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Protein

Penicillopepsin-1

Gene

aspA

Organism
Penicillium roqueforti
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Secreted aspartic endopeptidase that allows assimilation of proteinaceous substrates. The scissile peptide bond is attacked by a nucleophilic water molecule activated by two aspartic residues in the active site. Shows a broad primary substrate specificity. Favors hydrophobic residues at the P1 and P1' positions, but can also activate trypsinogen and hydrolyze the B chain of insulin between positions 'Gly-20' and 'Glu-21'.2 Publications

Catalytic activityi

Hydrolysis of proteins with broad specificity similar to that of pepsin A, preferring hydrophobic residues at P1 and P1', but also cleaving 20-Gly-|-Glu-21 in the B chain of insulin. Clots milk, and activates trypsinogen.1 Publication

pH dependencei

Optimum pH is 3.5.1 Publication

Temperature dependencei

Optimum temperature is 50 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei103PROSITE-ProRule annotation1
Active sitei285PROSITE-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

Keywordsi

Molecular functionAspartyl protease, Hydrolase, Protease

Protein family/group databases

MEROPSiA01.026.

Names & Taxonomyi

Protein namesi
Recommended name:
Penicillopepsin-1Curated (EC:3.4.23.201 Publication)
Alternative name(s):
Acid protease1 Publication
Aspartic protease aspA1 Publication
Gene namesi
Name:aspA1 Publication
OrganismiPenicillium roqueforti
Taxonomic identifieri5082 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaePenicillium

Subcellular locationi

GO - Cellular componenti

  • extracellular region Source: UniProtKB

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
PropeptideiPRO_000040705721 – 71Activation peptide1 PublicationAdd BLAST51
ChainiPRO_000040705872 – 397Penicillopepsin-1Add BLAST326

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi311N-linked (GlcNAc...)PROSITE-ProRule annotation1
Disulfide bondi322 ↔ 357PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Expressioni

Inductioni

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

Interactioni

Subunit structurei

Monomer.By similarity

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.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Family and domain databases

CDDicd06097. Aspergillopepsin_like. 1 hit.
Gene3Di2.40.70.10. 2 hits.
InterProiView protein in InterPro
IPR001461. Aspartic_peptidase_A1.
IPR001969. Aspartic_peptidase_AS.
IPR034163. Aspergillopepsin_like.
IPR033121. PEPTIDASE_A1.
IPR021109. Peptidase_aspartic_dom.
PANTHERiPTHR13683. PTHR13683. 1 hit.
PfamiView protein in Pfam
PF00026. Asp. 1 hit.
PRINTSiPR00792. PEPSIN.
SUPFAMiSSF50630. SSF50630. 1 hit.
PROSITEiView protein in PROSITE
PS00141. ASP_PROTEASE. 2 hits.
PS51767. PEPTIDASE_A1. 1 hit.

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

CDDicd06097. Aspergillopepsin_like. 1 hit.
Gene3Di2.40.70.10. 2 hits.
InterProiView protein in InterPro
IPR001461. Aspartic_peptidase_A1.
IPR001969. Aspartic_peptidase_AS.
IPR034163. Aspergillopepsin_like.
IPR033121. PEPTIDASE_A1.
IPR021109. Peptidase_aspartic_dom.
PANTHERiPTHR13683. PTHR13683. 1 hit.
PfamiView protein in Pfam
PF00026. Asp. 1 hit.
PRINTSiPR00792. PEPSIN.
SUPFAMiSSF50630. SSF50630. 1 hit.
PROSITEiView protein in PROSITE
PS00141. ASP_PROTEASE. 2 hits.
PS51767. PEPTIDASE_A1. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPEPA_PENRO
AccessioniPrimary (citable) accession number: Q01972
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 5, 2011
Last sequence update: November 1, 1996
Last modified: February 15, 2017
This is version 75 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Used in the production of blue cheese. During the fermentation process, aspartic protease hydrolyzes casein which leads to clotting of the milk.1 Publication

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.