ID A0A340X3A9_LIPVE Unreviewed; 1544 AA.
AC A0A340X3A9;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=MAP kinase-activating death domain protein {ECO:0000256|ARBA:ARBA00017868};
GN Name=MADD {ECO:0000313|RefSeq:XP_007455806.1};
OS Lipotes vexillifer (Yangtze river dolphin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Lipotidae; Lipotes.
OX NCBI_TaxID=118797 {ECO:0000313|Proteomes:UP000265300, ECO:0000313|RefSeq:XP_007455806.1};
RN [1] {ECO:0000313|RefSeq:XP_007455806.1}
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_007455806.1; XM_007455744.1.
DR GeneID; 103075914; -.
DR CTD; 8567; -.
DR OrthoDB; 24616at2759; -.
DR Proteomes; UP000265300; 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_007455806.1};
KW Membrane {ECO:0000256|ARBA:ARBA00022475};
KW Reference proteome {ECO:0000313|Proteomes:UP000265300};
KW Transferase {ECO:0000313|RefSeq:XP_007455806.1}.
FT DOMAIN 14..565
FT /note="UDENN"
FT /evidence="ECO:0000259|PROSITE:PS50211"
FT REGION 130..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 674..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 768..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 828..878
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 988..1014
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1066..1161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..719
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..799
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1078..1095
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1104..1133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1544 AA; 171071 MW; BFA45A2D8452C5A2 CRC64;
MVQKKKSCPR LLDYLVIVGA RHPSSDSVAQ TPELLRRYPL EDHAEFPLPP DVVFFCQPEG
CLSVRQRRMS LREDTSFVFT LTDKDTGVTR YGICVNFYRS FQKRMPKEKG EAGAGSRGKE
GPHATCISEE VGTQSSESGP SLQPPSADSI PDVNQSPRGK RRAKAESRSR NSTLTSLCVL
SHYPFFSAFR ECLYTLRRLV DCCSERLLGK KLGIPRGIQR DTVWRIFTGS LLVEEKSSAL
LHDLREIEAW IYRLLRSPVP VSGQKRVDIE VLPQELQQAL TFALPDPSRF TLVDFPLHLP
LELLGVDACL QVLTCILLEH KVVLQSRDYN ALSMSVMAFV AMIYPLEYMF PVIPLLPTCM
ASAEQLLLAP TPYIIGVPAS FFLYKLDFKM PDDVWLVDLD SSRVIAPTNA EVLPILPEPE
SLELKKHLKQ ALASMSLNTQ PILNLEKFHE GQDIPLLLGR PSNDLQSTPS TEFNPLIYGN
DVDSVDVATR VAMVRFFNSP NVLQGFQMHT RTLRLFPRPV VAFQAGSFLA SRPRQTPFAE
KLARTQAVEY FGEWILNPTN YAFQRIHNNT FDPALIGDKP KWYTHQLQPV HYRVYDSSSH
LAEALSVPPE HDSDSDPTDD SGSDSMDYDD SSSSYSSLGD FVSEMMKCDI NGDTPNVDPL
THVALGDASE VAVDELQSQK EAEEPGPDSE NSQENPPLRS SSSTTASSSP GTVIHGASSE
PADSTEMDDK AAVGVSRSLP SVPPSIGKAN VDRRQTEIGE GAQKLLRPNS LKLASDSDAE
SDSRASSPTS TVSNNSTEGF GGIMSFASSL YRNHSTSFSL SNLTLPTKGA REKTTPFPSL
KGNRRALVDQ KSSVIKHSPT VKREPPSPQG RSSNSSENQQ FLKEVVHSVL DGQGVGWLNT
KKVRRLLESE QLRVFVLSKL SRTVQSEDEA QQDIIPDVEI GRKVYKGMLD LLKCTVLSLE
QSYAHAGLGG MASIFALLEI AQTHYYSKEP DKRKRSPTES VNAPVGKDPG LAWRGDPKAM
AQLRVPQLGP RAPSASGKSP KELDARSLKE ENFVASVGPE VIKPTFDLGE TEEKKSQVSA
DSGVSLTSGP QRTDPDSVLG VSPAAMIRSS SQDSEVSTVS NSSGETLGAD SDLSSNAGDG
AGGEGSTHLA GSRGTLSDSE IETNSATSAI FGKAHSLKPS VKEKLVGSPV RFSEDVSQRV
YLYEGLLGKE RSTLWDQMQF WEDAFLDAVM LEREGMGMDQ GPQEMIDRYL SLGEHDRKRL
EDDEDRLLAT LLHNLISYML LMKVNKNDIR KKVRRLMGKS HIGLVYSQQI NEVLDQLANL
NGRDLSIRSS GSRHMKKQTF VVHAGTDTNG DIFFMEVCDD CVVLRSNIGT VYERWWYEKL
INMTYCPKTK VLCLWRRNGS ETQLNKFYTK KCRELYYCVK DSMERAAARQ QSIKPGPELG
GEFPVQDMKT GEGGLLQVTL EGINLKFMHN QVFIELNHIK KCNTVRGVFV LEEFVPEIKE
VVSHKYKTPM AHEICYSVLC LFSYVAAVRS SEEDLRTPPR PVSS
//
