ID   A0A0N4Z317_PARTI        Unreviewed;      1445 AA.
AC   A0A0N4Z317;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   22-FEB-2023, entry version 23.
DE   RecName: Full=MAP kinase-activating death domain protein {ECO:0000256|ARBA:ARBA00017868};
OS   Parastrongyloides trichosuri (Possum-specific nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Parastrongyloides.
OX   NCBI_TaxID=131310 {ECO:0000313|Proteomes:UP000038045, ECO:0000313|WBParaSite:PTRK_0000129800.1};
RN   [1] {ECO:0000313|WBParaSite:PTRK_0000129800.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) 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   STRING; 131310.A0A0N4Z317; -.
DR   WBParaSite; PTRK_0000129800.1; PTRK_0000129800.1; PTRK_0000129800.
DR   Proteomes; UP000038045; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006915; P:apoptotic process; 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   Membrane {ECO:0000256|ARBA:ARBA00022475}.
FT   DOMAIN          30..507
FT                   /note="UDENN"
FT                   /evidence="ECO:0000259|PROSITE:PS50211"
FT   REGION          558..577
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          624..649
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          762..787
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          934..1057
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        558..576
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        624..641
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        762..778
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        946..962
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        964..981
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        982..1002
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1003..1018
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1032..1057
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1445 AA;  164831 MW;  721D8B0DA27454E5 CRC64;
     MDDKNKELCP RLLDYVVLVG RRENTKFESQ PLLTSYAQHE KKHILISNSS ILRRYPSDDH
     KDFALPKDVT CFCQPEGCVT LVSRRKWQQR REISSFVFTL TEKDSAKIRY GVSLNFFLSA
     PQPIEITYAS MPKEPNATGP IKVKKRISLS HLTSICIISH HPFLSGLREI ANLLRKIIIA
     ANYRCNKNES IPKNAVWSIL LGYWNSSYIP EEVMKEIREI ETWILMVLSS PVPVPGKTKI
     ELELLPKEFM PMIMLALPDH TRFSLVDFPL HLPLELLGIE TTLKLLSAVM LEYKVILQST
     NYNAVSMCVM ALVALMYPLE YMFPVIPLLP SYMPSAENIL LAPTPFIIGL PSSFFAFKNI
     EVPNDVIVVD LDTNVMNIPE DMEIPEFPQP EKDKLKYDFE VALGKAANIY NNGLKNEECK
     NIQELDEDEI DIAVRVAMIN FYNSPNIFVN FSEHTRTLRL YPRPVVALQI ESFLQSRPIK
     SQFIKDLCMT QSVEYFAECS LCPRNETYVR VQTGIKQASQ IGDKSKWFHE NLMPIHFLVY
     PDNSTIREAL EMTRKIGNTL PNESEAEESS SEVEGSNVLE ELCKNDLTPE SEKNTEIKPI
     AHVNHVFCPP IKLEIPDDAS VKSFCSSASS GRSTPDSESD ASAIDSEPDF ARMAKNMVLK
     RNDKGHMAFE NQKLSNNEDK EQKIANETYG SKPSRIIRRP QIKAFGMRGL QTVTDSGEKM
     LGPNFMNTIN GFTERSSDML SQMINKTTPK AQALKEKTMR PLHEVTGHPS EQEKSDKESS
     LAATQQTKNQ QIVKETCDQI LNGNSIGVFA FPKVKRLMED ESLRELVCQK LNLGLSIKYT
     EEEYEQNFKL TKSQYKGYLK IFQACINGLE SSFNANGSNG LASMLHVLEI AHSAFWFNAD
     GVITPVSEIN SAITTPSSNS YKLNFHEEHP MVKLPATTFD TRQNKSSIDN EIKKEEKSDN
     TDKSIPPPIP PRPPRPPPPR QESLTRNNLT KINIIPNDSS RHLTVFKNDE DGEKTPKILN
     PNEPKGPVCF TPLTDNQDTS NPNGQVPHLP RSSNPPKTLN FTRRISGSTD QSYVQTPTTA
     AKHFLYVDLI GTNNLLWQNM TFWENGFFDV VAQERDKIGM DQEPSELIDR YSSLSDTEKK
     RLELDEDRIL ATLLHNMTAY MVMCGTNKKL IQQKVRRLLG KAHIGLIYSK KINQLLDQLP
     EEQTNGIPLK PLVSRLMQKQ SFAVHIGSDN DCQLAFMEVC DDAVVLRAVT GSIMERWWYE
     RLVNMTYSPK THVLCIWRKK DDQVYMHKFY TKKCRQLYNC MKSAMERAAA RGKVTVAGRD
     LEGEFPVHDT TVNQGGLLTV RIDGIKLTFA NWDHFIDLRD IKKCNTFGGN QFMIEEFNRE
     KQQLEQRRFY SNMAHDIIWN IHRIFSIITT LCEELPKKDF EEKEIASILV NHEIPKKIPL
     DILRI
//