ID A0A2K5E8V2_AOTNA Unreviewed; 2618 AA.
AC A0A2K5E8V2;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
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:ENSANAP00000029647.1};
OS Aotus nancymaae (Ma's night monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC Aotus.
OX NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000029647.1, ECO:0000313|Proteomes:UP000233020};
RN [1] {ECO:0000313|Ensembl:ENSANAP00000029647.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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_012317658.1; XM_012462235.1.
DR STRING; 37293.ENSANAP00000029647; -.
DR Ensembl; ENSANAT00000047677.1; ENSANAP00000029647.1; ENSANAG00000032575.1.
DR GeneID; 105723947; -.
DR CTD; 375449; -.
DR GeneTree; ENSGT00940000156399; -.
DR OrthoDB; 2915765at2759; -.
DR Proteomes; UP000233020; 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};
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:UP000233020};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 571..844
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 845..917
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 1142..1230
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 920..1083
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1108..1144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1229..1263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1290..1563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1612..1671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1769..1788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1810..2023
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2058..2367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2399..2618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..74
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..560
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 935..972
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1018..1068
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1069..1083
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1110..1144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1244..1260
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1290..1346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1381..1395
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1396..1414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1453..1481
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1514..1557
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1816..1833
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1845..1863
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1965..1979
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2001..2023
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2069..2084
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2212..2238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2250..2265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2432..2454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2515..2542
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2565..2592
