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UniProtKB - P09230 (AEP_YARLI)
Protein
Alkaline extracellular protease
Gene
XPR2
Organism
Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica)
Status
Functioni
Major secreted protein that belongs to the subtilisin family serine proteases.
6 PublicationsMiscellaneous
The pro-region inhibits protease activity (PubMed:2649495) and plays an additional essential role in the proper folding of the protein into a conformation compatible with secretion (PubMed:1995632, PubMed:1634541).3 Publications
Its complex processing and high level of secretion make XPR2 the perfect model to study the secretion pathway.2 Publications
Caution
Strain CLIB 122 / E 150 has a defective XPR2 sequence (xpr2-322) which lacks the N-terminus (positions 1 to 34).Curated
Catalytic activityi
- Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides.6 Publications EC:3.4.21.62
Activity regulationi
The protease activity is completely inhibited by the serine inhibitor PMSF but is not affected by thiol group inhibitors and in the presence of dithiothreitol (PubMed:6750031). In the presence of high concentrations of o-phenanthroline the protease activity is only partially inhibited (PubMed:6750031). The pro-region plays an inhibitory role and may provide a mechanism for preventing premature activation in the secretory pathway (PubMed:2649495).2 Publications
pH dependencei
Optimum pH is 9.0-10.0.2 Publications
Temperature dependencei
Optimum temperature is 40 degrees Celsius.1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 200 | Charge relay systemPROSITE-ProRule annotation | 1 | |
Active sitei | 231 | Charge relay systemPROSITE-ProRule annotation | 1 | |
Active sitei | 397 | Charge relay systemPROSITE-ProRule annotation | 1 |
GO - Molecular functioni
- serine-type endopeptidase activity Source: GO_Central
Keywordsi
Molecular function | Hydrolase, Protease, Serine protease |
Protein family/group databases
MEROPSi | S08.055 |
Names & Taxonomyi
Protein namesi | Recommended name: Alkaline extracellular protease1 Publication (EC:3.4.21.625 Publications)Short name: AEP1 Publication |
Gene namesi | Name:XPR21 Publication Ordered Locus Names:YALI0F31889g |
Organismi | Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica) |
Taxonomic identifieri | 284591 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Dipodascaceae › Yarrowia › |
Proteomesi |
|
Subcellular locationi
Extracellular region or secreted
- Secreted 8 Publications
Note: Proper secretion requires TSR1.1 Publication
Extracellular region or secreted
- extracellular space Source: GO_Central
Keywords - Cellular componenti
SecretedPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 397 | S → A: Abolishes protease activity, but not maturation. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 15 | 1 PublicationAdd BLAST | 15 | |
PropeptideiPRO_0000026984 | 16 – 157 | 2 PublicationsAdd BLAST | 142 | |
ChainiPRO_0000026985 | 158 – 454 | Alkaline extracellular proteaseAdd BLAST | 297 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 123 | N-linked (GlcNAc...) asparagine1 Publication | 1 |
Post-translational modificationi
The pro-region is removed through cleavage by XPR6 after Lys156-Arg157, which yields mature active XPR2.6 Publications
The 10 consecutive -X-Ala- or -X-Pro- dipeptides located over 100 amino acids upstream of the N-terminal of mature XPR2 are subject to dipeptidyl aminopeptidase (DPAPase)-processing (PubMed:9353927). DPAPase activity is not necessary for XPR6 cleavage and for secretion of mature active XPR2 (PubMed:9353927).4 Publications
N-glycosylated. Glycosylation within the pro-region has no effect on secretion and maturation at 18 degrees Celsius, but is required for secretion at 28 degrees Celsius (PubMed:1995632).3 Publications
Keywords - PTMi
Cleavage on pair of basic residues, Glycoprotein, ZymogenPTM databases
iPTMneti | P09230 |
Expressioni
Inductioni
