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Pyrin (Marenostrin)

 MEFV_HUMAN              Reviewed;         781 AA.
O15553; D3DUC0; F5H0Q3; Q3MJ84; Q96PN4; Q96PN5;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
22-NOV-2017, entry version 180.
RecName: Full=Pyrin;
AltName: Full=Marenostrin;
Name=MEFV; Synonyms=MEF, TRIM20 {ECO:0000303|PubMed:26347139};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ARFMF ILE-680;
VAL-694 AND ALA-726.
TISSUE=Leukocyte;
PubMed=9288758;
Aksentijevich I., Centola M., Deng Z., Sood R., Balow J.E. Jr.,
Wood G., Zaks N., Mansfield E., Chen X., Eisenberg S., Vedula A.,
Shafran N., Raben N., Pras E., Pras M., Kastner D.L., Blake T.,
Baxevanis A.D., Robbins C., Krizman D., Collins F.S., Liu P.P.,
Chen X., Shohat M., Hamon M., Kahan T., Cercek A., Rotter J.I.,
Fischel-Ghodsian N., Richards N., Shelton D.A., Gumucio D.,
Yokoyama Y., Mangelsdorf M., Orsborn A., Richards R.I., Ricke D.O.,
Buckingham J.M., Moyzis R.K., Deaven L.L., Doggett N.A.;
"Ancient missense mutations in a new member of the RoRet gene family
are likely to cause familial Mediterranean fever.";
Cell 90:797-807(1997).
[2]
NUCLEOTIDE SEQUENCE (ISOFORM 2), TISSUE SPECIFICITY, AND SUBCELLULAR
LOCATION.
TISSUE=Leukocyte;
PubMed=11115844; DOI=10.1093/hmg/9.20.3001;
Papin S., Duquesnoy P., Cazeneuve C., Pantel J., Coppey-Moisan M.,
Dargemont C., Amselem S.;
"Alternative splicing at the MEFV locus involved in familial
Mediterranean fever regulates translocation of the marenostrin/pyrin
protein to the nucleus.";
Hum. Mol. Genet. 9:3001-3009(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
GLN-202.
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 305-754, AND VARIANTS ARFMF ILE-680 AND
ILE-694.
PubMed=9288094; DOI=10.1038/ng0997-25;
Bernot A., Clepet C., Dasilva C., Devaud C., Petit J.-L.,
Caloustian C., Cruaud C., Samson D., Pulcini F., Weissenbach J.,
Heilig R., Notanicola C., Domingo C., Rozenbaum M., Benchetrit E.,
Topaloglu R., Dewalle M., Dross C., Hadjari P., Dupont M.,
Demaille J.G., Touitou I., Smaoui N., Nedelec B., Mery J.-P.,
Chaabouni H., Delpech M., Grateau G.;
"A candidate gene for familial Mediterranean fever.";
Nat. Genet. 17:25-31(1997).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 96-303 AND 599-781, AND VARIANTS ARFMF
LYS-230 AND HIS-653.
TISSUE=Blood;
PubMed=11470495; DOI=10.1016/S0027-5107(01)00221-4;
Timmann C., Muntau B., Kuhne K., Gelhaus A., Horstmann R.D.;
"Two novel mutations R653H and E230K in the Mediterranean fever gene
associated with disease.";
Mutat. Res. 479:235-239(2001).
[7]
FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
PubMed=10807793;
Centola M., Wood G., Frucht D.M., Galon J., Aringer M., Farrell C.,
Kingma D.W., Horwitz M.E., Mansfield E., Holland S.M., O'Shea J.J.,
Rosenberg H.F., Malech H.L., Kastner D.L.;
"The gene for familial Mediterranean fever, MEFV, is expressed in
early leukocyte development and is regulated in response to
inflammatory mediators.";
Blood 95:3223-3231(2000).
[8]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=10666224;
Tidow N., Chen X., Muller C., Kawano S., Gombart A.F.,
Fischel-Ghodsian N., Koeffler H.P.;
"Hematopoietic-specific expression of MEFV, the gene mutated in
familial Mediterranean fever, and subcellular localization of its
corresponding protein, pyrin.";
Blood 95:1451-1455(2000).
[9]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=11468188; DOI=10.1182/blood.V98.3.851;
Mansfield E., Chae J.J., Komarow H.D., Brotz T.M., Frucht D.M.,
Aksentijevich I., Kastner D.L.;
"The familial Mediterranean fever protein, pyrin, associates with
microtubules and colocalizes with actin filaments.";
Blood 98:851-859(2001).
[10]
INTERACTION WITH PYCARD, AND SUBCELLULAR LOCATION.
PubMed=11498534; DOI=10.1074/jbc.M104730200;
Richards N., Schaner P., Diaz A., Stuckey J., Shelden E., Wadhwa A.,
Gumucio D.L.;
"Interaction between pyrin and the apoptotic speck protein (ASC)
modulates ASC-induced apoptosis.";
J. Biol. Chem. 276:39320-39329(2001).
[11]
INTERACTION WITH PSTPIP1.
PubMed=14595024; DOI=10.1073/pnas.2135380100;
Shoham N.G., Centola M., Mansfield E., Hull K.M., Wood G., Wise C.A.,
Kastner D.L.;
"Pyrin binds the PSTPIP1/CD2BP1 protein, defining familial
Mediterranean fever and PAPA syndrome as disorders in the same
pathway.";
Proc. Natl. Acad. Sci. U.S.A. 100:13501-13506(2003).
[12]
DISEASE.
PubMed=12384939; DOI=10.1002/art.10575;
Notarnicola C., Didelot M.-N., Kone-Paut I., Seguret F., Demaille J.,
Touitou I.;
"Reduced MEFV messenger RNA expression in patients with familial
Mediterranean fever.";
Arthritis Rheum. 46:2785-2793(2002).
[13]
FUNCTION, AND MUTAGENESIS OF LEU-16 AND PHE-24.
PubMed=16037825; DOI=10.1038/sj.cdd.4401734;
Yu J.W., Wu J., Zhang Z., Datta P., Ibrahimi I., Taniguchi S.,
Sagara J., Fernandes-Alnemri T., Alnemri E.S.;
"Cryopyrin and pyrin activate caspase-1, but not NF-kappaB, via ASC
oligomerization.";
Cell Death Differ. 13:236-249(2006).
[14]
INTERACTION WITH CASP1, AND CHARACTERIZATION OF VARIANTS ILE-680;
VAL-694 AND ALA-726.
PubMed=16785446; DOI=10.1073/pnas.0602081103;
Chae J.J., Wood G., Masters S.L., Richard K., Park G., Smith B.J.,
Kastner D.L.;
"The B30.2 domain of pyrin, the familial Mediterranean fever protein,
interacts directly with caspase-1 to modulate IL-1beta production.";
Proc. Natl. Acad. Sci. U.S.A. 103:9982-9987(2006).
[15]
FUNCTION, INTERACTION WITH CASP1; CASP5; NLRP1; NLRP2; NLRP3 AND IL1B,
AND CHARACTERIZATION OF VARIANT VAL-694.
PubMed=17431422; DOI=10.1038/sj.cdd.4402142;
Papin S., Cuenin S., Agostini L., Martinon F., Werner S., Beer H.D.,
Grutter C., Grutter M., Tschopp J.;
"The SPRY domain of Pyrin, mutated in familial Mediterranean fever
patients, interacts with inflammasome components and inhibits proIL-
1beta processing.";
Cell Death Differ. 14:1457-1466(2007).
