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Protein

Aspartic protease pep1

Gene

pep1

Organism
Aspergillus phoenicis (Aspergillus saitoi)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Secreted aspartic endopeptidase that allows assimilation of proteinaceous substrates. Can catalyze hydrolysis of the major structural proteins of basement membrane, elastin, collagen, and laminin (By similarity).By similarity

Catalytic activityi

Hydrolysis of proteins with broad specificity. Generally favors hydrophobic residues in P1 and P1', but also accepts Lys in P1, which leads to activation of trypsinogen. Does not clot milk.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei101 – 1011PROSITE-ProRule annotation
Active sitei283 – 2831PROSITE-ProRule annotation

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Aspartyl protease, Hydrolase, Protease

Protein family/group databases

MEROPSiA01.016.

Names & Taxonomyi

Protein namesi
Recommended name:
Aspartic protease pep1 (EC:3.4.23.18)
Alternative name(s):
Aspergillopepsin A
Aspergillopepsin I
Protease type XIII
Gene namesi
Name:pep1
Synonyms:pepA
OrganismiAspergillus phoenicis (Aspergillus saitoi)
Taxonomic identifieri5063 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi145 – 1451D → S: Changes specificity toward basic substrates. 1 Publication

Protein family/group databases

Allergomei8264. Asp sa AP.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence analysisAdd
BLAST
Propeptidei21 – 6949Activation peptidePRO_0000025924Add
BLAST
Chaini70 – 394325Aspartic protease pep1PRO_0000025925Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi319 ↔ 3541 Publication

Keywords - PTMi

Disulfide bond, Zymogen

Structurei

Secondary structure

1
394
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi72 – 787Combined sources
Turni80 – 823Combined sources
Beta strandi85 – 928Combined sources
Beta strandi94 – 1018Combined sources
Beta strandi107 – 1104Combined sources
Helixi116 – 1194Combined sources
Beta strandi138 – 1425Combined sources
Beta strandi144 – 1463Combined sources
Beta strandi148 – 16013Combined sources
Beta strandi163 – 17614Combined sources
Helixi178 – 1814Combined sources
Beta strandi188 – 1914Combined sources
Helixi195 – 1973Combined sources
Beta strandi201 – 2033Combined sources
Helixi208 – 2125Combined sources
Helixi213 – 2153Combined sources
Beta strandi216 – 22611Combined sources
Beta strandi229 – 2379Combined sources
Helixi240 – 2423Combined sources
Beta strandi243 – 2453Combined sources
Beta strandi248 – 2514Combined sources
Beta strandi260 – 2634Combined sources
Beta strandi265 – 2684Combined sources
Beta strandi278 – 2825Combined sources
Beta strandi288 – 2914Combined sources
Helixi293 – 3008Combined sources
Beta strandi310 – 3145Combined sources
Beta strandi316 – 3183Combined sources
Beta strandi326 – 3305Combined sources
Beta strandi333 – 3375Combined sources
Helixi339 – 3424Combined sources
Beta strandi343 – 3486Combined sources
Beta strandi352 – 3609Combined sources
Turni362 – 3643Combined sources
Beta strandi366 – 3694Combined sources
Helixi371 – 3744Combined sources
Beta strandi377 – 3826Combined sources
Turni383 – 3864Combined sources
Beta strandi387 – 3937Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IBQX-ray2.14A/B70-394[»]
ProteinModelPortaliQ12567.
SMRiQ12567. Positions 70-394.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ12567.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini85 – 391307Peptidase A1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase A1 family.Curated
Contains 1 peptidase A1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase_A1.
IPR001969. Aspartic_peptidase_AS.
IPR033121. PEPTIDASE_A1.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
PANTHERiPTHR13683. PTHR13683. 1 hit.
PfamiPF00026. Asp. 1 hit.
[Graphical view]
PRINTSiPR00792. PEPSIN.
SUPFAMiSSF50630. SSF50630. 1 hit.
PROSITEiPS00141. ASP_PROTEASE. 2 hits.
PS51767. PEPTIDASE_A1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q12567-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVVFSKTAAL VLGLSTAVSA APAPTRKGFT INQIARPANK TRTVNLPGLY
60 70 80 90 100
ARSLAKFGGT VPQSVKEAAS KGSAVTTPQN NDEEYLTPVT VGKSTLHLDF
110 120 130 140 150
DTGSADLWVF SDELPSSEQT GHDLYTPSSS ATKLSGYSWD ISYGDGSSAS
160 170 180 190 200
GDVYRDTVTV GGVTTNKQAV EAASKISSEF VQDTANDGLL GLAFSSINTV
210 220 230 240 250
QPKAQTTFFD TVKSQLDSPL FAVQLKHDAP GVYDFGYIDD SKYTGSITYT
260 270 280 290 300
DADSSQGYWG FSTDGYSIGD GSSSSSGFSA IADTGTTLIL LDDEIVSAYY
310 320 330 340 350
EQVSGAQESY EAGGYVFSCS TDLPDFTVVI GDYKAVVPGK YINYAPVSTG
360 370 380 390
SSTCYGGIQS NSGLGLSILG DVFLKSQYVV FNSEGPKLGF AAQA
Length:394
Mass (Da):41,298
Last modified:November 1, 1997 - v1
Checksum:i70FC32D747101551
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D25318 Genomic DNA. Translation: BAA04988.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D25318 Genomic DNA. Translation: BAA04988.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IBQX-ray2.14A/B70-394[»]
ProteinModelPortaliQ12567.
SMRiQ12567. Positions 70-394.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei8264. Asp sa AP.
MEROPSiA01.016.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ12567.

Family and domain databases

Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase_A1.
IPR001969. Aspartic_peptidase_AS.
IPR033121. PEPTIDASE_A1.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
PANTHERiPTHR13683. PTHR13683. 1 hit.
PfamiPF00026. Asp. 1 hit.
[Graphical view]
PRINTSiPR00792. PEPSIN.
SUPFAMiSSF50630. SSF50630. 1 hit.
PROSITEiPS00141. ASP_PROTEASE. 2 hits.
PS51767. PEPTIDASE_A1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Primary structure of aspergillopepsin I deduced from nucleotide sequence of the gene and aspartic acid-76 is an essential active site of the enzyme for trypsinogen activation."
    Shintani T., Ichishima E.
    Biochim. Biophys. Acta 1204:257-264(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF ASP-145.
  2. "Structure of aspergillopepsin I from Aspergillus phoenicis: variations of the S1'-S2 subsite in aspartic proteinases."
    Cho S.W., Kim N., Choi M.U., Shin W.
    Acta Crystallogr. D 57:948-956(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.14 ANGSTROMS) OF 70-394, DISULFIDE BOND.

Entry informationi

Entry nameiPEPA_ASPPH
AccessioniPrimary (citable) accession number: Q12567
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: April 13, 2016
This is version 86 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

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.