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Caspase-4 (CASP-4) (EC 3.4.22.57) (ICE and Ced-3 homolog 2) (ICH-2) (ICE(rel)-II) (Mih1) (Protease TX) [Cleaved into: Caspase-4 subunit 1; Caspase-4 subunit 2]

 CASP4_HUMAN             Reviewed;         377 AA.
P49662; A2NHL8; A2NHL9; A2NHM0; B3KPZ9; B4DJH5; B4E2D2; O95601;
Q7KYX7; Q9UG96;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
30-AUG-2017, entry version 172.
RecName: Full=Caspase-4;
Short=CASP-4;
EC=3.4.22.57 {ECO:0000269|PubMed:23516580};
AltName: Full=ICE and Ced-3 homolog 2 {ECO:0000303|PubMed:7797510};
Short=ICH-2 {ECO:0000303|PubMed:7797510};
AltName: Full=ICE(rel)-II {ECO:0000303|PubMed:7797592};
AltName: Full=Mih1 {ECO:0000303|Ref.4};
AltName: Full=Protease TX {ECO:0000303|PubMed:7743998};
Contains:
RecName: Full=Caspase-4 subunit 1;
Contains:
RecName: Full=Caspase-4 subunit 2;
Flags: Precursor;
Name=CASP4; Synonyms=ICH2;
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), FUNCTION, MUTAGENESIS OF
CYS-258, 3D-STRUCTURE MODELING, AUTOCATALYSIS, AND TISSUE SPECIFICITY.
TISSUE=Placenta;
PubMed=7743998;
Faucheu C., Diu A., Chan A.W.E., Blanchet A.-M., Miossec C., Herve F.,
Collard-Dutilleul V., Gu Y., Aldape R.A., Lippke J.A., Rocher C.,
Su M.S.-S., Livingston D.J., Hercend T., Lalanne J.-L.;
"A novel human protease similar to the interleukin-1 beta converting
enzyme induces apoptosis in transfected cells.";
EMBO J. 14:1914-1922(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE
SPECIFICITY.
TISSUE=Monocytic leukemia;
PubMed=7797592; DOI=10.1074/jbc.270.26.15870;
Munday N.A., Vaillancourt J.P., Ali A., Casano F.J., Miller D.K.,
Molineaux S.M., Yamin T.-T., Yu V.L., Nicholson D.W.;
"Molecular cloning and pro-apoptotic activity of ICErelII and
ICErelIII, members of the ICE/CED-3 family of cysteine proteases.";
J. Biol. Chem. 270:15870-15876(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
AUTOCATALYTIC CLEAVAGE AT ASP-289, AND BIOPHYSICOCHEMICAL PROPERTIES.
TISSUE=Thymus;
PubMed=7797510; DOI=10.1074/jbc.270.25.15250;
Kamens J., Paskind M., Hugunin M., Talanian R.V., Allen H., Banach D.,
Bump N.J., Hackett M.C., Johnston C.G., Li P., Mankovich J.A.,
Terranova M., Ghayur T.;
"Identification and characterization of ICH-2, a novel member of the
interleukin-1 beta-converting enzyme family of cysteine proteases.";
J. Biol. Chem. 270:15250-15256(1995).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
TISSUE=T-cell;
Fernandes-Alnemri T., Litwack G., Alnemri E.S.;
"Cloning of human ICE homolog Mih1.";
Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 4 AND 5), AND
VARIANT CYS-134.
TISSUE=Small intestine, and Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Testis;
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).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 161-263 (ISOFORM 4).
TISSUE=Uterus;
PubMed=11230166; DOI=10.1101/gr.GR1547R;
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
Wambutt R., Korn B., Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and
analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[11]
TISSUE SPECIFICITY.
PubMed=10986288; DOI=10.1074/jbc.M007255200;
Lin X.Y., Choi M.S., Porter A.G.;
"Expression analysis of the human caspase-1 subfamily reveals specific
regulation of the CASP5 gene by lipopolysaccharide and interferon-
gamma.";
J. Biol. Chem. 275:39920-39926(2000).
[12]
FUNCTION, SUBCELLULAR LOCATION, AND CLEAVAGE IN RESPONSE TO
ENDOPLASMIC RETICULUM STRESS.
