ID PPZ1_YEAST STANDARD; PRT; 691 AA. AC P26570; Q00979; DT 01-AUG-1992 (Rel. 23, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 01-OCT-1996 (Rel. 34, Last annotation update) DE SERINE/THREONINE PROTEIN PHOSPHATASE PP-Z1 (EC 3.1.3.16). GN PPZ1 OR YML016C OR YM9571.02C. OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycetes; Saccharomycetales; OC Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=M5; RX MEDLINE=92291038; PubMed=1318299; RA Posas F., Casamayor A., Morral N., Arino J.; RT "Molecular cloning and analysis of a yeast protein phosphatase with an RT unusual amino-terminal region."; RL J. Biol. Chem. 267:11734-11740(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=AY926; RX MEDLINE=93373936; PubMed=8396031; RA Hughes V., Mueller A., Stark M.J.R., Cohen P.T.W.; RT "Both isoforms of protein phosphatase Z are essential for the RT maintenance of cell size and integrity in Saccharomyces cerevisiae in RT response to osmotic stress."; RL Eur. J. Biochem. 216:269-279(1993). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=S288C / AB972; RA Gentles S., Bowman S., Barrell B.G., Rajandream M.A., Walsh S.V.; RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE OF 345-692 FROM N.A. RX MEDLINE=90346193; PubMed=2166691; RA Cohen P.T.W., Brewis N.D., Hughes V., Mann D.J.; RT "Protein serine/threonine phosphatases; an expanding family."; RL FEBS Lett. 268:355-359(1990). CC -!- FUNCTION: ESSENTIAL FOR THE MAINTENANCE OF CELL SIZE AND CC INTEGRITY IN RESPONSE TO OSMOTIC STRESS. CC -!- CATALYTIC ACTIVITY: A PHOSPHOPROTEIN + H(2)O = A PROTEIN + CC ORTHOPHOSPHATE (THIS ENZYME IS SERINE/THREONINE SPECIFIC). CC -!- SIMILARITY: BELONGS TO THE PPP FAMILY OF PHOSPHATASES. PP-Z CC SUBFAMILY. CC -!- CAUTION: WAS ORIGINALLY (REF.4) THOUGHT TO ORIGINATE FROM A RABBIT CC CDNA LIBRARY AND WAS KNOWN AS PROTEIN PHOSPHATASE Z (PP-Z). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X74135; CAA52232.1; -. DR EMBL; M86242; AAA34898.1; -. DR EMBL; Z49810; CAA89936.1; -. DR PIR; S11060; PARB12. DR PIR; S31265; S31265. DR PIR; S35673; S35673. DR HSSP; P08129; 1FJM. DR SGD; S0004478; PPZ1. DR INTERPRO; IPR000934; -. DR PFAM; PF00149; STphosphatase; 1. DR PRINTS; PR00114; STPHPHTASE. DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1. KW Hydrolase; Iron; Manganese; Myristate. FT INIT_MET 0 0 BY SIMILARITY. FT LIPID 1 1 MYRISTATE (POTENTIAL). FT DOMAIN 1 318 SER-RICH. FT METAL 418 418 IRON (BY SIMILARITY). FT METAL 420 420 IRON (BY SIMILARITY). FT METAL 446 446 IRON AND MANGANESE (BY SIMILARITY). FT METAL 478 478 MANGANESE (BY SIMILARITY). FT ACT_SITE 479 479 GENERAL ACID (BY SIMILARITY). FT METAL 527 527 MANGANESE (BY SIMILARITY). FT METAL 602 602 MANGANESE (BY SIMILARITY). FT CONFLICT 339 339 G -> E (IN REF. 2 AND 3). FT CONFLICT 439 439 S -> A (IN REF. 4). FT CONFLICT 648 648 E -> K (IN REF. 4). SQ SEQUENCE 691 AA; 77287 MW; BC0BD720C2109247 CRC64; GNSSSKSSKK DSHSNSSSRN PRPQVSRTET SHSVKSAKSN KSSRSRRSLP SSSTTNTNSN VPDPSTPSKP NLEVNHQRHS SHTNRYHFPS SSHSHSNSQN ELLTTPSSSS TKRPSTSRRS SYNTKAAADL PPSMIQMEPK SPILKTNNSS THVSKHKSSY SSTYYENALT DDDNDDKDND ISHTKRFSRS SNSRPSSIRS GSVSRRKSDV THEEPNNGSY SSNNQENYLV QALTRSNSHA SSLHSRKSSF GSDGNTAYST PLNSPGLSKL TDHSGEYFTS NSTSSLNHHS SRDIYPSKHI SNDDDIENSS QLSNIHASME NVNDKNNNIT DSKKDPNEGF NDIMQSSGNK NAPKKFKKPI DIDETIQKLL DAGYAAKRTK NVCLKNNEIL QICIKAREIF LSQPSLLELS PPVKIVGDVH GQYGDLLRLF TKCGFPPSSN YLFLGDYVDR GKQSLETILL LFCYKIKYPE NFFLLRGNHE CANVTRVYGF YDECKRRCNI KIWKTFIDTF NTLPLAAIVA GKIFCVHGGL SPVLNSMDEI RHVVRPTDVP DFGLINDLLW SDPTDSPNEW EDNERGVSYC YNKVAINKFL NKFGFDLVCR AHMVVEDGYE FFNDRSLVTV FSAPNYCGEF DNWGAVMSVS EGLLCSFELL DPLDSAALKQ VMKKGRQERK LANQQQQMME TSITNDNESQ Q //