PHO11/YAR071W Protein Information

Standard Name	Pho11p 1
Systematic Name	Yar071wp
ORF Classification	Verified
Description	One of three repressible acid phosphatases; glycoprotein that is transported to the cell surface by the secretory pathway; induced by phosphate starvation and coordinately regulated by PHO4 and PHO2; PHO11 has a paralog, PHO12, that arose from a segmental duplication (2, 3, 4, 5)
Name Description	PHOsphate metabolism

Experimental Data
Molecules/cell	1460 6

Predicted Sequence	Formatted Sequence or sequence in FASTA format
Length (a.a.)	467
Molecular Weight (Da)	52,757
Isoelectric Point (pI)	4.86

Click on image for expanded interactive view

Post-translational Modifications	PhosphoGRID \| PhosphoPep Database
Domains/motifs	See the graphical view and list of proteins that share domains/motifs in common with Pho11p (InterPro)
Signal Peptide(s)	There are 1 total predicted predicted signal peptide(s) (SignalP)
Physical Interactions	There are 5 total physical interactions (BioGRID)
Homologs	PDB Homologs \| BLASTP \| BLASTP v. fungi \| Fungal Alignment \| Synteny Viewer
External Sequence Databases	EBI: UPI0000131FD1 \| P35842 MIPS: YAR071W NCBI: 456155 \| 548576 \| 6319351 \| 847755 \| NP_009434.1 GenBank/EMBL/DDBJ: DAA07011.1 \| L28920 \| U19789
External Classifications	EC: 3.1.3.2 [Acid phosphatase]

Amino Acid Sequence (or in FASTA format)
1 MLKSAVYSIL AASLVNAGTI PLGKLSDIDK IGTQTEIFPF LGGSGPYYSF 51 PGDYGISRDL PESCEMKQVQ MVGRHGERYP TVSKAKSIMT TWYKLSNYTG 101 QFSGALSFLN DDYEFFIRDT KNLEMETTLA NSVNVLNPYT GEMNAKRHAR 151 DFLAQYGYMV ENQTSFAVFT SNSNRCHDTA QYFIDGLGDK FNISLQTISE 201 AESAGANTLS AHHSCPAWDD DVNDDILKKY DTKYLSGIAK RLNKENKGLN 251 LTSSDANTFF AWCAYEINAR GYSDICNIFT KDELVRFSYG QDLETYYQTG 301 PGYDVVRSVG ANLFNASVKL LKESEVQDQK VWLSFTHDTD ILNYLTTIGI 351 IDDKNNLTAE HVPFMENTFH RSWYVPQGAR VYTEKFQCSN DTYVRYVIND 401 AVVPIETCST GPGFSCEIND FYDYAEKRVA GTDFLKVCNV SSVSNSTELT 451 FFWDWNTKHY NDTLLKQ*

Amino Acid Sequence (or in FASTA format)

       1  MLKSAVYSIL AASLVNAGTI PLGKLSDIDK IGTQTEIFPF LGGSGPYYSF
      51  PGDYGISRDL PESCEMKQVQ MVGRHGERYP TVSKAKSIMT TWYKLSNYTG
     101  QFSGALSFLN DDYEFFIRDT KNLEMETTLA NSVNVLNPYT GEMNAKRHAR
     151  DFLAQYGYMV ENQTSFAVFT SNSNRCHDTA QYFIDGLGDK FNISLQTISE
     201  AESAGANTLS AHHSCPAWDD DVNDDILKKY DTKYLSGIAK RLNKENKGLN
     251  LTSSDANTFF AWCAYEINAR GYSDICNIFT KDELVRFSYG QDLETYYQTG
     301  PGYDVVRSVG ANLFNASVKL LKESEVQDQK VWLSFTHDTD ILNYLTTIGI
     351  IDDKNNLTAE HVPFMENTFH RSWYVPQGAR VYTEKFQCSN DTYVRYVIND
     401  AVVPIETCST GPGFSCEIND FYDYAEKRVA GTDFLKVCNV SSVSNSTELT
     451  FFWDWNTKHY NDTLLKQ*

external links for Pho11p

Homologs	Interaction Resources	Protein databases/Other	Localization Resources
BLASTP (NCBI)	BioGRID	SCOP Superfamily	YPL+
Ashbya (AGD)	BOND	GPMdb (Mass Spec.)	YeastGFP
Candida (CGD)	BioPIXIE	MIPS	YeastRC Public Image Repository
Candida (CGD)	CYC2008 (complexes)	Pfam domains
YGOB	Complexome	YeastRC Structure Prediction (Seattle)
YOGY	DIP
	GeneMANIA

References cited on this page View Complete Literature Guide for Pho11p

1)	Kaback, D. (1989) Personal Communication, Mortimer Map Edition 10
2)	Shnyreva MG, et al. (1996) Biochemical properties and excretion behavior of repressible acid phosphatases with altered subunit composition. Microbiol Res 151(3):291-300
3)	Praetorius-Ibba M, et al. (1997) Homologous recombination partly restores the secretion defect of underglycosylated acid phosphatase in yeast. Curr Genet 32(3):190-6
4)	Rudolph H and Hinnen A (1987) The yeast PHO5 promoter: phosphate-control elements and sequences mediating mRNA start-site selection. Proc Natl Acad Sci U S A 84(5):1340-4
5)	Katju V, et al. (2009) Variation in gene duplicates with low synonymous divergence in Saccharomyces cerevisiae relative to Caenorhabditis elegans. Genome Biol 10(7):R75
6)	Ghaemmaghami S, et al. (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41