[16]
FUNCTION, SUBUNIT, INTERACTION WITH PYCARD AND PSTPIP1, AND INDUCTION
BY RETROVIRAL INFECTION.
PubMed=17964261; DOI=10.1016/j.molcel.2007.08.029;
Yu J.W., Fernandes-Alnemri T., Datta P., Wu J., Juliana C.,
Solorzano L., McCormick M., Zhang Z., Alnemri E.S.;
"Pyrin activates the ASC pyroptosome in response to engagement by
autoinflammatory PSTPIP1 mutants.";
Mol. Cell 28:214-227(2007).
[17]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RELA AND NFKBIA,
PROBABLE CLEAVAGE BY CASP-1, AND MUTAGENESIS OF ASP-330.
PubMed=18577712; DOI=10.1182/blood-2008-01-134932;
Chae J.J., Wood G., Richard K., Jaffe H., Colburn N.T., Masters S.L.,
Gumucio D.L., Shoham N.G., Kastner D.L.;
"The familial Mediterranean fever protein, pyrin, is cleaved by
caspase-1 and activates NF-kappaB through its N-terminal fragment.";
Blood 112:1794-1803(2008).
[18]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PSTPIP1; VASP AND
ACTR3.
PubMed=19109554; DOI=10.3181/0806-RM-184;
Waite A.L., Schaner P., Hu C., Richards N., Balci-Peynircioglu B.,
Hong A., Fox M., Gumucio D.L.;
"Pyrin and ASC co-localize to cellular sites that are rich in
polymerizing actin.";
Exp. Biol. Med. (Maywood) 234:40-52(2009).
[19]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=19584923; DOI=10.1371/journal.pone.0006147;
Waite A.L., Schaner P., Richards N., Balci-Peynircioglu B.,
Masters S.L., Brydges S.D., Fox M., Hong A., Yilmaz E., Kastner D.L.,
Reinherz E.L., Gumucio D.L.;
"Pyrin Modulates the Intracellular Distribution of PSTPIP1.";
PLoS ONE 4:E6147-E6147(2009).
[20]
FUNCTION, INTERACTION WITH ATG16L1; BECN1; GABARAP; GABARAPL1;
GABARAPL2; MAP1LC3A; MAP1LC3C; NLRP3; TRIM21 AND ULK1, SUBCELLULAR
LOCATION, INDUCTION BY IFNG, DEGRADATION BY AUTOPHAGY,
CHARACTERIZATION OF VARIANTS ARFMF ILE-680; VAL-694 AND ALA-726, AND
MUTAGENESIS OF 397-ILE--HIS-404; 470-TYR--GLY-488 AND
523-SER--ASP-530.
PubMed=26347139; DOI=10.1083/jcb.201503023;
Kimura T., Jain A., Choi S.W., Mandell M.A., Schroder K., Johansen T.,
Deretic V.;
"TRIM-mediated precision autophagy targets cytoplasmic regulators of
innate immunity.";
J. Cell Biol. 210:973-989(2015).
[21]
X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 586-776.
PubMed=19729025; DOI=10.1016/j.jmb.2009.08.059;
Weinert C., Grutter C., Roschitzki-Voser H., Mittl P.R., Grutter M.G.;
"The crystal structure of human pyrin b30.2 domain: implications for
mutations associated with familial Mediterranean fever.";
J. Mol. Biol. 394:226-236(2009).
[22]
VARIANTS ARFMF, AND VARIANT GLN-202.
PubMed=9668175; DOI=10.1093/hmg/7.8.1317;
Bernot A., da Silva C., Petit J.-L., Cruaud C., Caloustian C.,
Castet V., Ahmed-Arab M., Dross C., Dupont M., Cattan D., Smaoui N.,
Dode C., Pecheux C., Nedelec B., Medaxian J., Rozenbaum M., Rosner I.,
Delpech M., Grateau G., Demaille J., Weissenbach J., Touitou I.;
"Non-founder mutations in the MEFV gene establish this gene as the
cause of familial Mediterranean fever (FMF).";
Hum. Mol. Genet. 7:1317-1325(1998).
[23]
VARIANTS ARFMF ILE-680; ILE-681; ILE-694; VAL-694; MET-694 DEL AND
ALA-726.
PubMed=10024914; DOI=10.1093/qjmed/91.9.603;
Booth D.R., Gillmore J.D., Booth S.E., Pepys M.B., Hawkins P.N.;
"Pyrin/marenostrin mutations in familial Mediterranean fever.";
QJM 91:603-606(1998).
[24]
VARIANTS ARFMF.
PubMed=10090880; DOI=10.1086/302327;
Aksentijevich I., Torosyan Y., Samuels J., Centola M., Pras E.,
Chae J.J., Oddoux C., Wood G., Azzaro M.P., Palumbo G., Giustolisi R.,
Pras M., Ostrer H., Kastner D.L.;
"Mutation and haplotype studies of familial Mediterranean fever reveal
new ancestral relationships and evidence for a high carrier frequency
with reduced penetrance in the Ashkenazi Jewish population.";
Am. J. Hum. Genet. 64:949-962(1999).
[25]
VARIANTS ARFMF GLN-148; SER-369; GLN-408; LEU-479; ILE-680; VAL-694;
ALA-726 AND HIS-761.
PubMed=10364520; DOI=10.1086/302459;
Cazeneuve C., Sarkisian T., Pecheux C., Dervichian M., Nedelec B.,
Reinert P., Ayvazyan A., Kouyoumdjian J.-C., Ajrapetyan H.,
Delpech M., Goossens M., Dode C., Grateau G., Amselem S.;
"MEFV-Gene analysis in Armenian patients with familial Mediterranean
fever: diagnostic value and unfavorable renal prognosis of the M694V
homozygous genotype-genetic and therapeutic implications.";
Am. J. Hum. Genet. 65:88-97(1999).
[26]
VARIANTS ARFMF ILE-680; ILE-694; VAL-694 AND ALA-726.
PubMed=10234504; DOI=10.1038/sj.ejhg.5200303;
Shohat M., Magal N., Shohat T., Chen X., Dagan T., Mimouni A.,
Danon Y., Lotan R., Ogur G., Sirin A., Schlezinger M., Halpern G.J.,
Schwabe A., Kastner D., Rotter J.I., Fischel-Ghodsian N.;
"Phenotype-genotype correlation in familial Mediterranean fever:
evidence for an association between Met694Val and amyloidosis.";
Eur. J. Hum. Genet. 7:287-292(1999).
[27]
VARIANTS ARFMF GLN-148; ILE-680; ILE-694; VAL-694; ARG-695; ALA-726
AND HIS-761.
PubMed=10612841;
DOI=10.1002/(SICI)1098-1004(200001)15:1<118::AID-HUMU29>3.0.CO;2-5;
Akar N., Misiroglu M., Yalcinkaya F., Akar E., Cakar N., Tumer N.,
Akcakus M., Tastan H., Matzner Y.;
"MEFV mutations in Turkish patients suffering from familial
Mediterranean fever.";
Hum. Mutat. 15:118-119(2000).
[28]
VARIANT GLN-148.
PubMed=10737995;
DOI=10.1002/(SICI)1098-1004(200004)15:4<385::AID-HUMU22>3.3.CO;2-1;
Ben-Chetrit E., Lerer I., Malamud E., Domingo C., Abeliovich D.;
"The E148Q mutation in the MEFV gene: is it a disease-causing mutation
or a sequence variant?";
Hum. Mutat. 15:385-386(2000).