PubMed=15123740; DOI=10.1083/jcb.200310015;
Hitomi J., Katayama T., Eguchi Y., Kudo T., Taniguchi M., Koyama Y.,
Manabe T., Yamagishi S., Bando Y., Imaizumi K., Tsujimoto Y.,
Tohyama M.;
"Involvement of caspase-4 in endoplasmic reticulum stress-induced
apoptosis and Abeta-induced cell death.";
J. Cell Biol. 165:347-356(2004).
[13]
INDUCTION BY LPS.
PubMed=16893518; DOI=10.1016/j.bbrc.2006.07.104;
Eckhart L., Kittel C., Gawlas S., Gruber F., Mildner M., Jilma B.,
Tschachler E.;
"Identification of a novel exon encoding the amino-terminus of the
predominant caspase-5 variants.";
Biochem. Biophys. Res. Commun. 348:682-688(2006).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[15]
INTERACTION WITH NOD2.
PubMed=18511561; DOI=10.1073/pnas.0802726105;
Hsu L.C., Ali S.R., McGillivray S., Tseng P.H., Mariathasan S.,
Humke E.W., Eckmann L., Powell J.J., Nizet V., Dixit V.M., Karin M.;
"A NOD2-NALP1 complex mediates caspase-1-dependent IL-1beta secretion
in response to Bacillus anthracis infection and muramyl dipeptide.";
Proc. Natl. Acad. Sci. U.S.A. 105:7803-7808(2008).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[17]
FUNCTION, INTERACTION WITH CASP1, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND MUTAGENESIS OF CYS-258.
PubMed=22246630; DOI=10.4049/jimmunol.1101620;
Sollberger G., Strittmatter G.E., Kistowska M., French L.E.,
Beer H.D.;
"Caspase-4 is required for activation of inflammasomes.";
J. Immunol. 188:1992-2000(2012).
[18]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORM 2), CLEAVAGE OF
INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 2), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[19]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TMEM214, AND
MUTAGENESIS OF CYS-258.
PubMed=23661706; DOI=10.1074/jbc.M113.458836;
Li C., Wei J., Li Y., He X., Zhou Q., Yan J., Zhang J., Liu Y.,
Liu Y., Shu H.B.;
"Transmembrane protein 214 (TMEM214) mediates endoplasmic reticulum
stress-induced caspase 4 enzyme activation and apoptosis.";
J. Biol. Chem. 288:17908-17917(2013).
[20]
INTERACTION WITH E.COLI NLEF (MICROBIAL INFECTION), CATALYTIC
ACTIVITY, FUNCTION, AND ENZYME REGULATION (MICROBIAL INFECTION).
PubMed=23516580; DOI=10.1371/journal.pone.0058937;
Blasche S., Mortl M., Steuber H., Siszler G., Nisa S., Schwarz F.,
Lavrik I., Gronewold T.M., Maskos K., Donnenberg M.S., Ullmann D.,
Uetz P., Kogl M.;
"The E. coli effector protein NleF is a caspase inhibitor.";
PLoS ONE 8:E58937-E58937(2013).
[21]
FUNCTION, TISSUE SPECIFICITY, AND INDUCTION BY LPS.
PubMed=25121752; DOI=10.1016/j.chom.2014.07.002;
Knodler L.A., Crowley S.M., Sham H.P., Yang H., Wrande M., Ma C.,
Ernst R.K., Steele-Mortimer O., Celli J., Vallance B.A.;
"Noncanonical inflammasome activation of caspase-4/caspase-11 mediates
epithelial defenses against enteric bacterial pathogens.";
Cell Host Microbe 16:249-256(2014).
[22]
FUNCTION, AND INDUCTION BY LPS.
PubMed=24879791; DOI=10.4049/jimmunol.1303424;
Kajiwara Y., Schiff T., Voloudakis G., Gama Sosa M.A., Elder G.,
Bozdagi O., Buxbaum J.D.;
"A critical role for human caspase-4 in endotoxin sensitivity.";
J. Immunol. 193:335-343(2014).
[23]
FUNCTION, OLIGOMERIZATION, INTERACTION WITH LPS, ENZYME REGULATION,
SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF CYS-258.
PubMed=25119034; DOI=10.1038/nature13683;
Shi J., Zhao Y., Wang Y., Gao W., Ding J., Li P., Hu L., Shao F.;
"Inflammatory caspases are innate immune receptors for intracellular
LPS.";
Nature 514:187-192(2014).
[24]
FUNCTION.
