LOCUS 417490 869 aa 01-NOV-1997

DEFINITION 1-PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE PHOSPHODIESTERASE 1 (PLC-1) (PHOSPHOLIPASE C-1).

ACCESSION 417490 PID g417490 DBSOURCE SWISS-PROT: locus PLC1_YEAST, accession P32383 class: standard. created: Oct 1, 1993. sequence updated: Oct 1, 1993. annotation updated: Nov 1, 1997. xrefs: gi: 287611, gi: 287612, gi: 295640, gi: 295642, gi: 386552, gi: 1370552, gi: 422173, gi: 477132 xrefs (non-sequence databases): SGD L0001448, PROSITE PS00018, PROSITE PS50004, PROSITE PS50007, PROSITE PS50008 KEYWORDS HYDROLASE; LIPID DEGRADATION; TRANSDUCER; CALCIUM-BINDING.

SOURCE baker's yeast.

ORGANISM Saccharomyces cerevisiae Eukaryotae; Fungi; Ascomycota; Hemiascomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.

REFERENCE 1 (residues 1 to 869)

AUTHORS Yoko-o,T., Matsui,Y., Yagisawa,H., Nojima,H., Uno,I. and Toh-e,A.

TITLE The putative phosphoinositide-specific phospholipase C gene, PLC1, of the yeast Saccharomyces cerevisiae is important for cell growth

JOURNAL Proc. Natl. Acad. Sci. U.S.A. 90 (5), 1804-1808 (1993)

MEDLINE 93189586 REMARK SEQUENCE FROM N.A.

REFERENCE 2 (residues 1 to 869)

AUTHORS FLICK,J.S. and THORNER,J.W. JOURNAL METH. CELL BIOL. 13, 5861-5876 (1993) REMARK SEQUENCE FROM N.A.

REFERENCE 3 (residues 1 to 869)

AUTHORS Payne,W.E. and Fitzgerald-Hayes,M.

TITLE A mutation in PLC1, a candidate phosphoinositide-specific phospholipase C gene from Saccharomyces cerevisiae, causes aberrant mitotic chromosome segregation

JOURNAL Mol. Cell. Biol. 13 (7), 4351-4364 (1993)

MEDLINE 93309469 REMARK SEQUENCE FROM N.A.

REFERENCE 4 (residues 1 to 869)

AUTHORS DELIUS,H. and HEBLING,U.

TITLE Direct Submission

JOURNAL Submitted (??-JUN-1996) TO EMBL/GENBANK/DDBJ DATA BANKS REMARK SEQUENCE FROM N.A.

REFERENCE 5 (residues 1 to 869)

AUTHORS DUESTERHOEFT,A., FLOETH,M., FRITZ,M., HILBERT,H. and MOESTL,D.

TITLE Direct Submission

JOURNAL Submitted (??-JUN-1996) TO EMBL/GENBANK/DDBJ DATA BANKS REMARK SEQUENCE FROM N.A. COMMENT [FUNCTION] THE PRODUCTION OF THE SECOND MESSENGER MOLECULES DIACYLGLYCEROL (DAG) AND INOSITOL 1,4,5-TRISPHOSPHATE (IP3) IS MEDIATED BY ACTIVATED PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C ENZYMES. THIS ENZYME IS ALSO REQUIRED FOR CELL GROWTH. [CATALYTIC ACTIVITY] 1-PHOSPHATIDYL-D-MYO-INOSITOL 4,5-BISPHOSPHATE + H(2)O = D-MYO-INOSITOL 1,4,5-TRIPHOSPHATE + DIACYGLYCEROL. [SIMILARITY] DOMAINS X AND Y ARE CONSERVED IN DIFFERENT FORMS OF PLC AND ARE ESSENTIAL FOR CATALYTIC ACTIVITY. [SIMILARITY] CONTAINS A COPY OF THE C2 DOMAIN. FEATURES Location/Qualifiers source 1..869 /organism="Saccharomyces cerevisiae" /db_xref="taxon:4932" 1..869 Protein 1..869 /product="1-PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE PHOSPHODIESTERASE 1" /EC_number="3.1.4.11" Region 159 /note="T -> M (IN REF. 2)." /region_name="Conflict" Region 181 /note="A -> T (IN REF. 2)." /region_name="Conflict" Region 282..293 /region_name="Calcium binding region" Region 382..520 /note="DOMAIN X." /region_name="Domain" Site 395 /site_type="active" Site 439 /site_type="active" Region 581 /note="A -> V (IN REF. 2)." /region_name="Conflict" Region 590..709 /note="DOMAIN Y." /region_name="Domain" Region 734..846 /note="C2 DOMAIN." /region_name="Domain"

ORIGIN 1 mtesaiddqr fnltkelqrh scrdqgkitq kddaldfisy ssfqssfntd qksanngstv 61 rrsirsifrr aaelprvhmg pltyshgine lvnkklrkdc dlstlcrvlq rgirmirmtr 121 rrrkfyefkl innngqiiwk dgskylelds vkdirigdta styqeevdpk rlrsdsklwi 181 aiiykvsnkl kalhvvalne ldfntflsci cglvklrrel mesillpdns qfarihwqit 241 vsekeedekk dtlsfadvkk lcdkfhiyvs tgqlleffql adinhnglln yfefekfiki 301 lknrkevnmi wskftkpphs hlsfenffqf liteqheqvd rqtawsyfik yreptqltmg 361 qdgftkflke qpylvevkee lyskplnhyf iasshntyll gkqiaetpsv egyiqvlqqg 421 crcveidiwd gengpvvchg fltsaiplkt virvikkyaf itspypliis leincnkdnq 481 klaslimrev laeqlyfvgt rtdklpspre lkhkillksk ktseatrgls vnepfpssfs 541 ssyesaneqe lrmkddstns ssatnsssmq rikriglkkh adiindvsni sgihgikfrn 601 fslpesktia hcfslnerkv eymikdkhlk lsldkhnrry lmrvyphvlr ykssnfnpip 661 fwkagvqmva tnwqtndigq qlnlamfqil dhqpdgsfks gyvlkpkkll pvvtkakmip 721 liyehfengs dpvtvkiril stqllprlnd tspsrnntns fvkvefhtdd eptmpisidk 781 gtrisateas tkssqgngfn piwdaevsit lkdtdltfik fmviseetqi asvclklnyl 841 rmgyrhiplf nmegeqyifc tlfihtqil //

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