[29]
VARIANTS ARFMF PRO-110; GLN-148 AND VAL-694.
PubMed=10854105; DOI=10.1038/sj.ejhg.5200462;
Domingo C., Touitou I., Bayou A., Ozen S., Notarnicola C., Dewalle M.,
Demaille J., Buades R., Sayadat C., Levy M., Ben-Chetrit E.;
"Familial Mediterranean fever in the 'Chuetas' of Mallorca: a question
of Jewish origin or genetic heterogeneity.";
Eur. J. Hum. Genet. 8:242-246(2000).
[30]
VARIANTS ARFMF ASN-675 AND LEU-680.
PubMed=10842288;
DOI=10.1002/(SICI)1096-8628(20000605)92:4<241::AID-AJMG3>3.0.CO;2-G;
Dode C., Pecheux C., Cazeneuve C., Cattan D., Dervichian M.,
Goossens M., Delpech M., Amselem S., Grateau G.;
"Mutations in the MEFV gene in a large series of patients with a
clinical diagnosis of familial Mediterranean fever.";
Am. J. Med. Genet. 92:241-246(2000).
[31]
VARIANTS ADFMF GLN-148; ILE-680; ILE-694; MET-694 DEL AND VAL-694.
PubMed=10787449; DOI=10.1093/qjmed/93.4.217;
Booth D.R., Gillmore J.D., Lachmann H.J., Booth S.E., Bybee A.,
Soytuerk M., Akar S., Pepys M.B., Tunca M., Hawkins P.N.;
"The genetic basis of autosomal dominant familial Mediterranean
fever.";
QJM 93:217-221(2000).
[32]
REVIEW ON ARFMF VARIANTS.
PubMed=11464238; DOI=10.1038/sj.ejhg.5200658;
Touitou I.;
"The spectrum of familial mediterranean fever (FMF) mutations.";
Eur. J. Hum. Genet. 9:473-483(2001).
[33]
VARIANT FMF ALA-138.
PubMed=11139244;
DOI=10.1002/1098-1004(2001)17:1<71::AID-HUMU8>3.0.CO;2-3;
Akar E., Yalcinkaya F., Akar N.;
"Is the Ala138Gly alteration of MEFV gene important for amyloidosis?";
Hum. Mutat. 17:71-71(2001).
[34]
VARIANT FMF THR-591.
PubMed=12124996; DOI=10.1002/humu.10103;
Aldea A., Casademont J., Arostegui J.I., Rius J., Maso M., Vives J.,
Yague J.;
"I591T MEFV mutation in a Spanish kindred: is it a mild mutation, a
benign polymorphism, or a variant influenced by another modifier?";
Hum. Mutat. 20:148-150(2002).
[35]
VARIANT ADFMF TYR-478.
PubMed=14679589; DOI=10.1002/ajmg.a.20296;
Aldea A., Campistol J.M., Arostegui J.I., Rius J., Maso M., Vives J.,
Yaguee J.;
"A severe autosomal-dominant periodic inflammatory disorder with renal
AA amyloidosis and colchicine resistance associated to the MEFV H478Y
variant in a Spanish kindred: an unusual familial Mediterranean fever
phenotype or another MEFV-associated periodic inflammatory disorder?";
Am. J. Med. Genet. A 124:67-73(2004).
[36]
VARIANTS ARFMF ALA-163 AND LYS-319, AND VARIANT SER-744.
PubMed=15024744; DOI=10.1002/humu.9229;
Aldea A., Calafell F., Arostegui J.I., Lao O., Rius J., Plaza S.,
Maso M., Vives J., Buades J., Yaguee J.;
"The west side story: MEFV haplotype in Spanish FMF patients and
controls, and evidence of high LD and a recombination 'hot-spot' at
the MEFV locus.";
Hum. Mutat. 23:399-399(2004).
[37]
VARIANTS ARFMF ARG-108; GLN-148; VAL-148; ASP-167; ILE-177; ILE-267;
LYS-474; LEU-479; HIS-653; ILE-680; ILE-694; VAL-694; ARG-695;
MET-720; ALA-726; SER-744 AND HIS-761.
PubMed=16378925; DOI=10.1016/j.ejmg.2005.05.010;
Medlej-Hashim M., Serre J.-L., Corbani S., Saab O., Jalkh N.,
Delague V., Chouery E., Salem N., Loiselet J., Lefranc G.,
Megarbane A.;
"Familial Mediterranean fever (FMF) in Lebanon and Jordan: a
population genetics study and report of three novel mutations.";
Eur. J. Med. Genet. 48:412-420(2005).
[38]
VARIANTS ARFMF SER-632; MET-640; PHE-641; LEU-646; PRO-649; HIS-653;
ALA-656; ASN-661; ASN-675; GLU-678; LEU-680; ILE-681; CYS-688;
ILE-694; LEU-694; VAL-694; MET-695; ARG-695; ILE-704; SER-705;
MET-720; ALA-726; LEU-743; SER-744; SER-758; HIS-761 AND THR-780, AND
VARIANT CYS-702.
PubMed=16730661; DOI=10.1016/j.bbrc.2006.04.185;
Goulielmos G.N., Fragouli E., Aksentijevich I., Sidiropoulos P.,
Boumpas D.T., Eliopoulos E.;
"Mutational analysis of the PRYSPRY domain of pyrin and implications
for familial mediterranean fever (FMF).";
Biochem. Biophys. Res. Commun. 345:1326-1332(2006).
[39]
VARIANT ARFMF LYS-694.
PubMed=23031807; DOI=10.1016/j.gene.2012.09.073;
Yesilada E., Taskapan H., Gulbay G.;
"Prevalence of known mutations and a novel missense mutation (M694K)
in the MEFV gene in a population from the Eastern Anatolia Region of
Turkey.";
Gene 511:371-374(2012).
[40]
VARIANTS ILE-267; SER-369; GLN-408; ALA-577; ASN-577 AND SER-577, AND
INVOLVEMENT IN AUTOSOMAL DOMINANT INFLAMMATORY DISEASE.
PubMed=23505238; DOI=10.1136/annrheumdis-2012-202580;
Stoffels M., Szperl A., Simon A., Netea M.G., Plantinga T.S.,
van Deuren M., Kamphuis S., Lachmann H.J., Cuppen E.,
Kloosterman W.P., Frenkel J., van Diemen C.C., Wijmenga C.,
van Gijn M., van der Meer J.W.;
"MEFV mutations affecting pyrin amino acid 577 cause autosomal
dominant autoinflammatory disease.";
Ann. Rheum. Dis. 73:455-461(2014).
[41]
VARIANTS ARFMF PRO-110; GLN-148; LYS-230; ILE-680; ILE-694; VAL-694;
ARG-695; ALA-726; SER-744 AND HIS-761, AND VARIANTS TRP-196; GLN-202;
VAL-247; LEU-283; ARG-304 AND ALA-632.
PubMed=24929125; DOI=10.1016/j.gene.2014.06.019;
Gunesacar R., Celik M.M., Arica V., Elmacioglu S., Ozturk O.H.;
"Frequency of MEFV gene mutations in Hatay province, Mediterranean
region of Turkey and report of a novel missense mutation (I247V).";
Gene 546:195-199(2014).