PubMed=26174085; DOI=10.1002/eji.201545523;
Schmid-Burgk J.L., Gaidt M.M., Schmidt T., Ebert T.S., Bartok E.,
Hornung V.;
"Caspase-4 mediates non-canonical activation of the NLRP3 inflammasome
in human myeloid cells.";
Eur. J. Immunol. 45:2911-2917(2015).
[25]
FUNCTION.
PubMed=26173988; DOI=10.1002/eji.201545655;
Baker P.J., Boucher D., Bierschenk D., Tebartz C., Whitney P.G.,
D'Silva D.B., Tanzer M.C., Monteleone M., Robertson A.A., Cooper M.A.,
Alvarez-Diaz S., Herold M.J., Bedoui S., Schroder K., Masters S.L.;
"NLRP3 inflammasome activation downstream of cytoplasmic LPS
recognition by both caspase-4 and caspase-5.";
Eur. J. Immunol. 45:2918-2926(2015).
[26]
FUNCTION, AND INDUCTION BY LPS.
PubMed=26508369; DOI=10.1038/ncomms9761;
Vigano E., Diamond C.E., Spreafico R., Balachander A., Sobota R.M.,
Mortellaro A.;
"Human caspase-4 and caspase-5 regulate the one-step non-canonical
inflammasome activation in monocytes.";
Nat. Commun. 6:8761-8761(2015).
[27]
FUNCTION, AND GSDMD CLEAVAGE.
PubMed=26375003; DOI=10.1038/nature15514;
Shi J., Zhao Y., Wang K., Shi X., Wang Y., Huang H., Zhuang Y.,
Cai T., Wang F., Shao F.;
"Cleavage of GSDMD by inflammatory caspases determines pyroptotic cell
death.";
Nature 526:660-665(2015).
[28]
INDUCTION BY NF-KAPPA-B.
PubMed=25695505; DOI=10.1371/journal.pone.0117953;
Yang H.J., Wang M., Wang L., Cheng B.F., Lin X.Y., Feng Z.W.;
"NF-kappaB regulates caspase-4 expression and sensitizes neuroblastoma
cells to Fas-induced apoptosis.";
PLoS ONE 10:E0117953-E0117953(2015).
[29]
FUNCTION, AND INDUCTION BY LPS AND IFNB1.
PubMed=25964352; DOI=10.1073/pnas.1421699112;
Casson C.N., Yu J., Reyes V.M., Taschuk F.O., Yadav A.,
Copenhaver A.M., Nguyen H.T., Collman R.G., Shin S.;
"Human caspase-4 mediates noncanonical inflammasome activation against
gram-negative bacterial pathogens.";
Proc. Natl. Acad. Sci. U.S.A. 112:6688-6693(2015).
[30]
FUNCTION, AND MUTAGENESIS OF CYS-258.
PubMed=28314590; DOI=10.1016/j.immuni.2017.02.011;
Wang Y., Ning X., Gao P., Wu S., Sha M., Lv M., Zhou X., Gao J.,
Fang R., Meng G., Su X., Jiang Z.;
"Inflammasome Activation Triggers Caspase-1-Mediated Cleavage of cGAS
to Regulate Responses to DNA Virus Infection.";
Immunity 46:393-404(2017).
-!- FUNCTION: Inflammatory caspase (PubMed:7797510, PubMed:23516580,
PubMed:25119034). Essential effector of NLRP3 inflammasome-
dependent CASP1 activation and IL1B and IL18 secretion in response
to non-canonical activators, such as UVB radiation, cholera
enterotoxin subunit B and cytosolic LPS (PubMed:22246630,
PubMed:26174085, PubMed:26173988, PubMed:26508369,
PubMed:25964352). Independently of NLRP3 inflammasome and CASP1,
promotes pyroptosis, through GSDMD cleavage and activation, and
IL1A, IL18 and HMGB1 release in response to non-canonical
inflammasome activators (PubMed:24879791, PubMed:25964352). Plays
a crucial role in the restriction of Salmonella typhimurium
replication in colonic epithelial cells during infection
(PubMed:25121752). In later stages of the infection, LPS from
cytosolic Salmonella triggers CASP4 activation, which ultimately
results in pyroptosis of infected cells and their extrusion into
the gut lumen, as well as in IL18 secretion. Pyroptosis limits
bacterial replication, while cytokine secretion promotes the
recruitment and activation of immune cells and triggers mucosal
inflammation. Involved in LPS-induced IL6 secretion; this activity
may not require caspase enzymatic activity (PubMed:26508369).
