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Alkaline extracellular protease (AEP) (EC 3.4.21.62)

 AEP_YARLI               Reviewed;         454 AA.
P09230; Q6BZQ0;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 1.
25-OCT-2017, entry version 106.
RecName: Full=Alkaline extracellular protease {ECO:0000303|PubMed:2443483};
Short=AEP {ECO:0000303|PubMed:2443483};
EC=3.4.21.62 {ECO:0000269|PubMed:2649495, ECO:0000269|PubMed:6750031, ECO:0000269|PubMed:7007321, ECO:0000269|PubMed:870075, ECO:0000269|PubMed:9353927};
Flags: Precursor;
Name=XPR2 {ECO:0000303|PubMed:7007321};
OrderedLocusNames=YALI0F31889g;
Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida
lipolytica).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Dipodascaceae; Yarrowia.
NCBI_TaxID=284591;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2443483; DOI=10.1128/jb.169.10.4621-4629.1987;
Davidow L.S., O'Donnell M.M., Kaczmarek F.S., Pereira D.A.,
Dezeeuw J.R., Franke A.E.;
"Cloning and sequencing of the alkaline extracellular protease gene of
Yarrowia lipolytica.";
J. Bacteriol. 169:4621-4629(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-200, SUBCELLULAR LOCATION,
GLYCOSYLATION, AND PROTEOLYTIC PROCESSING.
PubMed=3211132; DOI=10.1128/MCB.8.11.4904;
Matoba S., Fukayama J., Wing R.A., Ogrydziak D.M.;
"Intracellular precursors and secretion of alkaline extracellular
protease of Yarrowia lipolytica.";
Mol. Cell. Biol. 8:4904-4916(1988).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 35-454.
STRAIN=CLIB 122 / E 150;
PubMed=15229592; DOI=10.1038/nature02579;
Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
Wincker P., Souciet J.-L.;
"Genome evolution in yeasts.";
Nature 430:35-44(2004).
[4]
PROTEIN SEQUENCE OF 158-182, SUBCELLULAR LOCATION, FUNCTION, CATALYTIC
ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, AND
GLYCOSYLATION.
PubMed=6750031; DOI=10.1099/00221287-128-6-1225;
Ogrydziak D.M., Scharf S.J.;
"Alkaline extracellular protease produced by Saccharomycopsis
lipolytica CX161-1B.";
J. Gen. Microbiol. 128:1225-1234(1982).
[5]
INDUCTION, FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=870075; DOI=10.1016/0304-4165(77)90209-4;
Ogrydziak D.M., Demain A.L., Tannenbaum S.R.;
"Regulation of extracellular protease production in Candida
lipolytica.";
Biochim. Biophys. Acta 497:525-538(1977).
[6]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=7007321;
Simms P.C., Ogrydziak D.M.;
"Structural gene for the alkaline extracellular protease of
Saccharomycopsis lipolytica.";
J. Bacteriol. 145:404-409(1981).
[7]
PROTEOLYTIC PROCESSING, ENZYME REGULATION, FUNCTION, AND CATALYTIC
ACTIVITY.
PubMed=2649495;
Matoba S., Ogrydziak D.M.;
"A novel location for dipeptidyl aminopeptidase processing sites in
the alkaline extracellular protease of Yarrowia lipolytica.";
J. Biol. Chem. 264:6037-6043(1989).
[8]
PROTEOLYTIC PROCESSING, FUNCTION OF THE PRO-REGION, SUBCELLULAR
LOCATION, AND GLYCOSYLATION.
PubMed=1995632;
Fabre E., Nicaud J.-M., Lopez M.C., Gaillardin C.;
"Role of the proregion in the production and secretion of the Yarrowia
lipolytica alkaline extracellular protease.";
J. Biol. Chem. 266:3782-3790(1991).
[9]
PROTEOLYTIC PROCESSING, FUNCTION OF THE PRO-REGION, AND SUBCELLULAR
LOCATION.
