ID PPIP1_HUMAN Reviewed; 416 AA. AC O43586; B5BU74; B5BUK4; O43585; O95657; DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 09-DEC-2015, entry version 138. DE RecName: Full=Proline-serine-threonine phosphatase-interacting protein 1; DE Short=PEST phosphatase-interacting protein 1; DE AltName: Full=CD2-binding protein 1; DE AltName: Full=H-PIP; GN Name=PSTPIP1; Synonyms=CD2BP1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, INTERACTION RP WITH CD2 AND PTPN12, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=9857189; DOI=10.1093/emboj/17.24.7320; RA Li J., Nishizawa K., An W., Hussey R.E., Lialios F.E., Salgia R., RA Sunder-Plassmann R., Reinherz E.L.; RT "A cdc15-like adaptor protein (CD2BP1) interacts with the CD2 RT cytoplasmic domain and regulates CD2-triggered adhesion."; RL EMBO J. 17:7320-7336(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS HIS-48; LYS-106; RP HIS-146; LEU-149; SER-151; ASP-155 AND HIS-156. RA Wilson L.A., Fields D., Cruz L., Lasky L., Friesen J., RA Siminovitch K.A.; RT "The human homologue of mouse PTP-PIP interactor protein."; RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=19054851; DOI=10.1038/nmeth.1273; RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B., RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., RA Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., RA Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., RA Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., RA Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., RA Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., RA Isogai T., Imai J., Watanabe S., Nomura N.; RT "Human protein factory for converting the transcriptome into an in RT vitro-expressed proteome."; RL Nat. Methods 5:1011-1017(2008). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP INTERACTION WITH MEFV, TISSUE SPECIFICITY, CHARACTERIZATION OF RP VARIANTS PAPAS THR-230 AND GLN-250, AND MUTAGENESIS OF TRP-232 AND RP TYR-345. RX PubMed=14595024; DOI=10.1073/pnas.2135380100; RA Shoham N.G., Centola M., Mansfield E., Hull K.M., Wood G., Wise C.A., RA Kastner D.L.; RT "Pyrin binds the PSTPIP1/CD2BP1 protein, defining familial RT Mediterranean fever and PAPA syndrome as disorders in the same RT pathway."; RL Proc. Natl. Acad. Sci. U.S.A. 100:13501-13506(2003). RN [7] RP FUNCTION, SUBUNIT, INTERACTION WITH MEFV, AND CHARACTERIZATION OF RP VARIANTS THR-230 AND GLN-250. RX PubMed=17964261; DOI=10.1016/j.molcel.2007.08.029; RA Yu J.W., Fernandes-Alnemri T., Datta P., Wu J., Juliana C., RA Solorzano L., McCormick M., Zhang Z., Alnemri E.S.; RT "Pyrin activates the ASC pyroptosome in response to engagement by RT autoinflammatory PSTPIP1 mutants."; RL Mol. Cell 28:214-227(2007). RN [8] RP FUNCTION, INTERACTION WITH DNM2, AND SUBCELLULAR LOCATION. RX PubMed=18480402; DOI=10.1091/mbc.E08-02-0225; RA Cooper K.M., Bennin D.A., Huttenlocher A.; RT "The PCH family member proline-serine-threonine phosphatase- RT interacting protein 1 targets to the leukocyte uropod and regulates RT directed cell migration."; RL Mol. Biol. Cell 19:3180-3191(2008). RN [9] RP INTERACTION WITH FASLG. RX PubMed=19807924; DOI=10.1186/1471-2172-10-53; RA Voss M., Lettau M., Janssen O.; RT "Identification of SH3 domain interaction partners of human FasL RT (CD178) by phage display screening."; RL BMC Immunol. 