Involved in cell death induced by endoplasmic reticulum stress and
by treatment with cytotoxic APP peptides found Alzheimer's patient
brains (PubMed:15123740, PubMed:22246630, PubMed:23661706).
Activated by direct binding to LPS without the need of an upstream
sensor (PubMed:25119034). Does not directly process IL1B
(PubMed:7743998, PubMed:7797592, PubMed:7797510). During non-
canonical inflammasome activation, cuts MB21D1 and may play a role
in the regulation of antiviral innate immune activation
(PubMed:28314590). {ECO:0000269|PubMed:15123740,
ECO:0000269|PubMed:22246630, ECO:0000269|PubMed:23516580,
ECO:0000269|PubMed:23661706, ECO:0000269|PubMed:24879791,
ECO:0000269|PubMed:25119034, ECO:0000269|PubMed:25121752,
ECO:0000269|PubMed:25964352, ECO:0000269|PubMed:26173988,
ECO:0000269|PubMed:26174085, ECO:0000269|PubMed:26508369,
ECO:0000269|PubMed:28314590, ECO:0000269|PubMed:7743998,
ECO:0000269|PubMed:7797510, ECO:0000269|PubMed:7797592}.
-!- CATALYTIC ACTIVITY: Strict requirement for Asp at the P1 position.
It has a preferred cleavage sequence of Tyr-Val-Ala-Asp-|- but
also cleaves at Asp-Glu-Val-Asp-|-. {ECO:0000269|PubMed:23516580}.
-!- ENZYME REGULATION: Activated by homooligomerization induced by
direct binding to cytosolic LPS, in a TLR4-independent manner
(PubMed:25119034). {ECO:0000269|PubMed:25119034}.
-!- ENZYME REGULATION: (Microbial infection) Inhibited by the effector
protein NleF produced by pathogenic E.coli; this inhibits
apoptosis (PubMed:23516580). {ECO:0000269|PubMed:23516580}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=681 uM for synthetic peptide acetyl-YVAD-p-nitroanilide
{ECO:0000269|PubMed:7797510};
Note=Values obtained using the partial C-terminal enzyme
sequence of 105-377. {ECO:0000269|PubMed:7797510};
-!- SUBUNIT: Upon direct LPS-binding, forms large homooligomers,
resulting in its activation. These oligomers are often referred to
as 'non-canonical inflammasomes' (PubMed:25119034). Active as a
heterotetramer consisting of two anti-parallel arranged
heterodimers, each one formed by a small and a large subunit (By
similarity). In its precursor form, interacts with TMEM214; this
interaction is required for association with the endoplasmic
reticulum membrane (PubMed:23661706). Interacts with CASP1
(PubMed:22246630). Interacts with NOD2 (PubMed:18511561).
{ECO:0000250, ECO:0000269|PubMed:18511561,
ECO:0000269|PubMed:22246630, ECO:0000269|PubMed:23661706,
ECO:0000269|PubMed:25119034}.
-!- SUBUNIT: (Microbial infection) Interacts with NleF protein from
pathogenic E.coli; this interaction leads to enzyme inhibition.
{ECO:0000269|PubMed:23516580}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:23661706}. Endoplasmic reticulum membrane
{ECO:0000269|PubMed:15123740, ECO:0000269|PubMed:23661706};
Peripheral membrane protein {ECO:0000269|PubMed:23661706};
Cytoplasmic side {ECO:0000269|PubMed:23661706}. Mitochondrion
{ECO:0000269|PubMed:15123740, ECO:0000269|PubMed:23661706}.
Inflammasome {ECO:0000269|PubMed:25119034,
ECO:0000269|PubMed:26508369}. Secreted
{ECO:0000269|PubMed:22246630}. Note=Predominantly localizes to the
endoplasmic reticulum (ER). Association with the ER membrane
requires TMEM214 (PubMed:15123740). Released in the extracellular
milieu by keratinocytes following UVB irradiation
(PubMed:22246630). {ECO:0000269|PubMed:15123740,
ECO:0000269|PubMed:22246630}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1; Synonyms=Alpha;
IsoId=P49662-1; Sequence=Displayed;
Name=2; Synonyms=Gamma, mih1-beta;
IsoId=P49662-2; Sequence=VSP_043495;
Note=Initiator Met-1 is removed. Ref.4 (AAC99851) sequence
differs from that shown due to a frameshift in position 19.
