ID A0A3B4HBM4_9CICH Unreviewed; 1586 AA.
AC A0A3B4HBM4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=MAP kinase-activating death domain protein {ECO:0000256|ARBA:ARBA00017868};
GN Name=MADD {ECO:0000313|Ensembl:ENSPNYP00000032089.1};
OS Pundamilia nyererei.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000032089.1, ECO:0000313|Proteomes:UP000261460};
RN [1] {ECO:0000313|Ensembl:ENSPNYP00000032089.1}
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 Ensembl; ENSPNYT00000032859.1; ENSPNYP00000032089.1; ENSPNYG00000024217.1.
DR GeneTree; ENSGT00940000156718; -.
DR Proteomes; UP000261460; 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 12..597
FT /note="UDENN"
FT /evidence="ECO:0000259|PROSITE:PS50211"
FT REGION 104..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 639..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 802..876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 911..956
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1068..1099
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1137..1259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..749
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..845
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 860..876
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 935..956
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1160..1216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1231..1257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1586 AA; 175780 MW; F283F1C9CA60C2AD CRC64;
MEKKKMCPRL LDYLVVVGAR QPTSDSVAQT PQLLRRYPLE DHQDFPLPPD VVFFCQPEGC
LSIRQRRVSL RDDSSFVFTL TDKDSGITRY GICVNFYRSF QRGHHRTRGE KSSHAETAER
ATETTSEGSD SGGGGVPHSV VSPPKNAESV PPPASGEEGG QQGAEQNAGK SPQHKRSAAK
VAARNRNSTL TSLCILSHYP FFSTFRECLY ILKRLVDCCS QRLTQRAGLP RATQRDTMWR
VFTGALSVEE KGSQLLADLR EIESWVYRLL RSPVPVAGQR RVDVEVLPHE LKRPLTFALP
DSSRFSMVDF PLHLPLELLG VDACLQVLSC VLLEHKVILQ SRDYNALSMS VMAFVAMIYP
LEYMFPVIPL LPTCMASAEQ LLLAPTPYII GVPASFFLYK SDFKMPDDIW LVDLDSSKVI
APTNAELLPP LPEPEAGELK KHLKQCLVRL TVITQKQIFS SENKALTSMS LNTQPILNLE
KFQEGQEMPL LPPGRDKASP SSTEFNPLIY GNDVDSVDVA TRVAMVRFFN SPNVLQGFQM
HTRTLRLFPR PVVAFQSTSF LASRPRRSTF ADKLSHTQAV EFYGEWALNP TNLAFQRIHN
NVFDPSLIGD KPKWYAHQLQ PVVYRVYDGS SQLVEAMAGP LEDEGNESDP TDSGSDSEAY
DDSSSSYSSL GDLVSEMIQG DIQGDTPSLD PPTHAALGDA SEVEFQDYHD FREGHGSEGP
PSGDGPAEPS DGQPLRSSSS TTASSSPSTI IQGVNHEQGE VPEIEASASA ALQNPVPGLA
NQPFLRPAAD AGLVEQANKK QEYDNPYFEP QYGFPSEDDP DAEEQVESYT PRFNQNLNGN
KAQRPLRPSS LRLPGESDGE GDSRNSSPNS TISNNSNDGF GGLMSFASNL YKNHGTSFSL
SNLALPNKAA REKSTPFPSL KGARAPRALV DQKSSVIKHS PTVKRESPSP QGRVNNTSEN
QQFLKEVVQS VLDGQGVGWL NMKKVRRLLE NEQLRVFVLS KLNRAVQSEE DARQEIIRDV
EVNRKVYKGM LDILKCTVSS LEHSYTNAGL GGMASVFSLL EIARTHYQTK DPEKRKRSPT
DSAGSPGSKE SPSGRMETAR PQGLLNIPHL QLPHHTTGKG ARHFDTRSLN EENFIASIGS
EGAKQQRPQV TDAEEKKSQI SADSGLSVTS GSQKSDTESV ASSEPPILTR STSQDSEAST
VISNSSGETL GADSDLSSTA GDGLGGRTAP HLTQSRGTLS DSEIETNPAT SSVFGKTHTL
KPGVKDHLPA LAKGLPAQPI EDTSMRIYLF EGLLGRDKSS VWDQLEDAAM ETFSLSKERS
TLWDQVQFWE DAFLDAVMLE REGMGMDQGP QEMIERYLSL GEHDRKRLED DEDRLLATLL
HNMIAYMLMM KVSKNDIRKK VRRLMGKSHI GLTYSQEINE ILDKLAQMNG RELSIRPSGS
RHIKKQTFVV HAGTDTTGDI FFMEVCDDCI VLRSNIGTVY ERWWYEKLIN MTYCPKTKVL
CLWRRNGQET QLNKFYTKKC RELYYCVKDS MERAAARQQS IKPGPELGGE FPVQDMKTGE
GGLLQVTLEG INLKFMHSQF LKLKKW
//