Reviewed, UniProtKB/Swiss-Prot Q6FMQ0 (PPN1_CANGA)

Names and origin

Protein names

Recommended name:
    Endopolyphosphatase
    EC=3.6.1.10

Gene names

Name:	PPN1
Ordered Locus Names:	CAGL0K06237g

Organism

Candida glabrata (Yeast) (Torulopsis glabrata) [Complete proteome]

Taxonomic identifier

5478 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Nakaseomyces › mitosporic Nakaseomyces

Protein attributes

Sequence length	663 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalyzes the hydrolysis of inorganic polyphosphate (poly P) chains of many hundreds of phosphate residues into shorter lengths By similarity.
Catalytic activity	Polyphosphate + n H2O = (n+1) oligophosphate.
Subcellular location	Vacuole membrane; Single-pass type II membrane protein.
Post-translational modification	Processing by proteases in the vacuole may be required for activation By similarity.

Ontologies

Keywords
Cellular component	Membrane Vacuole
Domain	Signal-anchor Transmembrane
Molecular function	Hydrolase
PTM	Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW vacuolar membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	endopolyphosphatase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 663	663	Endopolyphosphatase		PRO_0000058544
Regions
	Topological domain	1 – 14	14	Cytoplasmic Potential
	Transmembrane	15 – 35	21	Signal-anchor for type II membrane protein Potential
	Topological domain	36 – 663	628	Vacuolar Potential
	Compositional bias	439 – 454	16	Poly-Lys
	Compositional bias	539 – 544	6	Poly-Lys
Amino acid modifications
	Glycosylation	487	1	N-linked (GlcNAc...) Potential
	Glycosylation	526	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q6FMQ0-1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: DC75EC4189E9646C	FASTA	663	76,352
	10 20 30 40 50 60 MAVNEKDVGR KSRVSVVLWV FIALGTLFLC KNAFTFSSES IHGLKISSDD SDSVDIERQI 70 80 90 100 110 120 SLGLTPRKPV VITDLRTGNK RKLHGRFLHI TDMHPDEYYV AGTSIDNVCH SGEPTKGKDR 130 140 150 160 170 180 AAKFGNAMSG CDSPMLLMDM TLDWIDKNLK DQIDFVVWTG DNIRHDNDRT YPRTEDEIFR 190 200 210 220 230 240 MNAEVAEKIK KIFRTPNSPD PRDFAVPVVP SIGNNDVFPH NLFSLGPTLQ TREYYRLWGD 250 260 270 280 290 300 FIPEEQQRMF DRDASFFTEV IPGKLAVLSF NTLYLFKANP LVDNCDSRKQ PGYQLLLWLG 310 320 330 340 350 360 YVLDEIRERG MKVWISGHVP PIAKNYDSSC YDKFSLWMHE YRDVIIGGLY GHMNMDHFVP 370 380 390 400 410 420 VDVQAIRENM EEQQMSLLSE DERLTKTIRE HAIAAREAHL MGAKPVNKES YLDGVLDTYY 430 440 450 460 470 480 KGVLQEIEQA VDSDLDIEKK KKKKGKKKKG KKEKRTLEEI YDQHSIVQVS GSVIPTFNPS 490 500 510 520 530 540 IRVWEYNISD ITDSSSIFGE NQLEYQSWDL FFEDLEHKMK NEFDDNESSF WAASAEQNKK 550 560 570 580 590 600 KKKKNGKPDK SIPRKKPDEL PAGPGHIQQL FSPTKFVQYF ADLDSINSEY EKLIDKGLAE 610 620 630 640 650 660 HDAINKAFNY EVEYTSKDEP YPMESLLVKD YLHLAADLAR DNGLWKIFKE RAFISTGYED ERN

References

[1]

"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: ATCC 2001 / CBS 138 / IFO 0622 / NRRL Y-65.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CR380957 Genomic DNA. Translation: CAG61455.1.
RefSeq	XP_448494.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2890459.
KEGG	cgr:CAGL0K06237g.
Phylogenomic databases
HOGENOM	Q6FMQ0.
OMA	Q6FMQ0. GGLYGHM.
Enzyme and pathway databases
BRENDA	3.6.1.10. 189220.
Family and domain databases
InterPro	IPR012358. EndopolyPtase_N1. IPR004843. M-pesterase. [Graphical view]
PANTHER	PTHR10340:SF4. EndopolyPtase_N1. 1 hit.
Pfam	PF00149. Metallophos. 1 hit. [Graphical view]
PIRSF	PIRSF027093. EndopolyPtase_N1. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PPN1_CANGA

Accession

Primary (citable) accession number: Q6FMQ0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2005
Last sequence update:	July 19, 2004
Last modified:	June 16, 2009
This is version 30 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)