ID A0A3Q7TEM6_VULVU Unreviewed; 1605 AA.
AC A0A3Q7TEM6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, 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_025859812.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025859812.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025859812.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025859812.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025859812.1};
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_025859812.1; XM_026004027.1.
DR STRING; 9627.ENSVVUP00000036395; -.
DR Proteomes; UP000286640; 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_025859812.1};
KW Membrane {ECO:0000256|ARBA:ARBA00022475};
KW Reference proteome {ECO:0000313|Proteomes:UP000286640};
KW Transferase {ECO:0000313|RefSeq:XP_025859812.1}.
FT DOMAIN 14..565
FT /note="UDENN"
FT /evidence="ECO:0000259|PROSITE:PS50211"
FT REGION 106..169
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 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..1060
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1114..1201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..169
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..1173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1605 AA; 178613 MW; FA2DB86D17161CA3 CRC64;
MVQKKKFCPR LLDYLVIVGA RHPSSDSVAQ TPELLRRYPL EDHAEFPLPP DVVFFCQPEG
CLSVRQRRMS LRDDTSFVFT LTDKDTGVTR YGICVNFYRS FQKRMPKDKG DGGAGSRGKE
GPRATCAPEE IGTESSESGL SLQPPSADSA PNVTQSPRGK PRAKTGSRSR NSTLTSLCVL
SHYPFFSTFR ECLYTLKRLV DCCSERLLGK KLGIPRGIQR DTMWRIFTGS LLVEEKSSAL
LHDLREIEAW IYRLLRSPVP VSGQKRVDIE VLPQELQQAL TFALPDPSRF TLVDFPLHLP
LELLGVDACL QVLTCILLEH KVVLQSRDYN ALSMSVMAFV AMIYPLEYMF PVIPLLPTCM
ASAEQLLLAP TPYIIGVPAS FFLYKLDFKM PDDVWLVDLD SNRVIAPTNA EMLPILPEPE
SLELKKHLKQ ALASMSLNTQ PILNLEKFHE GQEIPLLLGR PSNDLQSTPS TEFNPLIYGN
DVDSVDVATR VAMVRFFNSP NVLQGFQMHT RTLRLFPRPV VAFQAGSFLA SRPRQTPFAE
KLARTQAVEY FGEWILNPTN YAFQRIHNNM FDPALIGDKP KWYAHQLQPI HYRVYDSNSQ
LAEALSVPRE RDSDSDPTDD SGSDSMDYDD SSSSYSSLGD FVSEMMKCDI NGDTPNVDPL
THAALGDASE VEIDELQNQK ESEEPGPDSE NSQENPPLRS SSSTTASSSP STVIHGANSE
PADSTEVDDK AAVGVSKPPP TVPPSIGKSN VDRRQTEIGE GSVHRRTYDN PYFEPQYGFP
PEEEDDEQGE SYTPRFSQHV NGNRAQKMLR PNSLKLASDS DAESDSRASS PTSTVSNTST
EGFGGIMSFA SSLYRNHSTS FSLSNLTLPT KGAREKTTPF PSLKGNRRAL VDQKSSVIKH
SPTVKREPPS PQGRSSNSSE NQQFLKEVVH SVLDGQGVGW LNMKKVRRLL ESEQLRVFVL
SKLNRTVQSE DDAWQDVIPD VEISRKVYKG MLDLLKCTVL SLEQSYAHAG LGGMASIFGL
LEIAQTHYYS KEPDKRKRSP TESVNTPVGK DPGLAGRGDP KAMAQLRVPQ LGPRAPSAAG
KGPKELDTRS LKEENFVASV GPEVIKPVFD LGETEEKKSQ ISADSGVSLT SGSQRTDTDS
VIGVSPAVMI RSSSQDSEVS NSSGETLGAD SDLSSNAGDG PGGEGSTHLA SSRGTLSDSE
IETNSATSTI FGKAHSLKPS VKEKLVGSPV RSSEDVSQRV YLYEGLLGRD KGSMWDQLED
AAMETFSISK ERSTLWDQMQ FWEDAFLDAV MLEREGMGMD QGPQEMIDRY LSLGEHDRKR
LEDDEDRLLA TLLHNLISYM LLMKVNKNDI RKKVRRLMGK SHIGLVYSQQ INEVLDQLVN
LNGRDLSIRS SGSRHMKKQT FVVHAGTDTN GDIFFMEVCD DCVVLRSNIG TVYERWWYEK
LINMTYCPKT KVLCLWRRNG SETQLNKFYT KKCRELYYCV KDSMERAAAR QQSIKPGPEL
GGEFPVQDMK TGEGGLLQVT LEGINLKFMH NQVFIELNHI KKCNTVRGVF VLEEFVPEIK
EVVSHKYKTP MAHEICYSVL CLFSYVAAVR SSEEDLRTPP RPVSS
//