Contains a N-acetylalanine at position 2.
{ECO:0000244|PubMed:22814378, ECO:0000305};
Name=3; Synonyms=mih1-delta;
IsoId=P49662-3; Sequence=VSP_058177, VSP_058178;
Note=May be due to competing acceptor splice site. May be
produced at very low levels due to a premature stop codon in the
mRNA, leading to nonsense-mediated mRNA decay. {ECO:0000305};
Name=4;
IsoId=P49662-4; Sequence=VSP_058181, VSP_058182;
Note=No experimental confirmation available. {ECO:0000305};
Name=5;
IsoId=P49662-5; Sequence=VSP_058179, VSP_058180;
Note=No experimental confirmation available. {ECO:0000305};
-!- TISSUE SPECIFICITY: Widely expressed, including in keratinocytes
and colonic and small intestinal epithelial cells (at protein
level). Not detected in brain. {ECO:0000269|PubMed:10986288,
ECO:0000269|PubMed:22246630, ECO:0000269|PubMed:25121752,
ECO:0000269|PubMed:7743998, ECO:0000269|PubMed:7797510,
ECO:0000269|PubMed:7797592}.
-!- INDUCTION: In peripheral blood mononuclear cells and purified
monocytes, up-regulated by bacterial lipopolysaccharides (LPS) and
interferon-beta/IFNB1 at the mRNA level (PubMed:16893518,
PubMed:24879791). However, this increase is not observed at the
protein level, which remains constant in monocytes and other cell
types following LPS treatment (PubMed:25121752) (PubMed:26508369).
In monocyte-derived macrophages, some up-regulation at the protein
level is observed following treatment with LPS and IFNB1
(PubMed:25964352). In SH-EP1 neuroblastoma cell line, up-regulated
by NF-kappa-B RELA/p65 at both mRNA and protein levels.
{ECO:0000269|PubMed:16893518, ECO:0000269|PubMed:24879791,
ECO:0000269|PubMed:25695505}.
-!- DOMAIN: The CARD domain mediates LPS recognition and
homooligomerization. {ECO:0000269|PubMed:25119034}.
-!- PTM: In response to activation signals, including endoplasmic
reticulum stress or treatment with amyloid beta A4 protein
fragments (such as beta-amyloid protein 40), undergoes
autoproteolytic cleavage. {ECO:0000269|PubMed:15123740,
ECO:0000269|PubMed:7743998, ECO:0000269|PubMed:7797510}.
-!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC99854.1; Type=Erroneous translation; Note=Erroneous CDS prediction.; Evidence={ECO:0000305};
Sequence=EAW67050.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/casp4/";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; Z48810; CAA88750.1; -; mRNA.
EMBL; U28014; AAA75171.1; -; mRNA.
EMBL; U25804; AAA86890.1; -; mRNA.
EMBL; U28976; AAC99850.1; -; mRNA.
EMBL; U28977; AAC99851.1; ALT_FRAME; mRNA.
EMBL; U28978; AAC99852.1; -; mRNA.
EMBL; U28979; AAC99853.1; -; mRNA.
EMBL; U28979; AAC99854.1; ALT_SEQ; mRNA.
EMBL; AK057094; BAG51861.1; -; mRNA.
EMBL; AK296081; BAG58837.1; -; mRNA.
EMBL; AK304222; BAG65094.1; -; mRNA.
EMBL; EF636667; ABR09278.1; -; Genomic_DNA.
EMBL; AP001153; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP002004; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471065; EAW67050.1; ALT_SEQ; Genomic_DNA.
EMBL; CH471065; EAW67051.1; -; Genomic_DNA.
EMBL; CH471065; EAW67052.1; -; Genomic_DNA.
EMBL; BC017839; AAH17839.1; -; mRNA.
EMBL; AL050391; CAB43686.2; -; mRNA.
CCDS; CCDS41704.1; -. [P49662-2]
CCDS; CCDS8327.1; -. [P49662-1]
PIR; A57511; A57511.
RefSeq; NP_001216.1; NM_001225.3. [P49662-1]
RefSeq; NP_150649.1; NM_033306.2. [P49662-2]
RefSeq; XP_011541321.1; XM_011543019.1.
RefSeq; XP_016873886.1; XM_017018397.1.
UniGene; Hs.138378; -.
