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Database: UniProt
Entry: G1PEK3_MYOLU
LinkDB: G1PEK3_MYOLU
Original site: G1PEK3_MYOLU 
ID   G1PEK3_MYOLU            Unreviewed;       788 AA.
AC   G1PEK3;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   SubName: Full=MEFV innate immuity regulator, pyrin {ECO:0000313|Ensembl:ENSMLUP00000008951.2};
GN   Name=MEFV {ECO:0000313|Ensembl:ENSMLUP00000008951.2};
OS   Myotis lucifugus (Little brown bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC   Myotis.
OX   NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000008951.2, ECO:0000313|Proteomes:UP000001074};
RN   [1] {ECO:0000313|Ensembl:ENSMLUP00000008951.2, ECO:0000313|Proteomes:UP000001074}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSMLUP00000008951.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   EMBL; AAPE02021022; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; G1PEK3; -.
DR   STRING; 59463.ENSMLUP00000008951; -.
DR   Ensembl; ENSMLUT00000009819.2; ENSMLUP00000008951.2; ENSMLUG00000009793.2.
DR   eggNOG; KOG2177; Eukaryota.
DR   GeneTree; ENSGT00940000161955; -.
DR   HOGENOM; CLU_016050_0_0_1; -.
DR   InParanoid; G1PEK3; -.
DR   OMA; CQRHMKQ; -.
DR   TreeFam; TF351091; -.
DR   Proteomes; UP000001074; Unassembled WGS sequence.
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   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00024};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001074};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00024};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00024}.
FT   DOMAIN          1..92
FT                   /note="Pyrin"
FT                   /evidence="ECO:0000259|PROSITE:PS50824"
FT   DOMAIN          382..419
FT                   /note="B box-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50119"
FT   DOMAIN          587..782
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000259|PROSITE:PS50188"
FT   REGION          97..275
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          359..379
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        147..162
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        188..220
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        227..243
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        245..275
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   788 AA;  87846 MW;  A536DE7A036D8AB4 CRC64;
     MAKTPSDYLL HSLEELVPYD FEKFKFKLQN TSLEKEQQRI PRGLLPSARP VKLADLLLNH
     YGEKYAVQLT LQILRAMNQH LLAEELHRAI DPEYPIQESG TDCPAMSCSS GENKPKSLKM
     PDGLEGDRQQ QSGDGAASQP EAGKGPQKKP QGKRRDQKGS EGLDVQGKPG ARGGTLCSRR
     SPLPSKQPGE KGSDSSVRLR RNASSAGRLQ GLSSGSYAGS LGRKASEARS PSKKNRPRSL
     EFTISSRERA LSNLETLLPQ EKVRSENLDS SATPSKVATL DAGATMAVEK GSRNPEHSVT
     RRPQDEAVCP LSRAQEGDLV GSTCVRDSGS CSIASKDPKA SDGCLPNCLR CQVSLPGKSS
     GGIEPQEGPP MGSLSPTLQP QCTRHRKQVQ LLFCEDHREP ICLICSLSQE HRGHRVRPIE
     EAALEYKEQI QKELEHLKAL RRSGEEQRSE GDKNTANYLK QTEIQKQRVR CQMEQLCRFL
     EQQERLFVAW LEKLAQTIVQ VGETYDTQVS RDIALLTELI EELETKQRQP EWELMQDIGV
     TLRRVKTVTV PEPWATPLEV KEKIHLLLQK SEFVEKSMKH FSGTLRSEME TFNVPELIDA
     QTHAVNVVLD AETAHPNLII SDDLKSARLG NKWIHMPDSP ERFDSCIFAL GSPSFRSGRH
     YWEVEVGDKT GWVLGICKAS TSRKGNMTLS PENGYWVVMM MKRNEYQAST FPPTRLRMRE
     PPRRVGIFLD YKAGDISFYN VTAKSHIYTF TSFSFSGPLQ AIFSPGTHDG GKNMDPLTIC
     PVGDQGPH
//
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