PubMed=1634541;
Fabre E., Tharaud C., Gaillardin C.;
"Intracellular transit of a yeast protease is rescued by trans-
complementation with its prodomain.";
J. Biol. Chem. 267:15049-15055(1992).
[10]
PROTEOLYTIC PROCESSING, SUBCELLULAR LOCATION, AND SECRETION PATHWAY
OVERLOAD.
PubMed=7954894; DOI=10.1007/BF00326302;
Le Dall M.T., Nicaud J.M., Gaillardin C.;
"Multiple-copy integration in the yeast Yarrowia lipolytica.";
Curr. Genet. 26:38-44(1994).
[11]
INDUCTION.
PubMed=8264600; DOI=10.1128/MCB.14.1.327;
Blanchin-Roland S., Cordero Otero R.R., Gaillardin C.;
"Two upstream activation sequences control the expression of the XPR2
gene in the yeast Yarrowia lipolytica.";
Mol. Cell. Biol. 14:327-338(1994).
[12]
PROTEOLYTIC PROCESSING BY XPR6.
PubMed=8203153; DOI=10.1002/yea.320100107;
Enderlin C.S., Ogrydziak D.M.;
"Cloning, nucleotide sequence and functions of XPR6, which codes for a
dibasic processing endoprotease from the yeast Yarrowia lipolytica.";
Yeast 10:67-79(1994).
[13]
SUBCELLULAR LOCATION.
PubMed=8798620; DOI=10.1074/jbc.271.39.23895;
Mamoun C.B., Beckerich J.M., Gaillardin C.;
"The TSR1 gene of Yarrowia lipolytica is involved in the signal
recognition particle-dependent translocation pathway of secretory
proteins.";
J. Biol. Chem. 271:23895-23901(1996).
[14]
INDUCTION.
PubMed=8842151; DOI=10.1007/BF02173777;
Otero R.C., Gaillardin C.;
"Dominant mutations affecting expression of pH-regulated genes in
Yarrowia lipolytica.";
Mol. Gen. Genet. 252:311-319(1996).
[15]
INDUCTION.
PubMed=9308186; DOI=10.1099/00221287-143-9-3045;
Glover D.J., McEwen R.K., Thomas C.R., Young T.W.;
"pH-regulated expression of the acid and alkaline extracellular
proteases of Yarrowia lipolytica.";
Microbiology 143:3045-3054(1997).
[16]
SIGNAL PEPTIDE, PROTEOLYTIC PROCESSING, SUBCELLULAR LOCATION,
MUTAGENESIS OF SER-397, FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=9353927; DOI=10.1099/00221287-143-10-3263;
Matoba S., Morano K.A., Klionsky D.J., Kim K., Ogrydziak D.M.;
"Dipeptidyl aminopeptidase processing and biosynthesis of alkaline
extracellular protease from Yarrowia lipolytica.";
Microbiology 143:3263-3272(1997).
[17]
INDUCTION.
PubMed=9199331; DOI=10.1128/MCB.17.7.3966;
Lambert M., Blanchin-Roland S., Le Louedec F., Lepingle A.,
Gaillardin C.;
"Genetic analysis of regulatory mutants affecting synthesis of
extracellular proteinases in the yeast Yarrowia lipolytica:
identification of a RIM101/pacC homolog.";
Mol. Cell. Biol. 17:3966-3976(1997).
[18]
INDUCTION.
PubMed=10206713; DOI=10.1099/13500872-145-1-75;
Madzak C., Blanchin-Roland S., Cordero-Otero R.R., Gaillardin C.;
"Functional analysis of upstream regulating regions from the Yarrowia
lipolytica XPR2 promoter.";
Microbiology 145:75-87(1999).
[19]
INDUCTION.
PubMed=11861549;
Gonzalez-Lopez C.I., Szabo R., Blanchin-Roland S., Gaillardin C.;
"Genetic control of extracellular protease synthesis in the yeast
Yarrowia lipolytica.";
Genetics 160:417-427(2002).