ProteinModelPortal; P49662; -.
SMR; P49662; -.
BioGrid; 107287; 34.
DIP; DIP-44806N; -.
IntAct; P49662; 3.
MINT; MINT-1533864; -.
STRING; 9606.ENSP00000388566; -.
BindingDB; P49662; -.
ChEMBL; CHEMBL2226; -.
GuidetoPHARMACOLOGY; 1620; -.
MEROPS; C14.007; -.
iPTMnet; P49662; -.
PhosphoSitePlus; P49662; -.
BioMuta; CASP4; -.
DMDM; 1352420; -.
EPD; P49662; -.
MaxQB; P49662; -.
PaxDb; P49662; -.
PeptideAtlas; P49662; -.
PRIDE; P49662; -.
DNASU; 837; -.
Ensembl; ENST00000393150; ENSP00000376857; ENSG00000196954. [P49662-2]
Ensembl; ENST00000444739; ENSP00000388566; ENSG00000196954. [P49662-1]
GeneID; 837; -.
KEGG; hsa:837; -.
UCSC; uc001pib.2; human. [P49662-1]
CTD; 837; -.
DisGeNET; 837; -.
GeneCards; CASP4; -.
HGNC; HGNC:1505; CASP4.
HPA; CAB037167; -.
HPA; HPA027588; -.
MIM; 602664; gene.
neXtProt; NX_P49662; -.
OpenTargets; ENSG00000196954; -.
PharmGKB; PA26088; -.
eggNOG; KOG3573; Eukaryota.
eggNOG; ENOG410ZQIE; LUCA.
GeneTree; ENSGT00760000118912; -.
HOGENOM; HOG000234399; -.
HOVERGEN; HBG076981; -.
InParanoid; P49662; -.
KO; K04394; -.
OMA; FFNIDQI; -.
OrthoDB; EOG091G07NO; -.
PhylomeDB; P49662; -.
TreeFam; TF102023; -.
BRENDA; 3.4.22.57; 2681.
Reactome; R-HSA-168638; NOD1/2 Signaling Pathway.
SABIO-RK; P49662; -.
ChiTaRS; CASP4; human.
GenomeRNAi; 837; -.
PRO; PR:P49662; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000196954; -.
CleanEx; HS_CASP4; -.
ExpressionAtlas; P49662; baseline and differential.
Genevisible; P49662; HS.
GO; GO:0097169; C:AIM2 inflammasome complex; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005783; C:endoplasmic reticulum; IDA:ParkinsonsUK-UCL.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0072557; C:IPAF inflammasome complex; IBA:GO_Central.
GO; GO:0005739; C:mitochondrion; IDA:ParkinsonsUK-UCL.
GO; GO:0072559; C:NLRP3 inflammasome complex; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0097153; F:cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
GO; GO:1904646; P:cellular response to amyloid-beta; IMP:ParkinsonsUK-UCL.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0097193; P:intrinsic apoptotic signaling pathway; IMP:ParkinsonsUK-UCL.
GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IMP:ParkinsonsUK-UCL.
GO; GO:0006508; P:proteolysis; TAS:ProtInc.
GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
GO; GO:0050727; P:regulation of inflammatory response; IBA:GO_Central.
CDD; cd00032; CASc; 1.
InterPro; IPR001315; CARD.
InterPro; IPR029030; Caspase-like_dom.
InterPro; IPR033139; Caspase_cys_AS.
InterPro; IPR016129; Caspase_his_AS.
InterPro; IPR011029; DEATH-like_dom.
InterPro; IPR002138; Pept_C14_p10.
InterPro; IPR001309; Pept_C14_p20.
InterPro; IPR015917; Pept_C14A.
Pfam; PF00619; CARD; 1.
PRINTS; PR00376; IL1BCENZYME.
SMART; SM00114; CARD; 1.
SMART; SM00115; CASc; 1.
SUPFAM; SSF47986; SSF47986; 1.
SUPFAM; SSF52129; SSF52129; 1.
PROSITE; PS50209; CARD; 1.
PROSITE; PS01122; CASPASE_CYS; 1.
PROSITE; PS01121; CASPASE_HIS; 1.
PROSITE; PS50207; CASPASE_P10; 1.
PROSITE; PS50208; CASPASE_P20; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
Endoplasmic reticulum; Hydrolase; Immunity; Inflammasome;
Inflammatory response; Innate immunity; Membrane; Mitochondrion;
Necrosis; Phosphoprotein; Polymorphism; Protease; Reference proteome;
Secreted; Thiol protease; Zymogen.