-!- FUNCTION: Involved in the regulation of innate immunity and the
inflammatory response in response to IFNG/IFN-gamma. Organizes
autophagic machinery by serving as a platform for the assembly of
ULK1, Beclin 1/BECN1, ATG16L1, and ATG8 family members and
recognizes specific autophagy targets, thus coordinating target
recognition with assembly of the autophagic apparatus and
initiation of autophagy. Acts as an autophagy receptor for the
degradation of several inflammasome components, including CASP1,
NLRP1 and NLRP3, hence preventing excessive IL1B- and IL18-
mediated inflammation (PubMed:16785446, PubMed:17431422,
PubMed:26347139). However, it may also have a positive effect in
the inflammatory pathway. In different experimental systems, it
has been shown to activate IL1B production (PubMed:16037825). It
has also been shown to be required for PSTPIP1-induced PYCARD
oligomerization and for formation of inflammasomes. Recruits
PSTPIP1 to inflammasomes, and is required for PSTPIP1
oligomerization (PubMed:10807793, PubMed:11468188,
PubMed:17964261, PubMed:18577712, PubMed:19109554,
PubMed:19584923). {ECO:0000269|PubMed:10807793,
ECO:0000269|PubMed:11468188, ECO:0000269|PubMed:16037825,
ECO:0000269|PubMed:16785446, ECO:0000269|PubMed:17431422,
ECO:0000269|PubMed:17964261, ECO:0000269|PubMed:18577712,
ECO:0000269|PubMed:19109554, ECO:0000269|PubMed:19584923,
ECO:0000269|PubMed:26347139}.
-!- SUBUNIT: Homotrimer. Interacts (via the B box-type zinc finger)
with PSTPIP1 (PubMed:14595024, PubMed:17964261, PubMed:19109554).
Interacts (via the B30.2/SPRY domain) with several components of
the inflammasome complex, including CASP1 p20 and p10 subunits,
CASP5, PYCARD, NLRP1, NLRP2 AND NLRP3, as well as with unprocessed
IL1B; this interaction may lead to autophagic degradation of these
proteins (PubMed:11498534, PubMed:16785446, PubMed:17431422,
PubMed:17964261, PubMed:26347139). Interacts with NFKBIA and RELA
(PubMed:18577712). Interacts weakly with VASP and ACTR3
(PubMed:19109554). Interacts with active ULK1 (phosphorylated on
'Ser-317') and BECN1 simultaneously. Also interacts with ATG16L1
(via WD repeats), and with ATG8 family members, including GABARAP,
GABARAPL1 and, to a lesser extent, GABARAPL2, MAP1LC3A/LC3A and
MAP1LC3C/LC3C. Interacts with TRIM21 (PubMed:26347139).
{ECO:0000269|PubMed:11498534, ECO:0000269|PubMed:14595024,
ECO:0000269|PubMed:16785446, ECO:0000269|PubMed:17431422,
ECO:0000269|PubMed:17964261, ECO:0000269|PubMed:18577712,
ECO:0000269|PubMed:19109554, ECO:0000269|PubMed:26347139}.
-!- INTERACTION:
Self; NbExp=8; IntAct=EBI-7644532, EBI-7644532;
P29466:CASP1; NbExp=3; IntAct=EBI-15588296, EBI-516667;
O43586:PSTPIP1; NbExp=4; IntAct=EBI-7644532, EBI-1050964;
Q9ULZ3:PYCARD; NbExp=8; IntAct=EBI-7644532, EBI-751215;
-!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasm, cytoskeleton. Cell
projection, ruffle. Cell projection, lamellipodium. Nucleus.
Cytoplasm {ECO:0000269|PubMed:26347139}. Cytoplasmic vesicle,
autophagosome {ECO:0000269|PubMed:26347139}. Note=Associated with
microtubules and with the filamentous actin of perinuclear
filaments and peripheral lamellar ruffles. In pre-apoptotic cells,
colocalizes with PYCARD/ASC in large specks (inflammasomes). In
migrating monocytes, strongly polarized at the leading edge of the
cell where it colocalizes with polymerizing actin and PYCARD/ASC.
-!- SUBCELLULAR LOCATION: Isoform 2: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=FL;
IsoId=O15553-2; Sequence=Displayed;
Name=2; Synonyms=D2;
IsoId=O15553-1; Sequence=VSP_008223;
Name=3;
IsoId=O15553-3; Sequence=VSP_008223, VSP_047663;
-!- TISSUE SPECIFICITY: Expressed in peripheral blood leukocytes,
particularly in mature granulocytes and to a lesser extent in
monocytes but not in lymphocytes. Detected in spleen, lung and
muscle, probably as a result of leukocyte infiltration in these
tissues. Not expressed in thymus, prostate, testis, ovary, small
intestine, colon, heart, brain, placenta, liver, kidney, pancreas.
Expression detected in several myeloid leukemic, colon cancer, and
prostate cancer cell lines. {ECO:0000269|PubMed:10666224,
ECO:0000269|PubMed:10807793, ECO:0000269|PubMed:11115844}.
-!- DEVELOPMENTAL STAGE: First detected in bone marrow promyelocytes.
Expression increases throughout myelocyte differentiation and
peaks in the mature myelomonocytic cells.
{ECO:0000269|PubMed:10807793}.
-!- INDUCTION: In monocytes, up-regulated by treatment with colchicine
and IFN-alpha, by the proinflammatory cytokines IFNG/IFN-gamma and
TNF, by bacterial lipopolysaccharides (LPS) and by retroviral
infection. Repressed in monocytes by the antiinflammatory
cytokines IL10/interleukin-10, TGFB1 and IL4/interleukin-4. In
neutrophils and macrophages, up-regulated by IFNG/IFN-gamma with a
peak after 8 hours of treatment. {ECO:0000269|PubMed:10807793,
ECO:0000269|PubMed:17964261, ECO:0000269|PubMed:26347139}.
-!- DOMAIN: The B box-type zinc finger interacts, possibly
intramolecularly, with the pyrin domain; this may be an
autoinhibitory mechanism released by PSTPIP1 binding.
-!- PTM: Cleaved by CASP1 (Probable). The N-terminal cleavage product
localizes to the nucleus as a filamentous network and to the
cytoplasm, interacts more strongly with RELA and NFKBIA than the
full-length protein, enhances the nuclear localization of RELA and
induces NFKBIA proteolysis. The C-terminal cleavage product
localizes to the cytoplasm. {ECO:0000305}.
-!- DISEASE: Familial Mediterranean fever, autosomal recessive (ARFMF)
[MIM:249100]: A hereditary periodic fever syndrome characterized
by recurrent episodic fever, serosal inflammation and pain in the
abdomen, chest or joints. It is frequently complicated by reactive
amyloidosis, which leads to renal failure and can be
prophylactically treated with colchicine.
{ECO:0000269|PubMed:10024914, ECO:0000269|PubMed:10090880,
ECO:0000269|PubMed:10234504, ECO:0000269|PubMed:10364520,
ECO:0000269|PubMed:10612841, ECO:0000269|PubMed:10842288,
ECO:0000269|PubMed:10854105, ECO:0000269|PubMed:11470495,
ECO:0000269|PubMed:15024744, ECO:0000269|PubMed:16378925,
ECO:0000269|PubMed:16730661, ECO:0000269|PubMed:23031807,
ECO:0000269|PubMed:24929125, ECO:0000269|PubMed:26347139,
ECO:0000269|PubMed:9288094, ECO:0000269|PubMed:9288758,
ECO:0000269|PubMed:9668175}. Note=The disease is caused by
mutations affecting the gene represented in this entry. The
disease-associated mutations in the B30.2/SPRY domain perturb ULK1
recruitment and autophagic degradation of inflammasome components,
including NLRP3, and hence may contribute to the inflammatory
phenotype associated with ARFMF. {ECO:0000269|PubMed:26347139}.