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2597..2618
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2618 AA; 283163 MW; FA5A11ECF093F424 CRC64;
MGEKVSEAPE PVPRGCSTHG SRTPASVAVA ASSLGASSAE SSSGSETLSE EGEPGGFSRK
QPPPPPPPPP GGALGARPLA AWAPARVLLE RGVPALPPPP PGGAALPAPR GSSASQEEQD
EELDHILSPP PMPFRKCSNP DVASGPGKSL KYKRQLSEDG RQLRRGSLGG ALTGRYLLPN
PVTGQAWPAS AETSNLVRMR SQALGQSAPS LTASLKELSL PRRGSLCRTS NRKSLIGNGQ
SPALPRPHSP LSAHAGNSPQ DSPRNFSPSA SAHFSFARRT DGRRWSLASL PSSGYGTNTP
SSTVSSSCSS QEKLHQLPYQ PTPDELHFLS KHFCTTESIA TENRCRNTPM RPRSRSLSPG
RSPACCDHEI IMMNHVYKER FPKATAQMEE RLKEIITSYS PDNVLPLADG VLSFTHHQII
ELARDCLDKS HQGLITSRYF LELQHKLDKL LQEAHDRSES GELAFIKQLV RKILIVIARP
ARLLECLEFD PEEFYYLLEA AEGHAKEGQG IKTDIPRYII SQLGLNKDPL EEMAQLGNYD
SGTAETPETD ESVSSSNTSL KLRRKPRESD FETIKLISNG AYGAVYFVRH KESRQRFAMK
KINKQNLILR NQIQQAFVER DILTFAENPF VVSMYCSFET RRHLCMVMEY VEGGDCATLM
KNMGPLPVDM ARMYFAETVL ALEYLHNYGI VHRDLKPDNL LVTSMGHIKL TDFGLSKVGL
MSMTTNLYEG HIEKDAREFL DKQVCGTPEY IAPEVILRQG YGKPVDWWAM GIILYEFLVG
CVPFFGDTPE ELFGQVISDE INWPEKDEAP PPDAQDLITL LLRQNPLERL GTGGAYEVKQ
HRFFRSLDWN SLLRQKAEFI PQLESEDDTS YFDTRSEKYH HMETEEEDDT NDEDFNVEIR
QFSSCSHRFS KVFSSIDRIT QNSAEEKEDS GDKTKSTTLP STETLSWSSE YSEMQQLSTS
NSSDTESNRH KLSSGLLPKL AISTEGEQDE ATSCPGDPHE DPGKPALPPE ECAQEEPEVT
TPASTISSST LSVGSFSEHL DQINGRSECV DSTDNSSKPS SEPTSHMARQ RLESTEKKKI
SGKVTKSLSA SALSLMIPGD MFAVSPLGSP MSPHSLSSDP SSSRDSSPSR DSSAASASPH
QPIVIHSSGK NYGFTIRAIR VYVGDSDIYT VHHIVWNVEE GSPACQLGLK AGDLITHING
EPVHGLVHTE VIELLLKSGN KVSITTTPFE NTSIKTGPAR RNSYKSRMVR RSKKSKKKES
LERRRSLFKK LAKQPSPLLH TSRSFSCLNR SLSSGESLPG SPTHSLSPRS PTPSYRSTPD
FPSGTNSSQS SSPSSSAPNS PAGSGHIRPS TLHGLAPKLS GQRYRSGRRK SAGNIPLSPL
ARTPSPTPQP TSPQRSPSPL LGHSLGNSKI AQAFPSKMHS PPTIVRHIVR PKSAEPPRSP
LLKRVQSEEK LSPSYGSDKK HLCSRKHSLE VTQEEVQREQ SQREAPLQSL DENVCDAPPL
SRARPVEQGC LKRPVSRKLG RQESVDDLDR DKLKAKVVVK KPDGFPEKPE SHQKSHGPGS
DLENLALFKL EEREKKIYPK AVERSSPFEN KVALQETPPL GSLLKDALHK QASVRASEGA
ISDGLASAEH SQGGGDFRRA PAPGTLQDGL CHSLDRGVAG KGEGTEKASQ AKELLRCEKL
DSKLANIDYL RKKMSLEDKE DNLCPVLKPK MTASTHECLP GNQVRPMGGP QEPPPASESR
AFVSSTHAAQ MSTVSFVPLK ALTGRVDSGA EKPGLVAPES PVRKSPSEYK LEGRTVSCLK
PIEGTLDIAL LSGPQASKTE LPSPESVQSP SPGGDVGPSV PPALPSSSGK KSETASARDL
SPASLKMNKS YLLEPRFLPP SHGLQNSPAV SLPHPELKRE RKGPHPTARS PATVMESNPQ
QREGSSPKHQ DHTTDNKLLT GPGQNLQADL ARPRGLLPPE VSPSREKPGL RESAERGPST
ARSERSAPRA DICREPCMQL CSPETTKTSD NSKNLPSMGR THPDFYTQTQ AMEKAWAPGG
KTNHKDGLDE TRLLCRDDSS LHSAGTPCEK ELGKVRRGVE PKPEAPPARR SLQPPGIESG
KSEKLSSFPS VQKDGAKEPE RKEQPLQRHP SSIPPPPLTA KDLPSPAARQ PCSSPSHASG
RGPGAKLSAP EPSPSPQDPP KPVAAHSENS SHKPRPGPDP GPPKSKHPDR SLSSQKPSVG
ATKGQEPATQ SVGGSSREGK GHSRSGPDVF PATPGSQNKA SGEVGQGESG PSVCLHTDRG
PLDSKLQPAN GGRPLEVLEK PVHLPRPGHP GPSEPADQKL TAVGEKQTLS PKHPKPSTVK
DCPALCRQTD KSPSQPAAAT DRRAEGKKCT EALYAPADSN THEASLAFAH GEARLKGAER
PAAGVGKGFP EARGKGPCAQ KPPVEADKPS SMKRSPSATG QSSLRSTALP EKPLSCSSSF
PEARPGVREA STACSDTSSD KAAGGAQEPP APSSRNHRKA QPAGEARTHM TKSDSLPCFR
VSTLTLESNH PDPNTTGGAS HRDRALSVTA TVGETRGKDP ALAQPPTTRK QNVGRDVTKP
SPAPNTDRLI SLSNEKDFVV RQRRGKESLR SSPHKKAL
//
