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Database: UniProt
Entry: A0A1W4WIX3_AGRPL
LinkDB: A0A1W4WIX3_AGRPL
Original site: A0A1W4WIX3_AGRPL 
ID   A0A1W4WIX3_AGRPL        Unreviewed;      1819 AA.
AC   A0A1W4WIX3;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=MAP kinase-activating death domain protein {ECO:0000256|ARBA:ARBA00017868};
GN   Name=LOC108733349 {ECO:0000313|RefSeq:XP_018319970.1};
OS   Agrilus planipennis (Emerald ash borer) (Agrilus marcopoli).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Elateriformia;
OC   Buprestoidea; Buprestidae; Agrilinae; Agrilus.
OX   NCBI_TaxID=224129 {ECO:0000313|Proteomes:UP000192223, ECO:0000313|RefSeq:XP_018319970.1};
RN   [1] {ECO:0000313|RefSeq:XP_018319970.1}
RP   IDENTIFICATION.
RC   TISSUE=Entire body {ECO:0000313|RefSeq:XP_018319970.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
CC       Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004370}.
CC   -!- SIMILARITY: Belongs to the MADD family.
CC       {ECO:0000256|ARBA:ARBA00005978}.
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DR   RefSeq; XP_018319970.1; XM_018464468.1.
DR   EnsemblMetazoa; XM_018464468.1; XP_018319970.1; LOC108733349.
DR   GeneID; 108733349; -.
DR   OrthoDB; 24616at2759; -.
DR   Proteomes; UP000192223; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.450.200; -; 1.
DR   Gene3D; 3.40.50.11500; -; 1.
DR   InterPro; IPR001194; cDENN_dom.
DR   InterPro; IPR005112; dDENN_dom.
DR   InterPro; IPR043153; DENN_C.
DR   InterPro; IPR039980; MADD.
DR   InterPro; IPR037516; Tripartite_DENN.
DR   InterPro; IPR005113; uDENN_dom.
DR   PANTHER; PTHR13008:SF7; MAP KINASE-ACTIVATING DEATH DOMAIN PROTEIN; 1.
DR   PANTHER; PTHR13008; MAP-KINASE ACTIVATING DEATH DOMAIN PROTEIN MADD /DENN/AEX-3 C.ELEGANS; 1.
DR   Pfam; PF02141; DENN; 1.
DR   Pfam; PF03456; uDENN; 1.
DR   SMART; SM00801; dDENN; 1.
DR   SMART; SM00799; DENN; 1.
DR   SMART; SM00800; uDENN; 1.
DR   PROSITE; PS50211; DENN; 1.
PE   3: Inferred from homology;
KW   Apoptosis {ECO:0000256|ARBA:ARBA00022703};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Kinase {ECO:0000313|RefSeq:XP_018319970.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192223};
KW   Transferase {ECO:0000313|RefSeq:XP_018319970.1}.