-!- DISEASE: Familial Mediterranean fever, autosomal dominant (ADFMF)
[MIM:134610]: A hereditary periodic fever syndrome characterized
by periodic fever, serosal inflammation and pain in the abdomen,
chest or joints as seen also in the autosomal recessive form of
the disease. It is associated with reactive renal amyloidosis and
characterized by colchicine unresponsiveness.
{ECO:0000269|PubMed:10787449, ECO:0000269|PubMed:14679589}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- MISCELLANEOUS: Degraded along with the delivery of its substrates
to autolysosomal compartments (at protein level).
{ECO:0000269|PubMed:26347139}.
-!- WEB RESOURCE: Name=INFEVERS; Note=Repertory of FMF and hereditary
autoinflammatory disorders mutations;
URL="http://fmf.igh.cnrs.fr/ISSAID/infevers/search.php?n=1";
-----------------------------------------------------------------------
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EMBL; AF018080; AAB70557.1; -; mRNA.
EMBL; CH471112; EAW85382.1; -; Genomic_DNA.
EMBL; CH471112; EAW85383.1; -; Genomic_DNA.
EMBL; BC101511; AAI01512.1; -; mRNA.
EMBL; BC101537; AAI01538.1; -; mRNA.
EMBL; Y14441; CAA74793.1; -; mRNA.
EMBL; AJ003147; CAA05906.1; -; Genomic_DNA.
EMBL; AF111163; AAD26152.1; -; Genomic_DNA.
EMBL; AF301150; AAK97223.1; -; Genomic_DNA.
EMBL; AF301151; AAK97224.1; -; Genomic_DNA.
CCDS; CCDS10498.1; -. [O15553-2]
CCDS; CCDS55981.1; -. [O15553-3]
RefSeq; NP_000234.1; NM_000243.2. [O15553-2]
RefSeq; NP_001185465.1; NM_001198536.1.
UniGene; Hs.632221; -.
PDB; 2MPC; NMR; -; A=1-92.
PDB; 2WL1; X-ray; 1.35 A; A=586-776.
PDB; 4CG4; X-ray; 2.40 A; A/B/C/D/E/F=414-781.
PDBsum; 2MPC; -.
PDBsum; 2WL1; -.
PDBsum; 4CG4; -.
ProteinModelPortal; O15553; -.
SMR; O15553; -.
BioGrid; 110374; 12.
DIP; DIP-41878N; -.
IntAct; O15553; 4.
MINT; MINT-206922; -.
STRING; 9606.ENSP00000219596; -.
iPTMnet; O15553; -.
PhosphoSitePlus; O15553; -.
BioMuta; MEFV; -.
EPD; O15553; -.
PaxDb; O15553; -.
PeptideAtlas; O15553; -.
PRIDE; O15553; -.
Ensembl; ENST00000219596; ENSP00000219596; ENSG00000103313. [O15553-2]
Ensembl; ENST00000536379; ENSP00000445079; ENSG00000103313. [O15553-1]
Ensembl; ENST00000541159; ENSP00000438711; ENSG00000103313. [O15553-3]
GeneID; 4210; -.
KEGG; hsa:4210; -.
UCSC; uc002cun.1; human. [O15553-2]
CTD; 4210; -.
DisGeNET; 4210; -.
EuPathDB; HostDB:ENSG00000103313.11; -.
GeneCards; MEFV; -.
GeneReviews; MEFV; -.
HGNC; HGNC:6998; MEFV.
MalaCards; MEFV; -.
MIM; 134610; phenotype.
MIM; 249100; phenotype.
MIM; 608107; gene.
neXtProt; NX_O15553; -.
OpenTargets; ENSG00000103313; -.
Orphanet; 117; Behcet disease.
Orphanet; 342; Familial Mediterranean fever.
Orphanet; 329967; Intermittent hydrarthrosis.
PharmGKB; PA30736; -.
eggNOG; KOG2177; Eukaryota.
eggNOG; ENOG4111G04; LUCA.
GeneTree; ENSGT00760000118838; -.
HOGENOM; HOG000113552; -.
HOVERGEN; HBG006343; -.
InParanoid; O15553; -.
KO; K12803; -.
OMA; PQCERHM; -.
OrthoDB; EOG091G05W2; -.
PhylomeDB; O15553; -.
TreeFam; TF351091; -.
Reactome; R-HSA-844456; The NLRP3 inflammasome.
EvolutionaryTrace; O15553; -.
GeneWiki; MEFV; -.
GenomeRNAi; 4210; -.
PRO; PR:O15553; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000103313; -.
CleanEx; HS_MEFV; -.
ExpressionAtlas; O15553; baseline and differential.
GO; GO:0005776; C:autophagosome; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0005875; C:microtubule associated complex; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
GO; GO:0003779; F:actin binding; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB.
GO; GO:0006954; P:inflammatory response; IDA:UniProtKB.
GO; GO:1900016; P:negative regulation of cytokine production involved in inflammatory response; IMP:UniProtKB.
GO; GO:0050728; P:negative regulation of inflammatory response; IMP:BHF-UCL.
GO; GO:0032691; P:negative regulation of interleukin-1 beta production; IMP:BHF-UCL.
GO; GO:0032695; P:negative regulation of interleukin-12 production; IMP:BHF-UCL.
GO; GO:0071641; P:negative regulation of macrophage inflammatory protein 1 alpha production; IMP:BHF-UCL.
GO; GO:1900226; P:negative regulation of NLRP3 inflammasome complex assembly; IMP:UniProtKB.
GO; GO:0010508; P:positive regulation of autophagy; IDA:UniProtKB.
GO; GO:2001056; P:positive regulation of cysteine-type endopeptidase activity; IDA:UniProtKB.
GO; GO:0034341; P:response to interferon-gamma; IDA:UniProtKB.
CDD; cd00021; BBOX; 1.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR001870; B30.2/SPRY.
InterPro; IPR003879; Butyrophylin_SPRY.
InterPro; IPR013320; ConA-like_dom_sf.
InterPro; IPR004020; DAPIN.
InterPro; IPR011029; DEATH-like_dom_sf.
InterPro; IPR006574; PRY.
InterPro; IPR028841; Pyrin.
InterPro; IPR003877; SPRY_dom.
InterPro; IPR000315; Znf_B-box.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
PANTHER; PTHR45323; PTHR45323; 2.
Pfam; PF13765; PRY; 1.
Pfam; PF02758; PYRIN; 1.
Pfam; PF00622; SPRY; 1.
Pfam; PF00643; zf-B_box; 1.
PRINTS; PR01407; BUTYPHLNCDUF.
SMART; SM00336; BBOX; 1.
SMART; SM00589; PRY; 1.
SMART; SM01289; PYRIN; 1.
SMART; SM00449; SPRY; 1.
SUPFAM; SSF47986; SSF47986; 1.
SUPFAM; SSF49899; SSF49899; 1.
PROSITE; PS50188; B302_SPRY; 1.
