ID A0A2K6BLJ9_MACNE Unreviewed; 1588 AA.
AC A0A2K6BLJ9;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=MAP kinase-activating death domain protein {ECO:0000256|ARBA:ARBA00017868};
GN Name=MADD {ECO:0000313|Ensembl:ENSMNEP00000012243.1};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000012243.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000012243.1}
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 RefSeq; XP_011722687.1; XM_011724385.1.
DR RefSeq; XP_011722688.1; XM_011724386.1.
DR Ensembl; ENSMNET00000036438.1; ENSMNEP00000012243.1; ENSMNEG00000030300.1.
DR GeneID; 105471682; -.
DR CTD; 8567; -.
DR GeneTree; ENSGT00940000156718; -.
DR OrthoDB; 24616at2759; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000030300; Expressed in pituitary gland and 12 other cell types or tissues.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000233120}.
FT DOMAIN 14..565
FT /note="UDENN"
FT /evidence="ECO:0000259|PROSITE:PS50211"
FT REGION 108..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 604..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 680..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 875..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1031..1090
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1116..1205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..156
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 793..808
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..842
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1121..1177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1588 AA; 176656 MW; DFE11341AD9791F7 CRC64;
MVQKKKFCPR LLDYLVIVGA RHPSSDSVAQ TPELLRRYPL EDHAEFPLPP DVVFFCQPEG
CLSVRQRRMS LRDDTSFVFT LTDKDTGVTR YGICVNFYRS FQKRIPKEKG EGGAGSHGKE
GTRATCASEE GGTESSESGS SQQPPSADST PDVNQSPRGK RRAKVGSRSR NSTLTSLCVL
SHYPFFSTFR ECLYTLKRLV DCCSERLLGK KLGIPRGVQR DTMWRIFTGS LLVEEKSSAL
LHDLREIEAW IYRLLRSPVP VSGQKRVDIE VLPQELQPAL TFALPDPSRF TLVDFPLHLP
LELLGVDACL QVLTCILLEH KVVLQSRDYN ALSMSVMAFV AMIYPLEYMF PVIPLLPTCM
ASAEQLLLAP TPYIIGVPAS FFLYKLDFKM PDDVWLVDLD SNRVIAPTNA EVLPILPEPE
SLELKKHLKQ ALASMSLNTQ PILNLEKFHE GQEIPLLLGR PSNDLQSTPS TEFNPLIYGN
DVDSVDVATR VAMVRFFNSA NVLQGFQMHT RTLRLFPRPV VAFQAGSFLA SRPRQTPFAE
KLARTQAVEY FGEWILNPTN YAFQRIHNNM FDPALIGDKP KWYAHQLQPI HYRVYDSNSQ
LAEALSVPPE RDSDSEPTDD SGSDSMDYDD SSSSYSSLGD FVSEMMKCDI NGDTPNVDPL
THAALGDASE VEIDELQNQK EAEEPGLDSE NSQENPPLRS SSSTTASSSP STIIHGANSE
PADSTEMDDK AAVGVSKPLP SVPPSIGKSN VDRRQAEIGE GSVRRRIYDN PYFEPQYGFP
PEEDEDEQGE SYTPRFSQHV SGNRAQKLLR PNSLRLASDS DAESDSRASS PNSTVSNTST
EGFGGIMSFA SSLYRNHSTS FSLSNLTLPT KGVREKATPF PSLKGNRRAL VDQKSSVIKH
SPTVKREPPS PQGRSSNSSE NQQFLKEVVH NVLDGQGVGW LNMKKVRRLL ESEQLRVFVL
SKLNRTVQSE DDARQDIIPD VEVSRKVYKG MLDLLKCTIL SLEQSYAHAG LGGMASIFGL
LEIAQTHYYS KEPDKRKRSP TESVNTPVGK DPGLAGRGDP KAMAQLRVPQ VGPRAPSATG
KGPKELDTRS LKEENFIASI GPEVIKPVFD LGETEEKKSQ ISADSGVSLT SSSQRTDQDS
VISVSPAVMI RSSSQDSEVS TVVSNSSGET LGADSDLSSN AGDGPGGEGS VHLASSRGTL
SDSEIETNSA TSTIFGKAHS LKPSVKEKLA GSPIRTSEDV SQRVYLYEGL LGKERSTLWD
QMQFWEDAFL DAVMLEREGM GMDQGPQEMI DRYLSLGEHD RKRLEDDEDR LLATLLHNLI
SYMLLMKVNK NDIRKKVRRL MGKSHIGLVY SQQINEVLDQ LANLNGRDLS IWSSGSRHMK
KQTFVVHAGT DTNGDIFFME VCDDCVVLRS NIGTVYERWW YEKLINMTYC PKTKVLCLWR
RNGSETQLNK FYTKKCRELY YCVKDSMERA AARQQSIKPG PELGGEFPVQ DMKTGEGGLL
QVTLEGINLK FMHNQVFIEL NHIKKCNTVR GVFVLEEFVP EIKEVVSHKY KTPMAHEICY
SVLCLFSYVA AVRSSEEDLR TPPRPVSS
//
