Reviewed, UniProtKB/Swiss-Prot P30887 (PHO2_YARLI)

Names and origin

Protein names

Recommended name:
    Acid phosphatase
    EC=3.1.3.2

Gene names

Name:	PHO2
Ordered Locus Names:	YALI0D03465g

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

General annotation (Comments)

Function	Probably serves to scavenge phosphorus for growing cells.
Catalytic activity	A phosphate monoester + H2O = an alcohol + phosphate.
Cofactor	Magnesium By similarity.
Subcellular location	Secreted.
Sequence similarities	Belongs to the surE nucleotidase family.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
PTM	Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	acid phosphatase activity Inferred from electronic annotation. Source: EC magnesium ion binding 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
	Chain	18 – 358	341	Acid phosphatase		PRO_0000033476
Sites
	Active site	189	1	Potential
	Metal binding	49	1	Magnesium By similarity
	Metal binding	50	1	Magnesium By similarity
	Metal binding	81	1	Magnesium By similarity
	Metal binding	156	1	Magnesium By similarity
Amino acid modifications
	Glycosylation	20	1	N-linked (GlcNAc...) Potential
	Glycosylation	27	1	N-linked (GlcNAc...) Potential
	Glycosylation	32	1	N-linked (GlcNAc...) Potential
	Glycosylation	92	1	N-linked (GlcNAc...) Potential
	Glycosylation	145	1	N-linked (GlcNAc...) Potential
	Glycosylation	199	1	N-linked (GlcNAc...) Potential
	Glycosylation	278	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	228	1	G → V in CAA46331. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P30887-1 [UniParc]. Last modified October 11, 2004. Version 2. Checksum: 0362F01F892E693B	FASTA	358	38,003
	10 20 30 40 50 60 MKFSTIALPL LASAALAQTN SSHSGTNATS HNSTVPNENS KTTIVVTNDD SWASANIRAF 70 80 90 100 110 120 YDELKKEGYN VFMFAPALQQ SGTGGTFVLP KNTTLAKGAE WGSAPVGAPA WGQDEKDDHI 130 140 150 160 170 180 WYFDGTPGAA VTFGFDYALP KFHNNITVDL VVSGPNEGWN LGPFVYTLSG TEGAMYTSVL 190 200 210 220 230 240 RGVPAIAFSG ENKHTYYANA SNSETASHNI YAKASTAIVK NLLKNAKGRP SVLPYGVGLS 250 260 270 280 290 300 VNLPLVGDID PTGKCTDPKP IFTRQTGRGA ITDKLVFNET TGLFKYGDIK SDATKACLNG 310 320 330 340 350 DCFLPDETDV INNWGCYSSI SVVSTDYDAP GALAAEAQFL NRGLVEFAPT GYGSFPGN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complementation of Saccharomyces cerevisiae acid phosphatase mutation by a genomic sequence from the yeast Yarrowia lipolytica identifies a new phosphatase." Treton B.Y., le Dall M.-T., Gaillardin C. Curr. Genet. 22:345-355(1992) [PubMed: 1423722] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 20460 / W29 / CBS 7504 / IFP29.
[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	X65225 Genomic DNA. Translation: CAA46331.1. CR382130 Genomic DNA. Translation: CAG80552.1.
PIR	S19993.
RefSeq	XP_502364.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2910307.
KEGG	yli:YALI0D03465g.
Phylogenomic databases
HOGENOM	P30887.
Enzyme and pathway databases
BRENDA	3.1.3.2. 3602.
Family and domain databases
InterPro	IPR002828. SurE-like_Pase/nucleotidase. [Graphical view]
Gene3D	G3DSA:3.40.1210.10. SurE-like_Pase/nucleotidase. 1 hit.
Pfam	PF01975. SurE. 1 hit. [Graphical view]
ProDom	PD005378. SurE. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR00087. surE. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PHO2_YARLI

Accession

Primary (citable) accession number: P30887
Secondary accession number(s): Q6CAE8

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	October 11, 2004
Last modified:	June 16, 2009
This is version 54 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)