[20]
FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=17432872; DOI=10.1021/jf0633894;
Poza M., Sestelo A.B., Ageitos J.M., Vallejo J.A., Veiga-Crespo P.,
Villa T.G.;
"Cloning and expression of the XPR2 gene from Yarrowia lipolytica in
Pichia pastoris.";
J. Agric. Food Chem. 55:3944-3948(2007).
[21]
PROTEOLYTIC PROCESSING, SUBCELLULAR LOCATION, AND SECRETION PATHWAY
OVERLOAD.
PubMed=22909173; DOI=10.1111/j.1567-1364.2012.00846.x;
Ogrydziak D.M., Nicaud J.M.;
"Characterization of Yarrowia lipolytica XPR2 multi-copy strains over-
producing alkaline extracellular protease - a system for rapidly
increasing secretory pathway cargo loads.";
FEMS Yeast Res. 12:938-948(2012).
-!- FUNCTION: Major secreted protein that belongs to the subtilisin
family serine proteases. {ECO:0000269|PubMed:17432872,
ECO:0000269|PubMed:2649495, ECO:0000269|PubMed:6750031,
ECO:0000269|PubMed:7007321, ECO:0000269|PubMed:870075,
ECO:0000269|PubMed:9353927}.
-!- CATALYTIC ACTIVITY: Hydrolysis of proteins with broad specificity
for peptide bonds, and a preference for a large uncharged residue
in P1. Hydrolyzes peptide amides. {ECO:0000269|PubMed:17432872,
ECO:0000269|PubMed:2649495, ECO:0000269|PubMed:6750031,
ECO:0000269|PubMed:7007321, ECO:0000269|PubMed:870075,
ECO:0000269|PubMed:9353927}.
-!- ENZYME REGULATION: 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). {ECO:0000269|PubMed:2649495,
ECO:0000269|PubMed:6750031}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 9.0-10.0. {ECO:0000269|PubMed:17432872,
ECO:0000269|PubMed:6750031};
Temperature dependence:
Optimum temperature is 40 degrees Celsius.
{ECO:0000269|PubMed:6750031};
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1634541,
ECO:0000269|PubMed:1995632, ECO:0000269|PubMed:22909173,
ECO:0000269|PubMed:3211132, ECO:0000269|PubMed:6750031,
ECO:0000269|PubMed:7954894, ECO:0000269|PubMed:8798620,
ECO:0000269|PubMed:9353927}. Note=Proper secretion requires TSR1.
{ECO:0000269|PubMed:8798620}.
-!- INDUCTION: 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).
{ECO:0000269|PubMed:10206713, ECO:0000269|PubMed:11861549,
ECO:0000269|PubMed:8264600, ECO:0000269|PubMed:870075,
ECO:0000269|PubMed:8842151, ECO:0000269|PubMed:9199331,
ECO:0000269|PubMed:9308186}.
-!- PTM: The pro-region is removed through cleavage by XPR6 after
Lys156-Arg157, which yields mature active XPR2.
{ECO:0000269|PubMed:1634541, ECO:0000269|PubMed:22909173,
ECO:0000269|PubMed:3211132, ECO:0000269|PubMed:7954894,
ECO:0000269|PubMed:8203153, ECO:0000269|PubMed:9353927}.
-!- PTM: 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).
{ECO:0000269|PubMed:1995632, ECO:0000269|PubMed:2649495,
ECO:0000269|PubMed:8203153, ECO:0000269|PubMed:9353927}.
-!- PTM: 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).
{ECO:0000269|PubMed:1995632, ECO:0000269|PubMed:3211132,
ECO:0000269|PubMed:6750031}.
-!- MISCELLANEOUS: 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).
{ECO:0000269|PubMed:1634541, ECO:0000269|PubMed:1995632,
ECO:0000269|PubMed:2649495}.
-!- MISCELLANEOUS: Its complex processing and high level of secretion
make XPR2 the perfect model to study the secretion pathway.
{ECO:0000269|PubMed:22909173, ECO:0000269|PubMed:7954894}.
-!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
-!- CAUTION: Strain CLIB 122 / E 150 has a defective XPR2 sequence
(xpr2-322) which lacks the N-terminus (positions 1 to 34).