PROPEP 1 ?80 {ECO:0000255}.
/FTId=PRO_0000004596.
CHAIN ?81 270 Caspase-4 subunit 1.
/FTId=PRO_0000004597.
PROPEP 271 289 {ECO:0000255,
ECO:0000305|PubMed:7797510}.
/FTId=PRO_0000004598.
CHAIN 290 377 Caspase-4 subunit 2.
/FTId=PRO_0000004599.
DOMAIN 1 91 CARD. {ECO:0000255|PROSITE-
ProRule:PRU00046}.
REGION 1 59 Required for LPS-binding.
{ECO:0000250|UniProtKB:P70343}.
ACT_SITE 210 210 {ECO:0000250}.
ACT_SITE 258 258 {ECO:0000269|PubMed:22246630,
ECO:0000269|PubMed:23661706,
ECO:0000269|PubMed:25119034,
ECO:0000269|PubMed:7743998}.
MOD_RES 83 83 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
VAR_SEQ 1 56 Missing (in isoform 2).
{ECO:0000303|Ref.4}.
/FTId=VSP_043495.
VAR_SEQ 88 116 AHPNMEAGPPESGESTDALKLCPHEEFLR -> GDKLGHRG
RNHNLCSAISCSSSEYGGWTT (in isoform 3).
{ECO:0000303|Ref.4}.
/FTId=VSP_058177.
VAR_SEQ 117 377 Missing (in isoform 3).
{ECO:0000303|Ref.4}.
/FTId=VSP_058178.
VAR_SEQ 125 157 IYPIKERNNRTRLALIICNTEFDHLPPRNGADF -> VLCY
LYEIEKKEEISLLSFSAPFLTALNDWGWG (in isoform
5). {ECO:0000303|PubMed:14702039}.
/FTId=VSP_058179.
VAR_SEQ 158 377 Missing (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_058180.
VAR_SEQ 261 263 ANR -> GEC (in isoform 4).
{ECO:0000303|PubMed:11230166,
ECO:0000303|PubMed:14702039}.
/FTId=VSP_058181.
VAR_SEQ 264 377 Missing (in isoform 4).
{ECO:0000303|PubMed:11230166,
ECO:0000303|PubMed:14702039}.
/FTId=VSP_058182.
VARIANT 47 47 D -> N (in dbSNP:rs56226603).
/FTId=VAR_061081.
VARIANT 134 134 R -> C (in dbSNP:rs181090259).
{ECO:0000269|PubMed:14702039}.
/FTId=VAR_075654.
VARIANT 284 284 E -> D (in dbSNP:rs55901059).
/FTId=VAR_061082.
MUTAGEN 258 258 C->A: Loss of enzymatic activity. Loss of
LPS-induced pyroptosis. No effect on the
interaction with LPS. Decrease in cell
death induced by TMEM214 overexpression.
Does not support IL1B and IL18 secretion
following UVB irradiation.
{ECO:0000269|PubMed:22246630,
ECO:0000269|PubMed:23661706,
ECO:0000269|PubMed:25119034,
ECO:0000269|PubMed:28314590}.
MUTAGEN 258 258 C->S: Loss of autocatalysis.
{ECO:0000269|PubMed:7743998}.
SEQUENCE 377 AA; 43262 MW; DC7CCEC6E9D483EB CRC64;
MAEGNHRKKP LKVLESLGKD FLTGVLDNLV EQNVLNWKEE EKKKYYDAKT EDKVRVMADS
MQEKQRMAGQ MLLQTFFNID QISPNKKAHP NMEAGPPESG ESTDALKLCP HEEFLRLCKE
RAEEIYPIKE RNNRTRLALI ICNTEFDHLP PRNGADFDIT GMKELLEGLD YSVDVEENLT
ARDMESALRA FATRPEHKSS DSTFLVLMSH GILEGICGTV HDEKKPDVLL YDTIFQIFNN
RNCLSLKDKP KVIIVQACRG ANRGELWVRD SPASLEVASS QSSENLEEDA VYKTHVEKDF
IAFCSSTPHN VSWRDSTMGS IFITQLITCF QKYSWCCHLE EVFRKVQQSF ETPRAKAQMP
TIERLSMTRY FYLFPGN


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