ID A0A2Y9PXA0_DELLE Unreviewed; 1630 AA.
AC A0A2Y9PXA0;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=MAP kinase-activating death domain protein {ECO:0000256|ARBA:ARBA00017868};
GN Name=MADD {ECO:0000313|RefSeq:XP_022447743.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022447743.1};
RN [1] {ECO:0000313|RefSeq:XP_022447743.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022447743.1};
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_022447743.1; XM_022592035.1.
DR Proteomes; UP000248483; 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_022447743.1};
KW Membrane {ECO:0000256|ARBA:ARBA00022475};
KW Reference proteome {ECO:0000313|Proteomes:UP000248483};
KW Transferase {ECO:0000313|RefSeq:XP_022447743.1}.
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..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 677..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 871..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1031..1057
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1071..1090
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1124..1222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..154
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 1124..1138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1139..1156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1165..1195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1630 AA; 181564 MW; B5616733F6649E22 CRC64;
MVQKKKSCPR LLDYLVIVGA RHPSSDSVAQ TPELLRRYPL EDHAEFPLPP DVVFFCQPEG
CLSVRQRRMS LREDTSFVFT LTDKDTGVTR YGICVNFYRS FQKRVPKEKG EAGAGSRGKE
GPHATCISEE VGTESSESGP SLQPPSADST PDVNQSPRGK HRAKAESRSR NSTLTSLCVL
SHYPFFSTFR ECLYTLKRLV DCCSERLLGK KLGIPRGIQR DTMWRIFTGS LLVEEKSSAL
LHDLREIEAW IYRLLRSPVP VSGQKRVDIE VLPQELQQAL TFALPDPSRF TLVDFPLHLP
LELLGVDACL QVLTCILLEH KVVLQSRDYN ALSMSVMAFV AMIYPLEYMF PVIPLLPTCM
ASAEQLLLAP TPYIIGVPAS FFLYKLDFKM PDDVWLVDLD SSRVIAPTNA EVLPILPEPE
SLELKKHLKQ ALASMSLNTQ PILNLEKFHE GQEIPLLLGR PSNDLQSTPS TEFNPLIYGN
DVDSVDVATR VAMVRFFNSP NVLQGFQMHT RTLRLFPRPV VAFQAGSFLA SRPRQTPFAE
KLARTQAVEY FGEWILNPTN YAFQRIHNNT FDPALIGDKP KWYTHQLQPV HYRVYDSSSH
LAEALSVPPE HDSDSDPTDD SGSDSMDYDD SSSSYSSLGD FVSEMMKCDI NGDTPNVDPL
THAALGDASE VAIDELQSQK EAEEPGPDSE NSQENPPLRS SSSTTASSSP STVIHGASSE
PADSTEMDDK AAVGVSKSLP SVPPSTGKAN VDRRQTEIGE GSVRRRTYEN PYFEPQYGFP
PEEDDDEQGE SYTPRCSQHV SGNRAQKLLR PNSLKLASDS DAESDSRASS PTSTVSNNST
EGFGGIMSFA SSLYRNHSTS FSLSNLTLPT KGAREKTTPF PSLKGNRRAL VDQKSSVIKH
SPTVKREPPS PQGRSSNSSE NQQFLKEVVH SVLDGQGVGW LNTKKVRRLL ESEQLRVFVL
SKLSRTVQSE DEAQQDIIPD VEVGRKVYKG MLDLLKCTVL SLEQSYAHAG LGGMASIFAL
LEIAQTHYYS KEPDKRKRSP TESVNTPIGK DPGLAWRGDP KAMAQLRVPQ LGPRAPSASG
KSPKELDTRS LKEENFVASI ELWNKHQEVK KQKALEKQRP EVIKPTFDLG ETEEKKSQVS
ADSGVSLTSG PQRTDPDSVL GVSPAVMIRS SSQDSEVSTV VSNSSGETLG ADSDLSSNAA
DGPGGEGGTH LAGSRGTLSD SEIETNSATS AIFGKAHNLK PSVKEKLVGS PVRFSEDVSQ
RVYLYEGLLG RDKGSMWDQL EDAAMETFSI SKERSTLWDQ MQFWEDAFLD AVMLEREGMG
MDQGPQEMID RYLSLGEHDR KRLEDDEDRL LATLLHNLIS YMLLMKVNKN DIRKKVRRLM
GKSHIGLVYS QQINEVLDQL ANLNGRDLSI RSSGSRHMKK QTFVVHAGTD TNGDIFFMEV
CDDCVVLRSN IGTVYERWWY EKLINMTYCP KTKVLCLWRR NGSETQLNKF YTKKCRELYY
CVKESMERAA ARQQSVRPGP ELGGEFPVQD MKTGEGGLLQ VTLEGINLKF MHNQERKVFI
ELNHIKKCNT VRGVFVLEEF VPEIKEVVSH KYKTPMAHEI CYSVLCLFSY VAAVRSSEED
LRTPPRPVSS
//