PROSITE; PS50824; DAPIN; 1.
PROSITE; PS50119; ZF_BBOX; 1.
1: Evidence at protein level;
3D-structure; Actin-binding; Alternative splicing; Amyloidosis;
Cell projection; Coiled coil; Complete proteome; Cytoplasm;
Cytoplasmic vesicle; Cytoskeleton; Disease mutation; Immunity;
Inflammatory response; Innate immunity; Metal-binding; Microtubule;
Nucleus; Polymorphism; Reference proteome; Zinc; Zinc-finger.
CHAIN 1 781 Pyrin.
/FTId=PRO_0000220364.
DOMAIN 1 92 Pyrin. {ECO:0000255|PROSITE-
ProRule:PRU00061}.
DOMAIN 580 775 B30.2/SPRY. {ECO:0000255|PROSITE-
ProRule:PRU00548}.
ZN_FING 370 412 B box-type. {ECO:0000255|PROSITE-
ProRule:PRU00024}.
REGION 266 280 Interaction with RELA.
{ECO:0000269|PubMed:18577712}.
REGION 420 582 Required for homotrimerization and
induction of pyroptosomes.
COILED 413 442 {ECO:0000255}.
MOTIF 420 437 Nuclear localization signal.
{ECO:0000255}.
SITE 330 331 Cleavage; by CASP1. {ECO:0000305}.
VAR_SEQ 93 303 Missing (in isoform 2 and isoform 3).
{ECO:0000305}.
/FTId=VSP_008223.
VAR_SEQ 587 781 VPELIGAQAHAVNVILDAETAYPNLIFSDDLKSVRLGNKWE
RLPDGPQRFDSCIIVLGSPSFLSGRRYWEVEVGDKTAWILG
ACKTSISRKGNMTLSPENGYWVVIMMKENEYQASSVPPTRL
LIKEPPKRVGIFVDYRVGSISFYNVTARSHIYTFASCSFSG
PLQPIFSPGTRDGGKNTAPLTICPVGGQGPD -> DHSPQH
GLGSWEERDYTQHSMQGPKQGVPCLSLLSGQCNLAPLNANA
QDFFPYLIFLRSSGADWRSGTCC (in isoform 3).
{ECO:0000305}.
/FTId=VSP_047663.
VARIANT 33 33 V -> L (in dbSNP:rs11466016).
/FTId=VAR_048398.
VARIANT 42 42 R -> W (in arFMF; dbSNP:rs61754767).
/FTId=VAR_028326.
VARIANT 108 108 S -> R (in arFMF; dbSNP:rs104895103).
{ECO:0000269|PubMed:16378925}.
/FTId=VAR_028327.
VARIANT 110 110 L -> P (in arFMF; dbSNP:rs11466018).
{ECO:0000269|PubMed:10854105,
ECO:0000269|PubMed:24929125}.
/FTId=VAR_016824.
VARIANT 138 138 G -> A (association with renal
amyloidosis).
{ECO:0000269|PubMed:11139244}.
/FTId=VAR_016825.
VARIANT 148 148 E -> Q (in arFMF and adFMF; common
mutation; associated with S-369 and Q-408
in cis; associated with I-694 in some
patients; dbSNP:rs3743930).
{ECO:0000269|PubMed:10364520,
ECO:0000269|PubMed:10612841,
ECO:0000269|PubMed:10737995,
ECO:0000269|PubMed:10787449,
ECO:0000269|PubMed:10854105,
ECO:0000269|PubMed:16378925,
ECO:0000269|PubMed:24929125}.
/FTId=VAR_009051.
VARIANT 148 148 E -> V (in arFMF; dbSNP:rs104895076).
{ECO:0000269|PubMed:16378925}.
/FTId=VAR_028328.
VARIANT 163 163 E -> A (in arFMF; dbSNP:rs104895106).
{ECO:0000269|PubMed:15024744}.
/FTId=VAR_028329.
VARIANT 167 167 E -> D (in arFMF; dbSNP:rs104895079).
{ECO:0000269|PubMed:16378925}.
/FTId=VAR_009052.
VARIANT 177 177 T -> I (in arFMF; dbSNP:rs104895143).
{ECO:0000269|PubMed:16378925}.
/FTId=VAR_028330.
VARIANT 196 196 G -> W (in a Turkish patient with arFMF;
unknown pathological significance;
dbSNP:rs104895179).
{ECO:0000269|PubMed:24929125}.
/FTId=VAR_072382.
VARIANT 202 202 R -> Q (in dbSNP:rs224222).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:24929125,
ECO:0000269|PubMed:9668175}.
/FTId=VAR_009053.
VARIANT 230 230 E -> K (in arFMF; dbSNP:rs104895080).
{ECO:0000269|PubMed:11470495,
ECO:0000269|PubMed:24929125}.
/FTId=VAR_016826.
VARIANT 247 247 I -> V (in a Turkish patient with arFMF;
unknown pathological significance).
{ECO:0000269|PubMed:24929125}.
/FTId=VAR_072383.
VARIANT 267 267 T -> I (in arFMF; dbSNP:rs104895081).
{ECO:0000269|PubMed:16378925,
ECO:0000269|PubMed:23505238}.
/FTId=VAR_009054.
VARIANT 283 283 P -> L (in Turkish patients with arFMF;
unknown pathological significance;
dbSNP:rs104895119).
{ECO:0000269|PubMed:24929125}.
/FTId=VAR_072384.
VARIANT 304 304 G -> R (in a Turkish patient with arFMF;
unknown pathological significance;
dbSNP:rs75977701).
{ECO:0000269|PubMed:24929125}.
/FTId=VAR_072385.
VARIANT 319 319 E -> K (in arFMF; dbSNP:rs104895110).
{ECO:0000269|PubMed:15024744}.
/FTId=VAR_028331.
VARIANT 369 369 P -> S (in arFMF; unknown pathological
significance; associated with Q-148 and
Q-408 in cis; dbSNP:rs11466023).
{ECO:0000269|PubMed:10364520,
ECO:0000269|PubMed:23505238}.
/FTId=VAR_009055.
VARIANT 408 408 R -> Q (in arFMF; associated with Q-148
and S-369 in cis; dbSNP:rs11466024).
{ECO:0000269|PubMed:10364520,
ECO:0000269|PubMed:23505238}.
/FTId=VAR_009056.
VARIANT 440 440 Q -> E (in dbSNP:rs11466026).
/FTId=VAR_024376.
VARIANT 474 474 E -> K (in arFMF; dbSNP:rs104895104).
{ECO:0000269|PubMed:16378925}.
/FTId=VAR_028332.
VARIANT 478 478 H -> Y (in adFMF; severe;
dbSNP:rs104895105).
{ECO:0000269|PubMed:14679589}.
/FTId=VAR_028333.
VARIANT 479 479 F -> L (in arFMF; dbSNP:rs104895083).
{ECO:0000269|PubMed:10364520,
ECO:0000269|PubMed:16378925}.
/FTId=VAR_009057.
VARIANT 577 577 T -> A (probable disease-associated
mutation found in an autosomal dominant
autoinflammatory disease with some
similarities to familial Mediterranean
fever). {ECO:0000269|PubMed:23505238}.
/FTId=VAR_070795.
VARIANT 577 577 T -> N (probable disease-associated
mutation found in an autosomal dominant
autoinflammatory disease with some
similarities to familial Mediterranean
fever). {ECO:0000269|PubMed:23505238}.