FT   DOMAIN          19..641
FT                   /note="UDENN"
FT                   /evidence="ECO:0000259|PROSITE:PS50211"
FT   REGION          136..210
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          501..541
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          685..710
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          740..918
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          976..1004
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1025..1054
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1092..1145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1293..1355
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        136..156
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        169..202
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        501..516
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        523..541
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        768..794
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        795..821
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        822..856
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        867..918
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1036..1054
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1092..1128
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1293..1329
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1819 AA;  201989 MW;  71338472E0BB1534 CRC64;
     MSSESERQFL CPRLIDYLTI VGVKSCNNTK SSSSTSVQAP ELLRRYPVQD HKDFPMPLDM
     VYFCQPEGCS TVGPKRSALR EAQSFVFALT DKDSGKTRYG ICVNFYRPVE KTSAGGGGGR
     GNSYLRRDSW RKSMEKSSDS AFSSDYRSSN IGPSDSERDF PSRRDSDAVG QPVPNTTQSC
     VRLGITPIPN DSESGGSHSP SPRASRRRQK VRNNSLTSLC LLSHHPFFSM FRECLYVLRK
     IIDACNESSS SKRVGASRQA GRDTVWSVLT GQATDTTPSI ILHDVREIET WILRLLSAPV
     PIPGKTKVEV EIISSNIQEP LCFALPDHTR FSLVDFPLHL PLELLGVETC LKVLTLILLE
     YKVILQSRDY NALSMSVMAF VTMIYPLEYM FPVIPLLPTC MSYAEQLLLA PTPYVIGLPA
     TFLMYKKNFR LPEDIWVVDL DSNKLSNVGS SMEIPSLPEP ESTILKNHLK QALSGLTATT
     SPTFQSLPVN REVQPVGNTL SVSMSKSKSP ETSPIMRNKP FKSLPSPFSQ PATPQQRSNA
     VSPVSPIPFN PIIYGNDVDS VDVATRVAMV RFFNSQNLLA NFTEHTRTLR LYPRPVVAFQ
     INSFLRSRPR SSQFINRFAR TQAVEFFAEW SLTPSNVAFQ RVQTGVLDPS QIGDKPKWYI
     QTLETIKFVV WDEGSSLNSA LKCMQNQESQ PTDESGSDSE GAESTSSSFS SLSDFMSEMV
     SSDISPGASN YEAKHSAAQK MTLSSNLDPQ SVYNPPSELR YPENFVPEKS SRPSSPQSTS
     SSQSDLSSPS FNRDSESEMD QRRKNDIPTA KEEKEEVGSI ENESDSNSTA TPRTVISGGA
     AKPGSSSSTT SESTEKSPIS RKSRYVPPIT PTLQKQPSIG NVLARTSSFG SSGSGSPALS
     SGGSVDKVQR QSSQGSLFEQ FASQAKELML ETTRQSSQDG ILAQMDKFKT QARGKLSEAE
     ESSLFAPFDK LASHAKKAAE EATKSVQEAG KTAIEASKSA ADASKTTFED LTYVGKSTLG
     DLTKGAREVS KKALKRTDSG SQSGSDSRRG SSNSLVHAST GLIAGTSRDF FSNISSDLTD
     IAQTTSSMFS DLFGSNKSTS RAQAQQQQQQ QQQQHSQTSQ QQKITKDTKS GIFGPFPRGP
     KGLVEKSPLI KHTPRRQDDF QRIQSVERST TNIENQTFLK EVVNQVLEGE GVGWLKLNRL
     KKLMEDESYR NFVLSKLNKT LERRIAPDDH IDDVCVSKSV WKGMLKVLLA SVHGLEYTYS
     NFGLGGMASA FQLQEIAHTH YWSKDLSDSL YSDNPSHLLS SQGSSPRGSK ENLSSPQSPR
     NSMSPDWDSS RKSSHAEPPQ VRLPQSDEAD VEQQQSTAEI FKDMLNQKKN LLLSKLTSFD
     SDAENTMHGS GGTLSPGGSI TTGPACNLNR GGFQSSYRST VSDTEVETLQ FPKPTKQRTA
     SVWSSKSSLS TGFRYHGGHM VNTLTSPSPE VARTYLFEGL IGKERSSLWD QMQFWEDAFL
     DAVSQERDMI GMDQGPREMM ERYKSLSETE RKRLEHEEDR LLSTMLYNLT AVLVMLKCNK
     AEIKKKIRRL LGKCHIGLVY SQEVNQLLDQ IEHLNGNDID LKPSLSRLLH RQSFTVHQGV
     NGEGELRFME VRDDGLVLRS VSGVIIERWW YERLVNMTYS PKNKVLCLWR RSGQQTQLHK
     YYTKKCKELY YCIKEAMERG GVAGKAPELG GEFPVQDMST GEGGLLQVCM EGVGLLFANS
     KDFEFFVRID HIRKCFTQKG GIFVLEEFNP KTRQVIQRKY KSSMANDMLL SIHRIFSICM
     TQRLSELYGV NDDNPSLPA
//
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