10:53-53(2009). RN [10] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MEFV. RX PubMed=19109554; DOI=10.3181/0806-RM-184; RA Waite A.L., Schaner P., Hu C., Richards N., Balci-Peynircioglu B., RA Hong A., Fox M., Gumucio D.L.; RT "Pyrin and ASC co-localize to cellular sites that are rich in RT polymerizing actin."; RL Exp. Biol. Med. (Maywood) 234:40-52(2009). RN [11] RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS RP THR-230 AND GLN-250, AND MUTAGENESIS OF TRP-232 AND ASP-266. RX PubMed=19584923; DOI=10.1371/journal.pone.0006147; RA Waite A.L., Schaner P., Richards N., Balci-Peynircioglu B., RA Masters S.L., Brydges S.D., Fox M., Hong A., Yilmaz E., Kastner D.L., RA Reinherz E.L., Gumucio D.L.; RT "Pyrin Modulates the Intracellular Distribution of PSTPIP1."; RL PLoS ONE 4:E6147-E6147(2009). RN [12] RP STRUCTURE BY NMR OF 358-416. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the SH3 domain of the human proline-serine- RT threonine phosphatase-interacting protein 1."; RL Submitted (FEB-2007) to the PDB data bank. RN [13] RP VARIANTS PAPAS THR-230 AND GLN-250, AND CHARACTERIZATION OF VARIANTS RP PAPAS THR-230 AND GLN-250. RX PubMed=11971877; DOI=10.1093/hmg/11.8.961; RA Wise C.A., Gillum J.D., Seidman C.E., Lindor N.M., Veile R., RA Bashiardes S., Lovett M.; RT "Mutations in CD2BP1 disrupt binding to PTP PEST and are responsible RT for PAPA syndrome, an autoinflammatory disorder."; RL Hum. Mol. Genet. 11:961-969(2002). RN [14] RP VARIANTS PAPAS THR-230; GLN-250 AND LYS-250. RX PubMed=22161697; DOI=10.1002/art.34332; RA Demidowich A.P., Freeman A.F., Kuhns D.B., Aksentijevich I., RA Gallin J.I., Turner M.L., Kastner D.L., Holland S.M.; RT "Brief report: genotype, phenotype, and clinical course in five RT patients with PAPA syndrome (pyogenic sterile arthritis, pyoderma RT gangrenosum, and acne)."; RL Arthritis Rheum. 64:2022-2027(2012). CC -!- FUNCTION: Involved in regulation of the actin cytoskeleton. May CC regulate WAS actin-bundling activity. Bridges the interaction CC between ABL1 and PTPN18 leading to ABL1 dephosphorylation. May CC play a role as a scaffold protein between PTPN12 and WAS and allow CC PTPN12 to dephosphorylate WAS. Has the potential to physically CC couple CD2 and CD2AP to WAS. Acts downstream of CD2 and CD2AP to CC recruit WAS to the T-cell:APC contact site so as to promote the CC actin polymerization required for synapse induction during T-cell CC activation (By similarity). Down-regulates CD2-stimulated adhesion CC through the coupling of PTPN12 to CD2. Also has a role in innate CC immunity and the inflammatory