/FTId=VAR_070796.
VARIANT 577 577 T -> S (probable disease-associated
mutation found in an autosomal dominant
autoinflammatory disease with some
similarities to familial Mediterranean
fever; dbSNP:rs104895193).
{ECO:0000269|PubMed:23505238}.
/FTId=VAR_070797.
VARIANT 585 585 F -> L (in dbSNP:rs11466043).
/FTId=VAR_028334.
VARIANT 591 591 I -> T (in arFMF; unknown pathological
significance; dbSNP:rs11466045).
{ECO:0000269|PubMed:12124996}.
/FTId=VAR_016827.
VARIANT 632 632 G -> A (in a Turkish patient with arFMF;
unknown pathological significance).
{ECO:0000269|PubMed:24929125}.
/FTId=VAR_072386.
VARIANT 632 632 G -> S (in arFMF; dbSNP:rs104895128).
{ECO:0000269|PubMed:16730661}.
/FTId=VAR_028335.
VARIANT 640 640 I -> M (in arFMF; dbSNP:rs104895115).
{ECO:0000269|PubMed:16730661}.
/FTId=VAR_028336.
VARIANT 641 641 I -> F (in arFMF; dbSNP:rs104895147).
{ECO:0000269|PubMed:16730661}.
/FTId=VAR_028337.
VARIANT 646 646 P -> L (in arFMF; dbSNP:rs104895107).
{ECO:0000269|PubMed:16730661}.
/FTId=VAR_028338.
VARIANT 649 649 L -> P (in arFMF; dbSNP:rs104895108).
{ECO:0000269|PubMed:16730661}.
/FTId=VAR_028339.
VARIANT 653 653 R -> H (in arFMF; dbSNP:rs104895085).
{ECO:0000269|PubMed:11470495,
ECO:0000269|PubMed:16378925,
ECO:0000269|PubMed:16730661}.
/FTId=VAR_016828.
VARIANT 656 656 E -> A (in arFMF; dbSNP:rs104895086).
{ECO:0000269|PubMed:16730661}.
/FTId=VAR_028340.
VARIANT 661 661 D -> N (in arFMF; dbSNP:rs104895120).
{ECO:0000269|PubMed:16730661}.
/FTId=VAR_028341.
VARIANT 675 675 S -> N (in arFMF; dbSNP:rs104895087).
{ECO:0000269|PubMed:10842288,
ECO:0000269|PubMed:16730661}.
/FTId=VAR_016829.
VARIANT 678 678 G -> E (in arFMF; dbSNP:rs104895088).
{ECO:0000269|PubMed:16730661}.
/FTId=VAR_028342.
VARIANT 680 680 M -> I (in arFMF and adFMF; reduced CASP1
interaction; decreased interaction with
ULK1 and diminished NLRP3 degradation
after induction of autophagy by
starvation; when associated with V-694
(PubMed:26347139); dbSNP:rs28940580).
{ECO:0000269|PubMed:10024914,
ECO:0000269|PubMed:10234504,
ECO:0000269|PubMed:10364520,
ECO:0000269|PubMed:10612841,
ECO:0000269|PubMed:10787449,
ECO:0000269|PubMed:16378925,
ECO:0000269|PubMed:16785446,
ECO:0000269|PubMed:24929125,
ECO:0000269|PubMed:26347139,
ECO:0000269|PubMed:9288094,
ECO:0000269|PubMed:9288758}.
/FTId=VAR_028343.
VARIANT 680 680 M -> L (in arFMF; dbSNP:rs104895089).
{ECO:0000269|PubMed:10842288,
ECO:0000269|PubMed:16730661}.
/FTId=VAR_016830.
VARIANT 681 681 T -> I (in arFMF; dbSNP:rs104895090).
{ECO:0000269|PubMed:10024914,
ECO:0000269|PubMed:16730661}.
/FTId=VAR_009059.
VARIANT 688 688 Y -> C (in arFMF; dbSNP:rs104895122).
{ECO:0000269|PubMed:16730661}.
/FTId=VAR_028344.
VARIANT 692 692 Missing (in arFMF).
/FTId=VAR_009060.
VARIANT 694 694 M -> I (in arFMF and adFMF; associated
with Q-148 in some patients;
dbSNP:rs28940578).
{ECO:0000269|PubMed:10024914,
ECO:0000269|PubMed:10234504,
ECO:0000269|PubMed:10612841,
ECO:0000269|PubMed:10787449,
ECO:0000269|PubMed:16378925,
ECO:0000269|PubMed:16730661,
ECO:0000269|PubMed:24929125,
ECO:0000269|PubMed:9288094}.
/FTId=VAR_009061.
VARIANT 694 694 M -> K (in arFMF).
{ECO:0000269|PubMed:23031807}.
/FTId=VAR_070798.
VARIANT 694 694 M -> L (in arFMF; dbSNP:rs61752717).
{ECO:0000269|PubMed:16730661}.
/FTId=VAR_028345.
VARIANT 694 694 M -> V (in arFMF and adFMF; very common
mutation particularly in North African
Jews; can be associated with amyloidosis
development; reduced interaction with
CASP1 and with ULK1 and diminished NLRP3
degradation after induction of autophagy
by starvation (PubMed:16785446)
(PubMed:26347139); effect on autophagic
NLRP3 degradation is increased; when
associated with I-680; no effect on
interaction with CASP1, CASP5, NLRP1,
NLRP2 or NLRP3 (PubMed:17431422);
dbSNP:rs61752717).
{ECO:0000269|PubMed:10024914,
ECO:0000269|PubMed:10234504,
ECO:0000269|PubMed:10364520,
ECO:0000269|PubMed:10612841,
ECO:0000269|PubMed:10787449,
ECO:0000269|PubMed:10854105,
ECO:0000269|PubMed:16378925,
ECO:0000269|PubMed:16730661,
ECO:0000269|PubMed:16785446,
ECO:0000269|PubMed:17431422,
ECO:0000269|PubMed:24929125,
ECO:0000269|PubMed:26347139,
ECO:0000269|PubMed:9288758}.
/FTId=VAR_009062.
VARIANT 694 694 Missing (in arFMF and adFMF).
{ECO:0000269|PubMed:10024914,
ECO:0000269|PubMed:10787449}.
/FTId=VAR_009063.
VARIANT 695 695 K -> M (in arFMF; dbSNP:rs104895094).
{ECO:0000269|PubMed:16730661}.
/FTId=VAR_028346.
VARIANT 695 695 K -> R (in arFMF; reduced penetrance
among Ashkenazi Jews; dbSNP:rs104895094).
{ECO:0000269|PubMed:10612841,
ECO:0000269|PubMed:16378925,
ECO:0000269|PubMed:16730661,
ECO:0000269|PubMed:24929125}.
/FTId=VAR_009064.
VARIANT 702 702 S -> C (in one patient with familial
Mediterranean fever; dbSNP:rs104895166).
{ECO:0000269|PubMed:16730661}.
/FTId=VAR_028347.
VARIANT 704 704 V -> I (in arFMF; dbSNP:rs104895096).
{ECO:0000269|PubMed:16730661}.
/FTId=VAR_028348.
VARIANT 705 705 P -> S (in arFMF; dbSNP:rs104895145).
{ECO:0000269|PubMed:16730661}.
/FTId=VAR_028349.
VARIANT 720 720 I -> M (in arFMF; dbSNP:rs104895102).
