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Protein

Caspase-1

Gene
N/A
Organism
Spodoptera frugiperda (Fall armyworm)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the activation cascade of caspases responsible for apoptosis execution (By similarity). Inhibited by the baculovirus anti-apoptotic protein p35. Cleaves p35 and nuclear immunophilin FKBP46.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei136By similarity1
Active sitei178By similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Apoptosis

Enzyme and pathway databases

BRENDAi3.4.22.36. 5836.

Protein family/group databases

MEROPSiC14.015.

Names & Taxonomyi

Protein namesi
Recommended name:
Caspase-1 (EC:3.4.22.-)
Cleaved into the following 2 chains:
OrganismiSpodoptera frugiperda (Fall armyworm)
Taxonomic identifieri7108 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaLepidopteraGlossataDitrysiaNoctuoideaNoctuidaeAmphipyrinaeSpodoptera

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000046581 – 28Add BLAST28
ChainiPRO_000000465929 – 184Caspase-1 subunit p19/18Add BLAST156
PropeptideiPRO_0000004660185 – 195Sequence analysisAdd BLAST11
ChainiPRO_0000004661196 – 299Caspase-1 subunit p12Add BLAST104

Post-translational modificationi

The two subunits are derived from the precursor sequence by an autocatalytic mechanism.

Keywords - PTMi

Zymogen

Miscellaneous databases

PMAP-CutDBP89116.

Interactioni

Subunit structurei

Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a 19/18 kDa (p19/18) and a 12 kDa (p12) subunit.

Structurei

Secondary structure

1299
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi41 – 43Combined sources3
Beta strandi57 – 67Combined sources11
Helixi82 – 95Combined sources14
Beta strandi99 – 105Combined sources7
Helixi108 – 119Combined sources12
Helixi123 – 125Combined sources3
Beta strandi126 – 135Combined sources10
Beta strandi141 – 143Combined sources3
Beta strandi145 – 149Combined sources5
Helixi153 – 156Combined sources4
Turni160 – 162Combined sources3
Helixi164 – 166Combined sources3
Beta strandi171 – 177Combined sources7
Beta strandi179 – 182Combined sources4
Beta strandi187 – 190Combined sources4
Beta strandi202 – 204Combined sources3
Beta strandi209 – 216Combined sources8
Beta strandi223 – 225Combined sources3
Turni226 – 228Combined sources3
Helixi231 – 243Combined sources13
Turni244 – 246Combined sources3
Helixi249 – 263Combined sources15
Beta strandi266 – 268Combined sources3
Helixi272 – 274Combined sources3
Beta strandi282 – 285Combined sources4
Beta strandi288 – 290Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M72X-ray2.30A/B/C29-299[»]
2NN3X-ray3.00C/D1-299[»]
ProteinModelPortaliP89116.
SMRiP89116.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP89116.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C14A family.Curated

Family and domain databases

CDDicd00032. CASc. 1 hit.
Gene3Di3.40.50.1460. 1 hit.
InterProiIPR029030. Caspase-like_dom.
IPR033139. Caspase_cys_AS.
IPR016129. Caspase_his_AS.
IPR002138. Pept_C14_p10.
IPR001309. Pept_C14_p20.
IPR015917. Pept_C14A.
[Graphical view]
PRINTSiPR00376. IL1BCENZYME.
SMARTiSM00115. CASc. 1 hit.
[Graphical view]
SUPFAMiSSF52129. SSF52129. 1 hit.
PROSITEiPS01122. CASPASE_CYS. 1 hit.
PS01121. CASPASE_HIS. 1 hit.
PS50207. CASPASE_P10. 1 hit.
PS50208. CASPASE_P20. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P89116-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLDGKQDNGN VDSVDIKQRT NGGGDEGDAL GSNSSSQPNR VARMPVDRNA
60 70 80 90 100
PYYNMNHKHR GMAIIFNHEH FDIHSLKSRT GTNVDSDNLS KVLKTLGFKV
110 120 130 140 150
TVFPNLKSEE INKFIQQTAE MDHSDADCLL VAVLTHGELG MLYAKDTHYK
160 170 180 190 200
PDNLWYYFTA DKCPTLAGKP KLFFIQACQG DRLDGGITLS RTETDGSPST
210 220 230 240 250
SYRIPVHADF LIAFSTVPGY FSWRNTTRGS WFMQALCEEL RYAGTERDIL
260 270 280 290
TLLTFVCQKV ALDFESNAPD SAMMHQQKQV PCITSMLTRL LVFGKKQSH
Length:299
Mass (Da):33,527
Last modified:May 1, 1997 - v1
Checksum:i99F4FED09B04EEDE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U81510 mRNA. Translation: AAC47442.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U81510 mRNA. Translation: AAC47442.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M72X-ray2.30A/B/C29-299[»]
2NN3X-ray3.00C/D1-299[»]
ProteinModelPortaliP89116.
SMRiP89116.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiC14.015.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.4.22.36. 5836.

Miscellaneous databases

EvolutionaryTraceiP89116.
PMAP-CutDBP89116.

Family and domain databases

CDDicd00032. CASc. 1 hit.
Gene3Di3.40.50.1460. 1 hit.
InterProiIPR029030. Caspase-like_dom.
IPR033139. Caspase_cys_AS.
IPR016129. Caspase_his_AS.
IPR002138. Pept_C14_p10.
IPR001309. Pept_C14_p20.
IPR015917. Pept_C14A.
[Graphical view]
PRINTSiPR00376. IL1BCENZYME.
SMARTiSM00115. CASc. 1 hit.
[Graphical view]
SUPFAMiSSF52129. SSF52129. 1 hit.
PROSITEiPS01122. CASPASE_CYS. 1 hit.
PS01121. CASPASE_HIS. 1 hit.
PS50207. CASPASE_P10. 1 hit.
PS50208. CASPASE_P20. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCASP1_SPOFR
AccessioniPrimary (citable) accession number: P89116
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 1, 1997
Last modified: November 30, 2016
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.