ID M3YUM4_MUSPF Unreviewed; 785 AA.
AC M3YUM4;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE SubName: Full=MEFV innate immuity regulator, pyrin {ECO:0000313|Ensembl:ENSMPUP00000015034.1};
GN Name=MEFV {ECO:0000313|Ensembl:ENSMPUP00000015034.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000015034.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000015034.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
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DR EMBL; AEYP01027789; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; M3YUM4; -.
DR STRING; 9669.ENSMPUP00000015034; -.
DR Ensembl; ENSMPUT00000015271.1; ENSMPUP00000015034.1; ENSMPUG00000015143.1.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000161955; -.
DR HOGENOM; CLU_016050_0_0_1; -.
DR InParanoid; M3YUM4; -.
DR OMA; CQRHMKQ; -.
DR GO; GO:0061702; C:canonical inflammasome complex; IEA:Ensembl.
DR GO; GO:0005875; C:microtubule associated complex; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0003779; F:actin binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR GO; GO:1900016; P:negative regulation of cytokine production involved in inflammatory response; IEA:Ensembl.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:0032691; P:negative regulation of interleukin-1 beta production; IEA:Ensembl.
DR GO; GO:0032695; P:negative regulation of interleukin-12 production; IEA:Ensembl.
DR GO; GO:0071641; P:negative regulation of macrophage inflammatory protein 1 alpha production; IEA:Ensembl.
DR GO; GO:1900226; P:negative regulation of NLRP3 inflammasome complex assembly; IEA:Ensembl.
DR GO; GO:0010508; P:positive regulation of autophagy; IEA:Ensembl.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IEA:Ensembl.
DR GO; GO:1904270; P:pyroptosome complex assembly; IEA:Ensembl.
DR GO; GO:0034341; P:response to type II interferon; IEA:Ensembl.
DR CDD; cd19771; Bbox2_TRIM20; 1.
DR CDD; cd08321; Pyrin_ASC-like; 1.
DR CDD; cd15813; SPRY_PRY_TRIM20; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 1.10.533.10; Death Domain, Fas; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR003879; Butyrophylin_SPRY.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR004020; DAPIN.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR006574; PRY.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR000315; Znf_B-box.
DR PANTHER; PTHR24103; E3 UBIQUITIN-PROTEIN LIGASE TRIM; 1.
DR PANTHER; PTHR24103:SF606; PYRIN; 1.
DR Pfam; PF13765; PRY; 1.
DR Pfam; PF02758; PYRIN; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00589; PRY; 1.
DR SMART; SM01289; PYRIN; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF47986; DEATH domain; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50824; DAPIN; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00024};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00024};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00024}.
FT DOMAIN 1..91
FT /note="Pyrin"
FT /evidence="ECO:0000259|PROSITE:PS50824"
FT DOMAIN 374..416
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 584..783
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000259|PROSITE:PS50188"
FT REGION 99..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 420..483
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 151..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..274
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 785 AA; 88278 MW; EA73186A8E42D4E7 CRC64;
MIKTPSDHLL DSLEELGDND FEKFKFKLSI RLEKDHSRIP WGQLQNAKPV KLATLMITHY
GEENAARLTL QVLRAMNQNL LAEKLNRVIG PELLIQASGT DGSAMSCSSG ENKPKGLKIP
DGLKGDRQRQ NGDGVPGLPS SQQEAGRGPQ KKPPGKQRDQ KSSEGLDMLH KSRPRSMTLG
ARRSPLPSKP QGEKGSPSAR LPRNANSLGR LQELDSGSHT GSLGRIKPKI SEGHLPSGQK
RPRSLELNIF LGERETPKPE TLLSQDKMRS DHPDSAAAPS EVATLDVGAT VAPEKGSRNP
EHSMIWKPQD EAIYPPGRAQ ERDDSCRYSI ASRESKTSGK CSSSSLMHLA SLTVNNSEDY
KQQEGLHMAN LSPKSLPQCE RHMKQVQLLF CEDHREPICL ICSLSQEHRG HQVRPIEEAA
LEYKEQIQKQ LEHLKALRKS GEEQRSQGDK KTAKLLKQTE TQKQRLQHQL EQLYHHLQQQ
EKLFVASLED LSQTIGQVRE KYSTQVSRDI AHLDKLIGDL EAKQSQPEWQ LMQDIGVTLH
RVKIATVPKP WYTPPEVEKK IHLIYQKSEF MEKSMKSFRE TLRSEMDIFN IPELICAQAH
AVNVILDTET AHPNLIFSNN LKSVRLGNKW NRLPDNPERF DSCTIALGLP SFLSGRHYWE
VEVGNKTGWI LGICKASASR KGTMTLSANN GYWVVMMMKR NEYQVSTIPP TRLQIREAPK
RVGIFLDYMA GDISFYNVTY KSLIYTFTSF SFSGALQPMF SPGIHDGGKN MDPLTICPMA
DQRPQ
//