{ECO:0000269|PubMed:16378925,
ECO:0000269|PubMed:16730661}.
/FTId=VAR_028350.
VARIANT 726 726 V -> A (in arFMF; common mutation; in
Iraqi and Ashkenazi Jews, Druze,
Armenians; reduced interaction with CASP1
and ULK1 and diminished NLRP3 degradation
after induction of autophagy by
starvation; when associated with I-680
and V-694; no effect on CASP1 activation;
dbSNP:rs28940579).
{ECO:0000269|PubMed:10024914,
ECO:0000269|PubMed:10234504,
ECO:0000269|PubMed:10364520,
ECO:0000269|PubMed:10612841,
ECO:0000269|PubMed:16378925,
ECO:0000269|PubMed:16730661,
ECO:0000269|PubMed:16785446,
ECO:0000269|PubMed:24929125,
ECO:0000269|PubMed:9288758}.
/FTId=VAR_009065.
VARIANT 743 743 F -> L (in arFMF; dbSNP:rs104895152).
{ECO:0000269|PubMed:16730661}.
/FTId=VAR_028351.
VARIANT 744 744 A -> S (in arFMF; uncertain pathological
significance; dbSNP:rs61732874).
{ECO:0000269|PubMed:15024744,
ECO:0000269|PubMed:16378925,
ECO:0000269|PubMed:16730661,
ECO:0000269|PubMed:24929125}.
/FTId=VAR_009066.
VARIANT 758 758 P -> S (in arFMF; dbSNP:rs104895114).
{ECO:0000269|PubMed:16730661}.
/FTId=VAR_028352.
VARIANT 761 761 R -> H (in arFMF; dbSNP:rs104895097).
{ECO:0000269|PubMed:10364520,
ECO:0000269|PubMed:10612841,
ECO:0000269|PubMed:16378925,
ECO:0000269|PubMed:16730661,
ECO:0000269|PubMed:24929125}.
/FTId=VAR_009067.
VARIANT 780 780 P -> T (in arFMF; dbSNP:rs104895154).
{ECO:0000269|PubMed:16730661}.
/FTId=VAR_028353.
MUTAGEN 16 16 L->P: Does not form MEFV- and PSTPIP1-
containing perinuclear specks.
{ECO:0000269|PubMed:16037825}.
MUTAGEN 24 24 F->S: Does not form MEFV- and PSTPIP1-
containing perinuclear specks.
{ECO:0000269|PubMed:16037825}.
MUTAGEN 330 330 D->A: Loss of cleavage by CASP1.
{ECO:0000269|PubMed:18577712}.
MUTAGEN 397 404 Missing: No effect on GABARAP-binding.
Loss of GABARAP-binding; when associated
with 470-Y--G-488 and 523-S--D-530.
MUTAGEN 470 488 Missing: No effect on GABARAP-binding.
Loss of GABARAP-binding; when associated
with 397-I--H-404 and 523-S--D-530.
MUTAGEN 523 530 Missing: No effect on GABARAP-binding.
Loss of GABARAP-binding; when associated
with 397-I--H-404 and 470-Y--G-488.
HELIX 5 15 {ECO:0000244|PDB:2MPC}.
HELIX 18 28 {ECO:0000244|PDB:2MPC}.
HELIX 42 47 {ECO:0000244|PDB:2MPC}.
TURN 50 52 {ECO:0000244|PDB:2MPC}.
HELIX 53 60 {ECO:0000244|PDB:2MPC}.
HELIX 63 76 {ECO:0000244|PDB:2MPC}.
HELIX 80 92 {ECO:0000244|PDB:2MPC}.
HELIX 414 519 {ECO:0000244|PDB:4CG4}.
HELIX 524 528 {ECO:0000244|PDB:4CG4}.
HELIX 531 539 {ECO:0000244|PDB:4CG4}.
HELIX 551 583 {ECO:0000244|PDB:4CG4}.
HELIX 584 586 {ECO:0000244|PDB:4CG4}.
HELIX 590 594 {ECO:0000244|PDB:2WL1}.
TURN 604 606 {ECO:0000244|PDB:2WL1}.
STRAND 611 613 {ECO:0000244|PDB:2WL1}.
STRAND 619 622 {ECO:0000244|PDB:2WL1}.
STRAND 637 639 {ECO:0000244|PDB:2WL1}.
STRAND 642 645 {ECO:0000244|PDB:2WL1}.
STRAND 650 658 {ECO:0000244|PDB:2WL1}.
STRAND 665 671 {ECO:0000244|PDB:2WL1}.
STRAND 676 678 {ECO:0000244|PDB:2WL1}.
HELIX 684 686 {ECO:0000244|PDB:2WL1}.
STRAND 688 695 {ECO:0000244|PDB:2WL1}.
STRAND 698 701 {ECO:0000244|PDB:2WL1}.
STRAND 707 709 {ECO:0000244|PDB:4CG4}.
STRAND 716 723 {ECO:0000244|PDB:2WL1}.
TURN 724 727 {ECO:0000244|PDB:2WL1}.
STRAND 728 733 {ECO:0000244|PDB:2WL1}.
TURN 734 737 {ECO:0000244|PDB:2WL1}.
STRAND 738 743 {ECO:0000244|PDB:2WL1}.
STRAND 752 757 {ECO:0000244|PDB:2WL1}.
HELIX 762 764 {ECO:0000244|PDB:2WL1}.
STRAND 770 773 {ECO:0000244|PDB:2WL1}.
SEQUENCE 781 AA; 86444 MW; 3692E5E6E9FC8204 CRC64;
MAKTPSDHLL STLEELVPYD FEKFKFKLQN TSVQKEHSRI PRSQIQRARP VKMATLLVTY
YGEEYAVQLT LQVLRAINQR LLAEELHRAA IQEYSTQENG TDDSAASSSL GENKPRSLKT
PDHPEGNEGN GPRPYGGGAA SLRCSQPEAG RGLSRKPLSK RREKASEGLD AQGKPRTRSP
ALPGGRSPGP CRALEGGQAE VRLRRNASSA GRLQGLAGGA PGQKECRPFE VYLPSGKMRP
RSLEVTISTG EKAPANPEIL LTLEEKTAAN LDSATEPRAR PTPDGGASAD LKEGPGNPEH
SVTGRPPDTA ASPRCHAQEG DPVDGTCVRD SCSFPEAVSG HPQASGSRSP GCPRCQDSHE
RKSPGSLSPQ PLPQCKRHLK QVQLLFCEDH DEPICLICSL SQEHQGHRVR PIEEVALEHK
KKIQKQLEHL KKLRKSGEEQ RSYGEEKAVS FLKQTEALKQ RVQRKLEQVY YFLEQQEHFF
VASLEDVGQM VGQIRKAYDT RVSQDIALLD ALIGELEAKE CQSEWELLQD IGDILHRAKT
VPVPEKWTTP QEIKQKIQLL HQKSEFVEKS TKYFSETLRS EMEMFNVPEL IGAQAHAVNV
ILDAETAYPN LIFSDDLKSV RLGNKWERLP DGPQRFDSCI IVLGSPSFLS GRRYWEVEVG
DKTAWILGAC KTSISRKGNM TLSPENGYWV VIMMKENEYQ ASSVPPTRLL IKEPPKRVGI
FVDYRVGSIS FYNVTARSHI YTFASCSFSG PLQPIFSPGT RDGGKNTAPL TICPVGGQGP
D


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