response. Recruited to inflammasomes CC by MEFV. Induces formation of pyroptosomes, large supramolecular CC structures composed of oligomerized PYCARD dimers which form prior CC to inflammatory apoptosis. Binding to MEFV allows MEFV to bind to CC PYCARD and facilitates pyroptosome formation. Regulates CC endocytosis and cell migration in neutrophils. {ECO:0000250, CC ECO:0000269|PubMed:17964261, ECO:0000269|PubMed:18480402, CC ECO:0000269|PubMed:19109554, ECO:0000269|PubMed:19584923, CC ECO:0000269|PubMed:9857189}. CC -!- SUBUNIT: Homodimer (PubMed:19584923). Homotrimer CC (PubMed:17964261). Interacts (via coiled-coil domain) with CD2AP, CC PTPN12 and PTPN18. Interacts (via SH3 domain) with ABL1 and WAS. CC Interacts (via SH3 and coiled-coil domains) with MEFV (via B-box CC zinc finger); the interaction allows binding of MEFV to PYCARD and CC facilitates formation of PYCARD pyroptosomes. Interacts with CD2, CC DNM2 and FASLG. {ECO:0000269|PubMed:14595024, CC ECO:0000269|PubMed:17964261, ECO:0000269|PubMed:18480402, CC ECO:0000269|PubMed:19109554, ECO:0000269|PubMed:19584923, CC ECO:0000269|PubMed:19807924, ECO:0000269|PubMed:9857189}. CC -!- INTERACTION: CC O43684:BUB3; NbExp=3; IntAct=EBI-1050964, EBI-1050987; CC Q86YD7:FAM90A1; NbExp=3; IntAct=EBI-1050964, EBI-6658203; CC P48023:FASLG; NbExp=5; IntAct=EBI-1050964, EBI-495538; CC Q96D16:FBXL18; NbExp=3; IntAct=EBI-1050964, EBI-744419; CC Q9Y4Z0:LSM4; NbExp=3; IntAct=EBI-1050964, EBI-372521; CC Q9Y5E9:PCDHB14; NbExp=3; IntAct=EBI-1050964, EBI-10329013; CC F1T0A5:PRPF31; NbExp=3; IntAct=EBI-1050964, EBI-10177194; CC Q99952:PTPN18; NbExp=4; IntAct=EBI-1050964, EBI-1384210; CC Q9Y2R2:PTPN22; NbExp=6; IntAct=EBI-1050964, EBI-1211241; CC Q14D33:RTP5; NbExp=3; IntAct=EBI-1050964, EBI-10217913; CC O00560:SDCBP; NbExp=3; IntAct=EBI-1050964, EBI-727004; CC Q9H788:SH2D4A; NbExp=3; IntAct=EBI-1050964, EBI-747035; CC Q9UQ90:SPG7; NbExp=3; IntAct=EBI-1050964, EBI-717201; CC Q9Y228:TRAF3IP3; NbExp=3; IntAct=EBI-1050964, EBI-765817; CC O75386:TULP3; NbExp=3; IntAct=EBI-1050964, EBI-5357290; CC Q96B02:UBE2W; NbExp=4; IntAct=EBI-1050964, EBI-716589; CC Q9Y473:ZNF175; NbExp=3; IntAct=EBI-1050964, EBI-3438881; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Cell CC projection, lamellipodium {ECO:0000250}. Cell projection, CC uropodium. Cytoplasm, perinuclear region {ECO:0000250}. Cleavage CC furrow {ECO:0000250}. Note=During interphase, colocalizes with F- CC actin in the cortical cytoskeleton, lamellipodia, and stress CC fibers. In dividing cells, colocalizes with the F-actin rich CC cytokinetic cleavage furrow. Colocalized with WAS to filamentous CC structures within the cytoplasm. Colocalized with PTPN12 in the CC cytoplasm and the perinuclear region. Colocalized with CD2AP and CC WAS in the actin cytoskeleton. Colocalized with CD2, CD2AP and WAS CC at the site of T-cell:APC contact (By similarity). In monocytes, CC forms a branched filamentous network in the cytoplasm. In CC migrating