ID A0A3Q7SSP7_VULVU Unreviewed; 1628 AA.
AC A0A3Q7SSP7;
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_025859808.1};
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_025859808.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025859808.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025859808.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025859808.1};
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_025859808.1; XM_026004023.1.
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_025859808.1};
KW Membrane {ECO:0000256|ARBA:ARBA00022475};
KW Reference proteome {ECO:0000313|Proteomes:UP000286640};
KW Transferase {ECO:0000313|RefSeq:XP_025859808.1}.
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 913..941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1051..1080
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1134..1221
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 1141..1193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1628 AA; 181030 MW; 5EE8AB7D59B371C1 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 PSLKVFGLNT LMEIVTEAGP
GSGEGNRRAL 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 NQERKVFIEL
NHIKKCNTVR GVFVLEEFVP EIKEVVSHKY KTPMAHEICY SVLCLFSYVA AVRSSEEDLR
TPPRPVSS
//
