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Protein

Aspergillopepsin-2

Gene
N/A
Organism
Aspergillus niger
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Preferential cleavage in B chain of insulin: 3-Asn-|-Gln-4, 13-Gly-|-Ala-14, and 26-Tyr-|-Thr-27.

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Aspartyl protease, Hydrolase, Protease

Protein family/group databases

MEROPSiG01.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Aspergillopepsin-2 (EC:3.4.23.19)
Alternative name(s):
Acid protease A
Aspergillopepsin II
Proctase A
Cleaved into the following 2 chains:
Alternative name(s):
Aspergillopepsin II light chain
Alternative name(s):
Aspergillopepsin II heavy chain
OrganismiAspergillus niger
Taxonomic identifieri5061 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Sequence analysisAdd BLAST18
PropeptideiPRO_000002849519 – 591 PublicationAdd BLAST41
ChainiPRO_000002849660 – 98Aspergillopepsin-2 light chainAdd BLAST39
PropeptideiPRO_000002849799 – 1091 PublicationAdd BLAST11
ChainiPRO_0000028498110 – 282Aspergillopepsin-2 heavy chainAdd BLAST173

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei110Pyrrolidone carboxylic acid1 Publication1
Disulfide bondi115 ↔ 1391 Publication
Disulfide bondi127 ↔ 2101 Publication

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Pyrrolidone carboxylic acid, Zymogen

Proteomic databases

PaxDbiP24665.

Interactioni

Subunit structurei

Heterodimer of two noncovalently bound light and heavy chains.

Protein-protein interaction databases

STRINGi5061.CADANGAP00000047.

Structurei

Secondary structure

1282
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi61 – 72Combined sources12
Beta strandi76 – 84Combined sources9
Beta strandi94 – 96Combined sources3
Beta strandi113 – 122Combined sources10
Beta strandi124 – 126Combined sources3
Beta strandi131 – 141Combined sources11
Beta strandi144 – 154Combined sources11
Beta strandi159 – 161Combined sources3
Beta strandi171 – 180Combined sources10
Beta strandi183 – 190Combined sources8
Turni191 – 194Combined sources4
Beta strandi195 – 201Combined sources7
Beta strandi213 – 219Combined sources7
Beta strandi235 – 245Combined sources11
Beta strandi248 – 250Combined sources3
Helixi252 – 254Combined sources3
Beta strandi256 – 262Combined sources7
Beta strandi268 – 272Combined sources5
Beta strandi277 – 281Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Y43X-ray1.40A60-98[»]
B110-282[»]
3TRSX-ray1.60A/C60-98[»]
B/D110-282[»]
ProteinModelPortaliP24665.
SMRiP24665.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP24665.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase G1 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IX0Z. Eukaryota.
ENOG4111QIQ. LUCA.

Family and domain databases

InterProiIPR013320. ConA-like_dom.
IPR000250. Peptidase_G1.
[Graphical view]
PfamiPF01828. Peptidase_A4. 1 hit.
[Graphical view]
PRINTSiPR00977. SCYTLDPTASE.
SUPFAMiSSF49899. SSF49899. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P24665-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKFSTILTGS LFATAALAAP LTEKRRARKE ARAAGKRHSN PPYIPGSDKE
60 70 80 90 100
ILKLNGTTNE EYSSNWAGAV LIGDGYTKVT GEFTVPSVSA GSSGSSGYGG
110 120 130 140 150
GYGYWKNKRQ SEEYCASAWV GIDGDTCETA ILQTGVDFCY EDGQTSYDAW
160 170 180 190 200
YEWYPDYAYD FSDITISEGD SIKVTVEATS KSSGSATVEN LTTGQSVTHT
210 220 230 240 250
FSGNVEGDLC ETNAEWIVED FESGDSLVAF ADFGSVTFTN AEATSGGSTV
260 270 280
GPSDATVMDI EQDGSVLTET SVSGDSVTVT YV
Length:282
Mass (Da):29,887
Last modified:March 1, 1992 - v1
Checksum:i4EA727F9AE33F72A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M68871 Genomic DNA. Translation: AAA32687.1.
PIRiA41025.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M68871 Genomic DNA. Translation: AAA32687.1.
PIRiA41025.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Y43X-ray1.40A60-98[»]
B110-282[»]
3TRSX-ray1.60A/C60-98[»]
B/D110-282[»]
ProteinModelPortaliP24665.
SMRiP24665.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5061.CADANGAP00000047.

Protein family/group databases

MEROPSiG01.002.

Proteomic databases

PaxDbiP24665.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG410IX0Z. Eukaryota.
ENOG4111QIQ. LUCA.

Miscellaneous databases

EvolutionaryTraceiP24665.

Family and domain databases

InterProiIPR013320. ConA-like_dom.
IPR000250. Peptidase_G1.
[Graphical view]
PfamiPF01828. Peptidase_A4. 1 hit.
[Graphical view]
PRINTSiPR00977. SCYTLDPTASE.
SUPFAMiSSF49899. SSF49899. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPRTA_ASPNG
AccessioniPrimary (citable) accession number: P24665
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: November 2, 2016
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

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.