ID A0A1S3W7F8_ERIEU Unreviewed; 1640 AA.
AC A0A1S3W7F8;
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_016041899.1};
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_016041899.1};
RN [1] {ECO:0000313|RefSeq:XP_016041899.1}
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_016041899.1; XM_016186413.1.
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_016041899.1};
KW Membrane {ECO:0000256|ARBA:ARBA00022475};
KW Reference proteome {ECO:0000313|Proteomes:UP000079721};
KW Transferase {ECO:0000313|RefSeq:XP_016041899.1}.
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..1231
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..1205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1640 AA; 182605 MW; 5D2ECD09CD131558 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 VSNSSGETLG
ADSDLSSNAG DGPGGEGNAH LASSRATLSD SEIETNSATS AIFGKAHSLK PSVREKLVGS
PVRSSEDTSQ RVYLYEGLLG RDKGSMWDQL EDAAMETFSI SKERSTLWDQ MQFWEDAFLD
AVMLEREGMG MDQGPQEMID RYLSLGEHDR KRLEDDEDRL LATLLHNLIS YMLLMKVNKN
DIRKKVRRLM GKSHIGLVYS QQINEVLDQL ADLNGRDLSI RSSGSRHMKK QTFVVHAGTD
TNGDIFFMEV CDDCVVLRSN IGTVYERWWY EKLINMTYCP KTKVLCLWRR NGSETQLNKF
YTKKCRELYY CVKDSMERAA ARQQSIKPGP ELGGEFPVQD MKTGEGGLLQ VTLEGINLKF
MHNQERKVFI ELNHIKKCNT VRGVFVLEEF VPEIKEVVSH KYKTPMAHEI CYSVLCLFSY
VAAVRSSEED LRTPPRPVSS
//
