAEPPRSP LLKRVQSEEK LSPSYGSDKK HLCSRKHSLE VTQEEVQREQ
SQREATLQSL EENNVCDAPS LSRARPVEQG CLKRPVSRKV GRQESVDDVD RDKLKSKVTV
KKPDGLPEKP ESHQKPHGLS SDAENHALFR LEEREKKVYP KPLERSSHFE NKAAEAQSLG
NRLKDVLHKQ ASVRATEGMA SDGTAAACGP APGEHNQGMG DFKRASAPGT LQDSLCRSPD
RSTSGKGENT EKTSQAKEFL RSEKLDSKLA NIDYLRKKMS LEDKEDGHCS MLKPKITSST
HECLPGNPVR PMGGQQEAPP GSESRAFISS THTTQMSTVS FVPLKTLAGR VDGGAEKSGL
VAPESPVRKS PSEYKLEGRS VSCLKPIEGT LDIALLSGPH ASKTEQPSPE PAQSPSPGGD
MAPSVPLPLP GSSGKKSETS SLREPSPASS KMNKSYLLEP RFLPPSWGLQ NSPAASLPDP
ELRRDRKVSH PAARSPLTVT ENDSQQRVCG PTKHQDCATD TKVIPGLGQT QHSNDQARSC
GPLPSEGAPS KEKANLKDPS EKGPSPGRSE RSALRADVHR DPIVELYPLE IAKANDNCKN
HPAVGRTHPD ASSAQAQTLE KAWGPCAKTY HKDGQGEARS LVRENSSLNS ARIPCEREVG
KIRSSMEPKP EAPPAKCPLQ PLGIESRKTE KLPSFSSLQK EGPKEPDRKE QPLQRHVSSD
SQHPLTTKDL SGPASHQHCS SSSLGPQGTK PGVAEPAAAF QDPPRPSVAV HSESSDHNLR
PGPDPSPSKS KHPDRSLSSQ KSSVVTAKGK EPVTQPLSGS SREGRNNSKG GLDVFTAIPG
SQSKANEVGG GAESVPFNPL HAEECPLDPK LKPSSGRGPE MQEKQLHLPR PGHPGSSESV
DHKPPIVSEK QSLSPKHPKP STVKDCPPLC RQTDRSPSQQ APAADRKPEG KKCTEVLYVP
AADSGKLEAS LSLAPGEARL KGTEKPGAAM GKSSSEAKGK GPGPQKTLPE AGKLSSMKRS
PSATGQSSFR SSALPEKSLS YSSSFPEARP GVRDAATASS SPSSAKANGA ALEPTAPSNR
DHRKSQSGAD GRTQMTKSDS LPSFRLATSA LESQHSDAQG LSGVGHRDRA LSVTAATGET
KGREPAPAQP FPTRKQNVGR EAIKAPQAPN SDRPITLSSE KDFVVRQRRG KESLRSSPHK
KAS
//
