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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei136 – 1361By similarity
Active sitei178 – 1781By similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 2828PRO_0000004658Add
BLAST
Chaini29 – 184156Caspase-1 subunit p19/18PRO_0000004659Add
BLAST
Propeptidei185 – 19511Sequence analysisPRO_0000004660Add
BLAST
Chaini196 – 299104Caspase-1 subunit p12PRO_0000004661Add
BLAST

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

1
299
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi41 – 433Combined sources
Beta strandi57 – 6711Combined sources
Helixi82 – 9514Combined sources
Beta strandi99 – 1057Combined sources
Helixi108 – 11912Combined sources
Helixi123 – 1253Combined sources
Beta strandi126 – 13510Combined sources
Beta strandi141 – 1433Combined sources
Beta strandi145 – 1495Combined sources
Helixi153 – 1564Combined sources
Turni160 – 1623Combined sources
Helixi164 – 1663Combined sources
Beta strandi171 – 1777Combined sources
Beta strandi179 – 1824Combined sources
Beta strandi187 – 1904Combined sources
Beta strandi202 – 2043Combined sources
Beta strandi209 – 2168Combined sources
Beta strandi223 – 2253Combined sources
Turni226 – 2283Combined sources
Helixi231 – 24313Combined sources
Turni244 – 2463Combined sources
Helixi249 – 26315Combined sources
Beta strandi266 – 2683Combined sources
Helixi272 – 2743Combined sources
Beta strandi282 – 2854Combined sources
Beta strandi288 – 2903Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M72X-ray2.30A/B/C29-299[»]
2NN3X-ray3.00C/D1-299[»]
ProteinModelPortaliP89116.
SMRiP89116. Positions 40-299.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP89116.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C14A family.Curated

Family and domain databases

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1M72X-ray2.30A/B/C29-299[»]
2NN3X-ray3.00C/D1-299[»]
ProteinModelPortaliP89116.
SMRiP89116. Positions 40-299.
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

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: June 8, 2016
This is version 84 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.