ID A0A3B3D4W9_ORYME Unreviewed; 1567 AA.
AC A0A3B3D4W9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, 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=MADD {ECO:0000313|Ensembl:ENSOMEP00000024906.1};
OS Oryzias melastigma (Marine medaka).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000024906.1, ECO:0000313|Proteomes:UP000261560};
RN [1] {ECO:0000313|Ensembl:ENSOMEP00000024906.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 STRING; 30732.ENSOMEP00000024906; -.
DR PaxDb; 30732-ENSOMEP00000024906; -.
DR Ensembl; ENSOMET00000008495.1; ENSOMEP00000024906.1; ENSOMEG00000005888.1.
DR GeneTree; ENSGT00940000156718; -.
DR OMA; KILCLWR; -.
DR Proteomes; UP000261560; 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: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 Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW Membrane {ECO:0000256|ARBA:ARBA00022475}.
FT DOMAIN 13..577
FT /note="UDENN"
FT /evidence="ECO:0000259|PROSITE:PS50211"
FT REGION 103..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 621..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 691..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 772..854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 911..935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1050..1190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..726
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..822
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..854
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..935
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1072..1128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1145..1169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1567 AA; 173203 MW; 46677CA44E900375 CRC64;
MEKKKMCPRL LDYLVVVGAR QPSSDSVAQT PQLLRRYPLE DHPDFPLPPD VVFFCQPEGC
LSIRQRRVSL RDDSSFVFTL TDKDSGTTRY GICVNFYRSF QRGHHRPRGD KSGHTETTAK
AAETTSEVSD GSSGESSTVL PASTSTESAP PPASGEQSEQ AGDELNSGKS PQHRRNAAKL
AARNRNSTLT SLCILSHYPF FSTFRECLYI LKRLVDCCSQ RLTQRAGLPR ATQRDTMWRV
FTGALSVEEK GSQLLADLRD IESWVYRLLR SPVPIASQRR VDVEVLPQEL KRALNFALPD
NSRFTLVDFP LHLPLELLGV DACLQVLSCV LLEHKVILQS RDYNALSMSV MAFVAMIYPL
EYMFPVIPLL PTCMASAEQL LLAPTPYIIG VPASFFLYKS DFKMPDDVWL VDLDSSKVIV
PTNAESLPPL PEPEAGELKK HLKQALASMS LNTQPILNLE KFQEGQEMSL LPPGRDKASP
SSTEFNPLIY GNDVDSVDVA TRVAMVRFFN SPNVLQGFQM HTRTLRLFPR PVVAFQSTSF
LASRPRRSLF ADKLSHTQAV EFYGEWALNP TNLAFQRIHN NVFDPSLIGD KPKWYAHQLQ
SVVYRVYDGG SQLVEAMAAP LEDEANDSDP TDSGSDSDGY DDSSSSYSSL GDLVSEMIQG
DIQGDTPNLD PPTHAALGDA SEVEFQDLRD GRNAEGPLSG DGAAEPSDGQ PLRSSSSTTA
SSSPSTIIQG VNHELGEVPE IEASASAALQ NPVPGVSSEQ FVRPAADAGL IDPANKKQEY
DNPYFEPQYG FPSEDDPDAE EQVESYTPRF IQNLNGNKAQ RPLRPSSLRL PGESDGEGDS
RNSSPNSTIS NSSNDGFGGL MSFASNLYKN HGTSFSLSNL ALPNKAAREK ATPFPSLKVP
PGARAPRALV DQKSSVIKHS PTVKRESPSP QGRINNTSEN QQFLKEVVQS VLDGQGVGWL
NMKKVRRLLE NEQLRVFVLS KLNRAVQSEE DARQEIIRDV EVSRKVYKGM LDILKCTVSS
LEQSYTNAGL GGMASVFSLL EIARTHYQTK GAEGAKQQRP QATDAEEKKS QISADSGLSV
ASGSQKSDTE SVTGSEPPIL TRSTSQDSEA STVISNSSGE TLGADSDLSS TAGDGLGGRT
APHLAQSRGT LSDSEIETNP ATSSVFGKTH TLKPGAKDHG PAVAKGPPAQ PMEDISMRIY
LCEGLLGRDK SSVWDQLEDA AMETFSLSKE RSTLWDQMQF WEDAYLDAVM LEREGMGMDQ
GPQEMIERYL SLGEHDRKRL EDDEDRLLAT LLHNMIAYML MLKVNKNDIR KKVRRLMGKS
HIGLTYSQEI NEILDKLANM NGRELSIRPS GSRHIKKQTF VVHAGTDTTG DIFFMEVCDD
CIVLRSNIGT VYERWWYEKL INMTYCPKTK VLCLWRRNGQ ETQLNKFYTK KCRELYYCVK
DSMERAAARQ QSIKPGPELG GEFPVQDMKT GEGGLLQVTL EGINLKFMHS QVFIELSHIK
KCNTVKGVFV LEEFVPETKE VVIHKYKTPM AHQICYSVLC LFSYVAAVKG KDADGKPKML
SPRPLPS
//