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M17741; AAA35242.1; -; Genomic_DNA.
EMBL; M23353; AAA35250.1; -; Genomic_DNA.
EMBL; CR382132; -; NOT_ANNOTATED_CDS; Genomic_DNA.
PIR; A26955; A26955.
ProteinModelPortal; P09230; -.
SMR; P09230; -.
MEROPS; S08.055; -.
InParanoid; P09230; -.
OrthoDB; EOG092C4A4B; -.
Proteomes; UP000001300; Chromosome F.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
CDD; cd04077; Peptidases_S8_PCSK9_Proteinase; 1.
Gene3D; 3.30.70.80; -; 1.
Gene3D; 3.40.50.200; -; 1.
InterPro; IPR034193; PCSK9_ProteinaseK-like.
InterPro; IPR009020; Peptidase/Inhibitor_I9.
InterPro; IPR000209; Peptidase_S8/S53_dom.
InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
InterPro; IPR023827; Peptidase_S8_Asp-AS.
InterPro; IPR022398; Peptidase_S8_His-AS.
InterPro; IPR023828; Peptidase_S8_Ser-AS.
InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
InterPro; IPR010259; S8pro/Inhibitor_I9.
InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
Pfam; PF05922; Inhibitor_I9; 1.
Pfam; PF00082; Peptidase_S8; 1.
PRINTS; PR00723; SUBTILISIN.
SUPFAM; SSF52743; SSF52743; 1.
SUPFAM; SSF54897; SSF54897; 1.
PROSITE; PS00136; SUBTILASE_ASP; 1.
PROSITE; PS00137; SUBTILASE_HIS; 1.
PROSITE; PS00138; SUBTILASE_SER; 1.
1: Evidence at protein level;
Cleavage on pair of basic residues; Complete proteome;
Direct protein sequencing; Glycoprotein; Hydrolase; Protease;
Reference proteome; Secreted; Serine protease; Signal; Zymogen.
SIGNAL 1 15 {ECO:0000269|PubMed:9353927}.
PROPEP 16 157 {ECO:0000269|PubMed:6750031,
ECO:0000269|PubMed:9353927}.
/FTId=PRO_0000026984.
CHAIN 158 454 Alkaline extracellular protease.
/FTId=PRO_0000026985.
DOMAIN 197 442 Peptidase S8. {ECO:0000255}.
ACT_SITE 200 200 Charge relay system.
{ECO:0000250|UniProtKB:P04189}.
ACT_SITE 231 231 Charge relay system.
{ECO:0000250|UniProtKB:P04189}.
ACT_SITE 397 397 Charge relay system.
{ECO:0000250|UniProtKB:P04189}.
CARBOHYD 123 123 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 292 292 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 330 330 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
MUTAGEN 397 397 S->A: Abolishes protease activity, but
not maturation.
{ECO:0000269|PubMed:9353927}.
SEQUENCE 454 AA; 46906 MW; 3DFBA196048B191E CRC64;
MKLATAFTIL TAVLAAPLAA PAPAPDAAPA AVPEGPAAAA YSSILSVVAK QSKKFKHHKR
DLDEKDQFIV VFDSSATVDQ IASEIQKLDS LVDEDSSNGI TSALDLPVYT DGSGFLGFVG
KFNSTIVDKL KESSVLTVEP DTIVSLPEIP ASSNAKRAIQ TTPVTQWGLS RISHKKAQTG
NYAYVRETVG KHPTVSYVVD SGIRTTHSEF GGRAVWGANF ADTQNADLLG HGTHVAGTVG
GKTYGVDANT KLVAVKVFAG RSAALSVINQ GFTWALNDYI SKRDTLPRGV LNFSGGGPKS
ASQDALWSRA TQEGLLVAIA AGNDAVDACN DSPGNIGGST SGIITVGSID SSDKISVWSG
GQGSNYGTCV DVFAPGSDII SASYQSDSGT LVYSGTSMAC PHVAGLASYY LSINDEVLTP
AQVEALITES NTGVLPTTNL KGSPNAVAYN GVGI


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