Reviewed, UniProtKB/Swiss-Prot Q92389 (AXP1_YARLI)

Names and origin

Protein names

Recommended name:
    Acid extracellular protease
    EC=3.4.23.-

Gene names

Name:	AXP1
Synonyms:	AXP
Ordered Locus Names:	YALI0B05654g

Organism

Yarrowia lipolytica (Candida lipolytica) [Complete proteome]

Taxonomic identifier

4952 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Dipodascaceae › Yarrowia

Protein attributes

Sequence length	397 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

General annotation (Comments)

Subcellular location	Secreted.
Sequence similarities	Belongs to the peptidase A1 family.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Aspartyl protease Hydrolase Protease
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	aspartic-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 17	17	Potential
	Propeptide	18 – ?		Activation peptide Potential		PRO_0000025832
	Chain	? – 397		Acid extracellular protease		PRO_0000025833
Sites
	Active site	77	1	By similarity
	Active site	264	1	By similarity
Amino acid modifications
	Glycosylation	88	1	N-linked (GlcNAc...) Potential
	Glycosylation	310	1	N-linked (GlcNAc...) Potential
	Glycosylation	314	1	N-linked (GlcNAc...) Potential
	Disulfide bond	93 ↔ 100		By similarity
	Disulfide bond	303 ↔ 343		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q92389-1 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: BD678814B4B8984F	FASTA	397	42,081
	10 20 30 40 50 60 MQFSLATLTT LLAFVAAAPA NKGFVHAPIK KQSLQAAQSK IPNFASSGPI TAELYNELMA 70 80 90 100 110 120 YQVQISLGGQ TISASIDTGS EILWVWENDS IACQVDQQDC DTDGSYNPKK SSTSKDTGVP 130 140 150 160 170 180 FNINYGKGHA DGYLYTDNAV IGGASAPGFK FGVNSGDLSS GGFSMVFGIG VNSDASTSIS 190 200 210 220 230 240 AQLQKSGEIS RNLYGMSFSD ANLAGTSNDN SEITFGAINT GRYTGSLKTI PRVATQGGYQ 250 260 270 280 290 300 HFSVSASGKF GDVDLFDNDL VILDSGTTMT YLKSDYYNAF LGGLEDLDIT LSDYSGGWHG 310 320 330 340 350 360 YPCSENSKIN FTYNFSGKEI TVTGHDLAIP GNAVNSNVDS SVCFMGVDDG GNMNLFGDTF 370 380 390 LRAIYSVYDL ERDEVSIAQA AHGKPDNYVV ITGDVPN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The extracellular acid protease gene of Yarrowia lipolytica: sequence and pH-regulated transcription." Young T.W., Wadeson A., Glover D.J., Quincey R.V., Butlin M.J., Kamei E.A. Microbiology 142:2913-2921(1996) [PubMed: 8885407] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 148.
[2]	"Genome evolution in yeasts." 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. Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CLIB 122 / E 150.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X97068 Genomic DNA. Translation: CAA65778.1. CR382128 Genomic DNA. Translation: CAG82769.1.
RefSeq	XP_500538.1.
3D structure databases
ModBase	Search...
Protein family/group databases
MEROPS	A01.036.
Genome annotation databases
GeneID	2907455.
GenomeReviews	Gene locus YALI0B05654g in contig CR382128_GR.
KEGG	yli:YALI0B05654g.
Phylogenomic databases
HOGENOM	Q92389.
OMA	ENDSIAC
OrthoDB	EOG9MKPZC
Family and domain databases
InterPro	IPR001461. Peptidase_A1. IPR001969. Peptidase_aspartic_AS. IPR009007. Peptidase_aspartic_catalytic. [Graphical view]
Gene3D	G3DSA:2.40.70.10. Pept_Aspartc_cat. 1 hit.
PANTHER	PTHR13683. Peptidase_A1. 1 hit.
Pfam	PF00026. Asp. 1 hit. [Graphical view]
PRINTS	PR00792. PEPSIN.
PROSITE	PS00141. ASP_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
PMAP-CutDB	Q92389.

Entry information

Entry name

AXP1_YARLI

Accession

Primary (citable) accession number: Q92389

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	February 1, 1997
Last modified:	November 24, 2009
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)