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Protein

Aspartic protease pep1

Gene

pep1

Organism
Penicillium roqueforti
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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.1 Publication

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)DescriptionActionsGraphical viewLength
Active sitei103PROSITE-ProRule annotation1
Active sitei286PROSITE-ProRule annotation1

GO - Molecular functioni

  • aspartic-type endopeptidase activity Source: UniProtKB

GO - Biological processi

  • response to ammonium ion Source: UniProtKB
  • response to pH Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Aspartyl protease, Hydrolase, Protease

Protein family/group databases

MEROPSiA01.026.

Names & Taxonomyi

Protein namesi
Recommended name:
Aspartic protease pep1 (EC:3.4.23.18)
Alternative name(s):
Penicillopepsin pep1
Gene namesi
Name:pep1
Synonyms:aspA
OrganismiPenicillium roqueforti
Taxonomic identifieri5082 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaePenicillium

Subcellular locationi

GO - Cellular componenti

  • extracellular region Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
PropeptideiPRO_000040705721 – 71Activation peptideBy similarityAdd BLAST51
ChainiPRO_000040705872 – 397Aspartic protease pep1Add BLAST326

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi311N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi322 ↔ 357By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Expressioni

Inductioni

Repressed by alkaline pH and in presence of ammonia.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ01972.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini87 – 394Peptidase A1PROSITE-ProRule annotationAdd BLAST308

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. 2 hits.
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.

Q01972-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVVFSQVTVA LTCFSAIASA AAVRQEPPQG FTVNQVQKAV PGTRTVNLPG
60 70 80 90 100
LYANALVKYG ATVPATVHAA AVSGSAITTP EADDVEYLTP VTIGSSTLNL
110 120 130 140 150
DFDTGSADLW VFSSELTSSQ QSGHDVYNVG SLGTKLSGAS WSISYGDGSS
160 170 180 190 200
ASGDVYKDTV TVGGVKATGQ AVEAAKKISS QFLQDKNNDG LLGMAFSSIN
210 220 230 240 250
TVSPTPQKTF FDTVKSSLGE PLFAVTLQGT GRPWHLRFGY IDSDKYTGTL
260 270 280 290 300
AYADVDDSDG FWSFTADSYK IGTGAAGKSI TGIADTGTTL LLLDSSIVTG
310 320 330 340 350
LLQEGYPGSQ NSSSAGGYIF PCSATLPDFT VTINGYDAVV PGKYINFAPV
360 370 380 390
STGSSSCYGG IQSNSGIGFS IFGDIFLKSQ YVVFDSEGPR LGFAAQA
Length:397
Mass (Da):41,112
Last modified:November 1, 1996 - v1
Checksum:i78993028B8A94EFE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X85984 Genomic DNA. Translation: CAA59972.1.
PIRiS52783.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X85984 Genomic DNA. Translation: CAA59972.1.
PIRiS52783.

3D structure databases

ProteinModelPortaliQ01972.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiA01.026.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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. 2 hits.
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...

Entry informationi

Entry nameiPEPA_PENRO
AccessioniPrimary (citable) accession number: Q01972
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 5, 2011
Last sequence update: November 1, 1996
Last modified: October 5, 2016
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. 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.