neutrophils, localizes most strongly to the trailing CC edge of the uropod where it colocalizes with PIP5K1C. In CC transfected cells, forms relatively straight filaments radiating CC out from the nucleus. Colocalizes with MEFV, particularly at the CC branch point of filaments. Filament formation requires an intact CC tubulin cytoskeleton. {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=CD2BP1L; CC IsoId=O43586-1; Sequence=Displayed; CC Name=2; Synonyms=CD2BP1S; CC IsoId=O43586-2; Sequence=VSP_015627; CC -!- TISSUE SPECIFICITY: Highly expressed in the peripheral blood CC leukocytes, granulocytes and monocytes, namely in T-cells and CC natural killer cells, and in spleen. Weakly expressed in the CC thymus, small intestine, lung and placenta. CC {ECO:0000269|PubMed:14595024, ECO:0000269|PubMed:9857189}. CC -!- DOMAIN: The F-BAR domain is important for filament formation. The CC SH3 domain is not required for filament formation or localization CC to the uropod. CC -!- PTM: Dephosphorylated on Tyr-345 by PTPN18, this event negatively CC regulates the association of PSTPIP1 with SH2 domain-containing CC proteins as tyrosine kinase. Phosphorylation of Tyr-345 is CC probably required for subsequent phosphorylation at other tyrosine CC residues. Phosphorylation is induced by activation of the EGFR and CC PDGFR in a ABL1 dependent manner. The phosphorylation regulates CC the interaction with WAS and with MEFV (By similarity). CC {ECO:0000250}. CC -!- DISEASE: PAPA syndrome (PAPAS) [MIM:604416]: Characterized by CC autosomal dominant inheritance of early-onset, primarily affecting CC skin and joint tissues. Recurring inflammatory episodes lead to CC accumulation of sterile, pyogenic, neutrophil-rich material within CC the affected joints, ultimately resulting in significant CC destruction. {ECO:0000269|PubMed:11971877, CC ECO:0000269|PubMed:22161697}. Note=The disease is caused by CC mutations affecting the gene represented in this entry. CC -!- SIMILARITY: Contains 1 F-BAR domain. {ECO:0000255|PROSITE- CC ProRule:PRU01077}. CC -!- SIMILARITY: Contains 1 SH3 domain. {ECO:0000255|PROSITE- CC ProRule:PRU00192}. CC -!- WEB RESOURCE: Name=INFEVERS; Note=Repertory of FMF and hereditary CC autoinflammatory disorders mutations; CC URL="http://fmf.igh.cnrs.fr/ISSAID/infevers/search.php?n=5"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF038602; AAD11958.1; -; mRNA. DR EMBL; AF038603; AAD11959.1; -; mRNA. DR EMBL; U94778; AAD00762.1; -; mRNA. DR EMBL; AB451310; BAG70124.1; -; mRNA. DR EMBL; AB451440; BAG70254.1; -; mRNA. DR EMBL; CH471136; EAW99213.1; -; Genomic_DNA. DR EMBL; BC008602; AAH08602.1; -; mRNA. DR CCDS; CCDS45312.1; -. [O43586-1] DR RefSeq; NP_003969.2; NM_003978.3. [O43586-1] DR UniGene; Hs.129758; -. DR PDB; 2DIL; NMR; -; A=361-416. DR PDBsum; 2DIL; -. DR ProteinModelPortal; O43586; -. DR SMR; O43586; 9-265, 328-416. DR BioGrid; 114513; 51. DR IntAct; O43586; 22. DR MINT; MINT-1130527; -. DR STRING; 