Expression is subject to at least 3 different regulatory controls, carbon, sulfur and nitrogen repression (PubMed:870075). Intracellular cysteine and ammonia appear to be the metabolic signals for sulfur and nitrogen repression (PubMed:870075). Moreover, pH regulates expression independently from other metabolic signals, with highest levels of AEP mRNA at pH 6.5 (PubMed:8842151, PubMed:9308186). The transcriptional activator RIM101 and the Rim pathway are required for the alkaline induction of gene expression (PubMed:9199331, PubMed:11861549). Two major upstream activation sequences (UASs) are essential for promoter activity under conditions of repression or full induction. The distal UAS (UAS1) is located at position -790 to -778, whereas the proximal UAS (UAS2) localizes at positions -148 to -124 (PubMed:8264600, PubMed:10206713).7 Publications
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 68 – 146 | Inhibitor I9Sequence analysisAdd BLAST | 79 | |
Domaini | 166 – 454 | Peptidase S8PROSITE-ProRule annotationAdd BLAST | 289 |
Sequence similaritiesi
Belongs to the peptidase S8 family.Curated
Keywords - Domaini
SignalPhylogenomic databases
InParanoidi | P09230 |
Family and domain databases
CDDi | cd04077, Peptidases_S8_PCSK9_ProteinaseK_like, 1 hit |
Gene3Di | 3.40.50.200, 1 hit |
InterProi | View protein in InterPro IPR034193, PCSK9_ProteinaseK-like IPR000209, Peptidase_S8/S53_dom IPR036852, Peptidase_S8/S53_dom_sf IPR023827, Peptidase_S8_Asp-AS IPR022398, Peptidase_S8_His-AS IPR023828, Peptidase_S8_Ser-AS IPR015500, Peptidase_S8_subtilisin-rel IPR010259, S8pro/Inhibitor_I9 |
Pfami | View protein in Pfam PF05922, Inhibitor_I9, 1 hit PF00082, Peptidase_S8, 1 hit |
PRINTSi | PR00723, SUBTILISIN |
SUPFAMi | SSF52743, SSF52743, 1 hit |
PROSITEi | View protein in PROSITE PS51892, SUBTILASE, 1 hit PS00136, SUBTILASE_ASP, 1 hit PS00137, SUBTILASE_HIS, 1 hit PS00138, SUBTILASE_SER, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P09230-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MKLATAFTIL TAVLAAPLAA PAPAPDAAPA AVPEGPAAAA YSSILSVVAK
60 70 80 90 100
QSKKFKHHKR DLDEKDQFIV VFDSSATVDQ IASEIQKLDS LVDEDSSNGI
110 120 130 140 150
TSALDLPVYT DGSGFLGFVG KFNSTIVDKL KESSVLTVEP DTIVSLPEIP
160 170 180 190 200
ASSNAKRAIQ TTPVTQWGLS RISHKKAQTG NYAYVRETVG KHPTVSYVVD
210 220 230 240 250
SGIRTTHSEF GGRAVWGANF ADTQNADLLG HGTHVAGTVG GKTYGVDANT
260 270 280 290 300
KLVAVKVFAG RSAALSVINQ GFTWALNDYI SKRDTLPRGV LNFSGGGPKS
310 320 330 340 350
ASQDALWSRA TQEGLLVAIA AGNDAVDACN DSPGNIGGST SGIITVGSID
360 370 380 390 400
SSDKISVWSG GQGSNYGTCV DVFAPGSDII SASYQSDSGT LVYSGTSMAC
410 420 430 440 450
PHVAGLASYY LSINDEVLTP AQVEALITES NTGVLPTTNL KGSPNAVAYN
GVGI
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M17741 Genomic DNA Translation: AAA35242.1 M23353 Genomic DNA Translation: AAA35250.1 CR382132 Genomic DNA No translation available. |
PIRi | A26955 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M17741 Genomic DNA Translation: AAA35242.1 M23353 Genomic DNA Translation: AAA35250.1 CR382132 Genomic DNA No translation available. |
PIRi | A26955 |
3D structure databases
SMRi | P09230 |
ModBasei | Search... |
Protein family/group databases
MEROPSi | S08.055 |
PTM databases
iPTMneti | P09230 |
Phylogenomic databases
InParanoidi | P09230 |
Family and domain databases
CDDi | cd04077, Peptidases_S8_PCSK9_ProteinaseK_like, 1 hit |
Gene3Di | 3.40.50.200, 1 hit |
InterProi | View protein in InterPro IPR034193, PCSK9_ProteinaseK-like IPR000209, Peptidase_S8/S53_dom IPR036852, Peptidase_S8/S53_dom_sf IPR023827, Peptidase_S8_Asp-AS IPR022398, Peptidase_S8_His-AS IPR023828, Peptidase_S8_Ser-AS IPR015500, Peptidase_S8_subtilisin-rel IPR010259, S8pro/Inhibitor_I9 |
Pfami | View protein in Pfam PF05922, Inhibitor_I9, 1 hit PF00082, Peptidase_S8, 1 hit |
PRINTSi | PR00723, SUBTILISIN |
SUPFAMi | SSF52743, SSF52743, 1 hit |
PROSITEi | View protein in PROSITE PS51892, SUBTILASE, 1 hit PS00136, SUBTILASE_ASP, 1 hit PS00137, SUBTILASE_HIS, 1 hit PS00138, SUBTILASE_SER, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | AEP_YARLI | |
Accessioni | P09230Primary (citable) accession number: P09230 Secondary accession number(s): Q6BZQ0 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 1, 1989 |
Last sequence update: | July 1, 1989 | |
Last modified: | February 23, 2022 | |
This is version 120 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Direct protein sequencing, Reference proteomeDocuments
- Peptidase families
Classification of peptidase families and list of entries - SIMILARITY comments
Index of protein domains and families