ID A0A1S3W5Y4_ERIEU Unreviewed; 1641 AA.
AC A0A1S3W5Y4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=MAP kinase-activating death domain protein {ECO:0000256|ARBA:ARBA00017868};
GN Name=MADD {ECO:0000313|RefSeq:XP_016041898.1};
OS Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_016041898.1};
RN [1] {ECO:0000313|RefSeq:XP_016041898.1}
RP IDENTIFICATION.
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_016041898.1; XM_016186412.1.
DR CTD; 8567; -.
DR OrthoDB; 24616at2759; -.
DR Proteomes; UP000079721; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
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 Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW Kinase {ECO:0000313|RefSeq:XP_016041898.1};
KW Membrane {ECO:0000256|ARBA:ARBA00022475};
KW Reference proteome {ECO:0000313|Proteomes:UP000079721};
KW Transferase {ECO:0000313|RefSeq:XP_016041898.1}.
FT DOMAIN 14..562
FT /note="UDENN"
FT /evidence="ECO:0000259|PROSITE:PS50211"
FT REGION 106..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 675..831
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 902..930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1040..1065
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1148..1172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1184..1235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..709
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..764
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 782..831
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1153..1172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1184..1209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1641 AA; 182578 MW; 2EF5E226B8238940 CRC64;
MVQKKKLCPR LLDYLVIVGA RHPSSDSVAQ TPELLRRYPL EDHAEFPLPP DVVFFCQPEG
CLSVRQRRMS LRDDTSFVFT LTDKDTGVTR YGICVNFYRS FQKRMPKDKG EGGAGSRAKE
GTRAPKETGT ESSESGSSLQ PPSADSTPDV NQSPRGKRRA KGVSRSRNST LTSLCVLSHY
PFFSTFRECL YTLKRLVDCC SEQLLGKKLG IPRGIQRDTM WRIFTGSLLV EEKSSALLHD
LREIEAWIYR LLRSPVPVSG QKRVDIEVLP QELQQALTFA LPDPSRFSLV DFPLHLPLEL
LGVDACLQVL TCILLEHKVV LQSRDYNALS MSVMAFVAMI YPLEYMFPVI PLLPTCMASA
EQLLLAPTPY IIGVPASFFL YKLDFKMPDD VWLVDLDSNR VIAPTHAEVL PILPEPESLE
LKKHLKQALA SMSLNTQPIL NLEKFHEGQE IPLLLGRPSS DLQSTPSTEF NPLIYGNDVD
SVDVATRVAM VRFFNSPNVL QGFQMHTRTL RLFPRPVVAF QAGSFLASRP RQTPFAEKLA
RTQAVEYFGE WILNPTNYAF QRIHNSMFDP ALIGDKPKWY AHQLQPIHYR VYDGNSQLAE
ALSIPPERDS DSDPTDDSGS DSMEYDDSSS SYSSLGDFVS EMMKCDINGD TPNVDPLTHA
ALGDASEVEI DELPSQKEAE DPGPNREVSQ ENPPLHSSPS TTVHGASSGT ADSAEMDAKA
TVGVTKPLPT VPGKIPTDKP LVETGEGSVH RRTYDNPHFE PPSDFPPEED EEEEEEQGES
YTPRFSQHVN GNRAQQLLRP NSLKLASDSD AESDSRASSP TSTVSNNSTE GFGGIMSFAS
SLYRNHSTSF SLSNLTLPTK GAREKATPFP SLKVFGLNTL MEIVTEAGPG SGEGNRRALV
DQKSSVIKHS PTVKREPPSP QGRSSNSSEN QQFLKEVVHS VLDGQGVGWL NMKKVRRLLE
SEQLRVFVLS KLSRTVQSEE DARQDIIPDV EISRKVYKGM LDLLKCTVLS LEQSYSHAGL
GGMASIFGLL EIAQTHYYSK EPEKRKRSPT ESINTPVGKD PGLAGRGDPK AMAQLRVPQL
GPWAPSSTGR GLKEPDTRSL KEENFVASIE LWNKHQEVKK QKALEKQIFS YSGPEVIKPV
FDLGETEEKK SQISADSGVS LTSGSQKTDS DSVIGVSPAV MIRSSSQDSE VSTVVSNSSG
ETLGADSDLS SNAGDGPGGE GNAHLASSRA TLSDSEIETN SATSAIFGKA HSLKPSVREK
LVGSPVRSSE DTSQRVYLYE GLLGRDKGSM WDQLEDAAME TFSISKERST LWDQMQFWED
AFLDAVMLER EGMGMDQGPQ EMIDRYLSLG EHDRKRLEDD EDRLLATLLH NLISYMLLMK
VNKNDIRKKV RRLMGKSHIG LVYSQQINEV LDQLADLNGR DLSIRSSGSR HMKKQTFVVH
AGTDTNGDIF FMEVCDDCVV LRSNIGTVYE RWWYEKLINM TYCPKTKVLC LWRRNGSETQ
LNKFYTKKCR ELYYCVKDSM ERAAARQQSI KPGPELGGEF PVQDMKTGEG GLLQVTLEGI
NLKFMHNQVF IELNHIKKCN TVRGVFVLEE FVPEIKEVVS HKYKTPMAHE ICYSVLCLFS
YVAAVRSSEE DLRTPPRPVS S
//