9606.ENSP00000452746; -. DR PhosphoSite; O43586; -. DR BioMuta; PSTPIP1; -. DR MaxQB; O43586; -. DR PaxDb; O43586; -. DR PRIDE; O43586; -. DR DNASU; 9051; -. DR Ensembl; ENST00000558012; ENSP00000452746; ENSG00000140368. [O43586-1] DR Ensembl; ENST00000559295; ENSP00000452743; ENSG00000140368. [O43586-2] DR GeneID; 9051; -. DR KEGG; hsa:9051; -. DR UCSC; uc002bcf.2; human. [O43586-1] DR UCSC; uc010bkw.1; human. [O43586-2] DR CTD; 9051; -. DR GeneCards; PSTPIP1; -. DR HGNC; HGNC:9580; PSTPIP1. DR HPA; HPA010600; -. DR MalaCards; PSTPIP1; -. DR MIM; 604416; phenotype. DR MIM; 606347; gene. DR neXtProt; NX_O43586; -. DR Orphanet; 69126; Pyogenic arthritis - pyoderma gangrenosum - acne. DR PharmGKB; PA33931; -. DR eggNOG; ENOG410IU8N; Eukaryota. DR eggNOG; ENOG410XR8X; LUCA. DR GeneTree; ENSGT00800000124090; -. DR HOGENOM; HOG000294218; -. DR HOVERGEN; HBG052960; -. DR InParanoid; O43586; -. DR KO; K12804; -. DR OMA; VQEMQGN; -. DR PhylomeDB; O43586; -. DR TreeFam; TF313677; -. DR Reactome; R-HSA-844456; The NLRP3 inflammasome. DR SignaLink; O43586; -. DR EvolutionaryTrace; O43586; -. DR GeneWiki; PSTPIP1; -. DR GenomeRNAi; 9051; -. DR NextBio; 33911; -. DR PRO; PR:O43586; -. DR Proteomes; UP000005640; Chromosome 15. DR Bgee; O43586; -. DR CleanEx; HS_PSTPIP1; -. DR ExpressionAtlas; O43586; baseline and differential. DR Genevisible; O43586; HS. DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0001931; C:uropod; IEA:UniProtKB-SubCell. DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc. DR GO; GO:0016477; P:cell migration; IEA:InterPro. DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW. DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW. DR GO; GO:0045087; P:innate immune response; TAS:Reactome. DR GO; GO:0035872; P:nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway; TAS:Reactome. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR InterPro; IPR031160; F_BAR. DR InterPro; IPR001060; FCH_dom. DR InterPro; IPR030777; PSTPIP1. DR InterPro; IPR001452; SH3_domain. DR InterPro; IPR013315; Spectrin_alpha_SH3. DR PANTHER; PTHR23065:SF3; PTHR23065:SF3; 1. DR Pfam; PF00611; FCH; 1. DR Pfam; PF14604; SH3_9; 1. DR PRINTS; PR00452; SH3DOMAIN. DR PRINTS; PR01887; SPECTRNALPHA. DR SMART; SM00055; FCH; 1. DR SMART; SM00326; SH3; 1. DR SUPFAM; SSF50044; SSF50044; 1. DR PROSITE; PS51741; F_BAR; 1. DR PROSITE; PS50002; SH3; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell adhesion; Cell projection; KW Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; KW Disease mutation; Endocytosis; Immunity; Inflammatory response; KW Innate immunity; Phosphoprotein; Polymorphism; Reference proteome; KW SH3 domain. FT CHAIN 1 416 Proline-serine-threonine phosphatase- FT interacting protein 1. FT /FTId=PRO_0000058539. FT DOMAIN 5 264 F-BAR. {ECO:0000255|PROSITE- FT ProRule:PRU01077}. FT DOMAIN 359 416 SH3. {ECO:0000255|PROSITE- FT ProRule:PRU00192}. FT COILED 166 212 {ECO:0000255}. FT MOD_RES 318 318 Phosphoserine. FT {ECO:0000250|UniProtKB:P97814}. FT VAR_SEQ 280 309 APVPYQNYYDREVTPLTSSPGIQPSCGMIK -> GEVRLAD FT SAAS (in isoform 2). FT {ECO:0000303|PubMed:9857189}. FT /FTId=VSP_015627. FT VARIANT 48 48 Q -> H (in dbSNP:rs1141038). FT {ECO:0000269|Ref.2}. FT /FTId=VAR_023515. FT VARIANT 106 106 E -> K (in dbSNP:rs1141039). FT {ECO:0000269|Ref.2}. FT /FTId=VAR_023516. FT VARIANT 146 146 Q -> H (in dbSNP:rs1141041). FT {ECO:0000269|Ref.2}. FT /FTId=VAR_023517. FT VARIANT 149 149 R -> L (in dbSNP:rs1141042). FT {ECO:0000269|Ref.2}. FT /FTId=VAR_023518. FT VARIANT 151 151 A -> S (in dbSNP:rs1141043). FT {ECO:0000269|Ref.2}. FT /FTId=VAR_023519. FT VARIANT 155 155 E -> D (in dbSNP:rs1141044). FT {ECO:0000269|Ref.2}. FT /FTId=VAR_023520. FT VARIANT 156 156 Q -> H (in dbSNP:rs1141045). FT {ECO:0000269|Ref.2}. FT /FTId=VAR_023521. FT VARIANT 230 230 A -> T (in PAPAS; severely reduced FT binding with PTPN12; markedly increased FT binding to MEFV; accentuates IL1B FT secretion; no effect on filament FT formation; increased induction of MEFV in FT response to retroviral infection; FT dbSNP:rs28939381). FT {ECO:0000269|PubMed:11971877, FT ECO:0000269|PubMed:14595024, FT ECO:0000269|PubMed:17964261, FT ECO:0000269|PubMed:19584923, FT ECO:0000269|PubMed:22161697}. FT /FTId=VAR_023522. FT VARIANT 250 250 E -> K (in PAPAS). FT {ECO:0000269|PubMed:22161697}. FT /FTId=VAR_070635. FT VARIANT 250 250 E -> Q (in PAPAS; severely reduced FT binding with PTPN12; markedly increased FT binding to MEFV; accentuates IL1B FT secretion; increased induction of MEFV in FT response to retroviral infection; FT dbSNP:rs28939089). FT {ECO:0000269|PubMed:11971877, FT ECO:0000269|PubMed:14595024, FT ECO:0000269|PubMed:17964261, FT ECO:0000269|PubMed:19584923, FT ECO:0000269|PubMed:22161697}. FT /FTId=VAR_023523. FT MUTAGEN 232 232 W->A: Abolishes binding to MEFV. FT Cytoplasmic filaments are finer with FT fewer branches. FT {ECO:0000269|PubMed:14595024, FT ECO:0000269|PubMed:19584923}. FT MUTAGEN 266 266 D->N: No effect on filament formation. FT {ECO:0000269|PubMed:19584923}. FT MUTAGEN 345 345 Y->F: Decreases binding to MEFV. FT {ECO:0000269|PubMed:14595024}. FT CONFLICT 367 367 L -> F (in Ref. 2; AAD00762). FT {ECO:0000305}. FT STRAND 363 365 {ECO:0000244|PDB:2DIL}. FT STRAND 373 377 {ECO:0000244|PDB:2DIL}. FT STRAND 385 390 {ECO:0000244|PDB:2DIL}. FT STRAND 393 401 {ECO:0000244|PDB:2DIL}. FT STRAND 404 409 {ECO:0000244|PDB:2DIL}. FT HELIX 410 412 {ECO:0000244|PDB:2DIL}. SQ SEQUENCE 416 AA; 47591 MW; 97818150B3D5D600 CRC64; MMPQLQFKDA FWCRDFTAHT GYEVLLQRLL DGRKMCKDME ELLRQRAQAE ERYGKELVQI ARKAGGQTEI NSLRASFDSL KQQMENVGSS HIQLALTLRE ELRSLEEFRE RQKEQRKKYE AVMDRVQKSK LSLYKKAMES KKTYEQKCRD ADDAEQAFER ISANGHQKQV EKSQNKARQC KDSATEAERV YRQSIAQLEK VRAEWEQEHR TTCEAFQLQE FDRLTILRNA LWVHSNQLSM QCVKDDELYE EVRLTLEGCS IDADIDSFIQ AKSTGTEPPA PVPYQNYYDR EVTPLTSSPG IQPSCGMIKR FSGLLHGSPK TTSLAASAAS TETLTPTPER NEGVYTAIAV QEIQGNPASP AQEYRALYDY TAQNPDELDL SAGDILEVIL EGEDGWWTVE RNGQRGFVPG SYLEKL //