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[1]
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NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1431103 [NCBI, ExPASy, EBI, Israel, Japan]
Nett-Fiordalisi M.A.,
Cerretti D.P.,
Berson D.R.,
Gilbert D.J.,
Jenkins N.A.,
Copeland N.G.,
Black R.A.,
Chaplin D.D.;
"Molecular cloning of the murine IL-1 beta converting enzyme cDNA.";
J. Immunol. 149:3254-3259(1992).
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[2]
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NUCLEOTIDE SEQUENCE.
PubMed=8446594 [NCBI, ExPASy, EBI, Israel, Japan]
Molineaux S.M.,
Casano F.J.,
Rolando A.M.,
Peterson E.P.,
Limjuco G.,
Chin J.,
Griffin P.R.,
Calaycay J.R.,
Ding G.J.-F.,
Yamin T.-T.,
Palyha O.C.,
Luell S.,
Fletcher D.,
Miller D.K.,
Howard A.D.,
Thornberry N.A.,
Kostura M.J.;
"Interleukin 1 beta (IL-1 beta) processing in murine macrophages requires a structurally conserved homologue of human IL-1 beta converting enzyme.";
Proc. Natl. Acad. Sci. U.S.A. 90:1809-1813(1993).
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[3]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=129;
DOI=10.1006/geno.1994.1203; PubMed=8034321 [NCBI, ExPASy, EBI, Israel, Japan]
Casano F.J.,
Rolando A.M.,
Mudgett J.S.,
Molineaux S.M.;
"The structure and complete nucleotide sequence of the murine gene encoding interleukin-1 beta converting enzyme (ICE).";
Genomics 20:474-481(1994).
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[4]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N;
TISSUE=Mammary gland;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
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[5]
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CHARACTERIZATION.
STRAIN=C3H/An;
DOI=10.1016/S0014-5793(97)00026-4; PubMed=9038361 [NCBI, ExPASy, EBI, Israel, Japan]
van de Craen M.,
Vandenabeele P.,
Declercq W.,
van den Brande I.,
van Loo G.,
Molemans F.,
Schotte P.,
van Criekinge W.,
Beyaert R.,
Fiers W.;
"Characterization of seven murine caspase family members.";
FEBS Lett. 403:61-69(1997).
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- FUNCTION: Thiol protease that cleaves IL-1 beta between an Asp and an Ala, releasing the mature cytokine which is involved in a variety of inflammatory processes. Important for defense against pathogens. Cleaves and activates sterol regulatory element binding proteins (SREBPs). Can also promote apoptosis.
- CATALYTIC ACTIVITY: Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Tyr-Val-Ala-Asp-|-.
- SUBUNIT: Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a 20 kDa (p20) and a 10 kDa (p10) subunit. The p20 subunit can also form a heterodimer with the epsilon isoform which then has an inhibitory effect. May be a component of the inflammasome, a protein complex which also includes PYCARD, CARD8 and NALP2 and whose function would be the activation of proinflammatory caspases. Interacts with INCA (By similarity).
- INTERACTION:
P18011:ipaB (xeno); NbExp=3; IntAct=EBI-489700, EBI-490239;
Q56134:sipB (xeno); NbExp=2; IntAct=EBI-489700, EBI-489689;
- SUBCELLULAR LOCATION: Cytoplasm.
- TISSUE SPECIFICITY: High level expression seen in spleen and lung, low level expression seen in brain, heart, liver, kidney, testis and skeletal muscle.
- PTM: The two subunits are derived from the precursor sequence by a autocatalytic mechanism.
- SIMILARITY: Belongs to the peptidase C14 family [view classification].
- SIMILARITY: Contains 1 CARD domain.
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 402 AA [This is the length of the unprocessed precursor] |
Molecular weight: 45640 Da [This is the MW of the unprocessed precursor] |
CRC64: 3BEBCEFA67C69B03 [This is a checksum on the sequence] |
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10 20 30 40 50 60
MADKILRAKR KQFINSVSIG TINGLLDELL EKRVLNQEEM DKIKLANITA MDKARDLCDH
70 80 90 100 110 120
VSKKGPQASQ IFITYICNED CYLAGILELQ SAPSAETFVA TEDSKGGHPS SSETKEEQNK
130 140 150 160 170 180
EDGTFPGLTG TLKFCPLEKA QKLWKENPSE IYPIMNTTTR TRLALIICNT EFQHLSPRVG
190 200 210 220 230 240
AQVDLREMKL LLEDLGYTVK VKENLTALEM VKEVKEFAAC PEHKTSDSTF LVFMSHGIQE
250 260 270 280 290 300
GICGTTYSNE VSDILKVDTI FQMMNTLKCP SLKDKPKVII IQACRGEKQG VVLLKDSVRD
310 320 330 340 350 360
SEEDFLTDAI FEDDGIKKAH IEKDFIAFCS STPDNVSWRH PVRGSLFIES LIKHMKEYAW
370 380 390 400
SCDLEDIFRK VRFSFEQPEF RLQMPTADRV TLTKRFYLFP GH
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P29452 in FASTA format |
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ExPASy Home page
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