ID INP52_YEAST Reviewed; 1183 AA. AC P50942; D6W174; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 04-NOV-2026, entry version 198. DE RecName: Full=Polyphosphatidylinositol phosphatase INP52 {ECO:0000303|PubMed:9560389}; DE AltName: Full=Synaptojanin-like protein 2 {ECO:0000303|PubMed:9788876}; DE Includes: DE RecName: Full=SAC1-like phosphoinositide phosphatase {ECO:0000303|PubMed:10224048}; DE EC=3.1.3.- {ECO:0000269|PubMed:10224048}; DE Includes: DE RecName: Full=Phosphatidylinositol 4,5-bisphosphate 5-phosphatase {ECO:0000303|PubMed:10224048}; DE EC=3.1.3.36 {ECO:0000269|PubMed:10224048}; GN Name=INP52 {ECO:0000303|PubMed:9560389}; GN Synonyms=SJL2 {ECO:0000303|PubMed:9788876}; OrderedLocusNames=YNL106C; GN ORFNames=N2160; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169873; DOI=10.1038/387s093; RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F., RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its RT evolutionary implications."; RL Nature 387:93-98(1997). RN [2] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1102. RC STRAIN=ATCC 96604 / S288c / FY1679; RX PubMed=8701612; RX DOI=10.1002/(sici)1097-0061(19960330)12:4%3c403::aid-yea923%3e3.0.co;2-h; RA Saiz J.E., Buitrago M.J., Soler A., del Rey F., Revuelta J.L.; RT "The sequence of a 21.3 kb DNA fragment from the left arm of yeast RT chromosome XIV reveals LEU4, MET4, POL1, RAS2, and six new open reading RT frames."; RL Yeast 12:403-409(1996). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 880-1183. RX PubMed=9090055; RX DOI=10.1002/(sici)1097-0061(19970315)13:3<261::aid-yea64>3.0.co;2-l; RA de Antoni A., D'Angelo M., Dal Pero F., Sartorello F., Pandolfo D., RA Pallavicini A., Lanfranchi G., Valle G.; RT "The DNA sequence of cosmid 14-13b from chromosome XIV of Saccharomyces RT cerevisiae reveals an unusually high number of overlapping open reading RT frames."; RL Yeast 13:261-266(1997). RN [5] RP FUNCTION. RX PubMed=9265642; DOI=10.1083/jcb.138.4.731; RA Luo W.-J., Chang A.; RT "Novel genes involved in endosomal traffic in yeast revealed by suppression RT of a targeting-defective plasma membrane ATPase mutant."; RL J. Cell Biol. 138:731-746(1997). RN [6] RP FUNCTION. RX PubMed=9560389; DOI=10.1093/genetics/148.4.1715; RA Stolz L.E., Huynh C.V., Thorner J., York J.D.; RT "Identification and characterization of an essential family of inositol RT polyphosphate 5-phosphatases (INP51, INP52 and INP53 gene products) in the RT yeast Saccharomyces cerevisiae."; RL Genetics 148:1715-1729(1998). RN [7] RP FUNCTION. RX PubMed=9788876; DOI=10.1242/jcs.111.22.3347; RA Singer-Krueger B., Nemoto Y., Daniell L., Ferro-Novick S., De Camilli P.; RT "Synaptojanin family members are implicated in endocytic membrane traffic RT in yeast."; RL J. Cell Sci. 111:3347-3356(1998). RN [8] RP FUNCTION, CATALYTIC ACTIVITY, AND DOMAIN. RX PubMed=10224048; DOI=10.1074/jbc.274.19.12990; RA Guo S., Stolz L.E., Lemrow S.M., York J.D.; RT "SAC1-like domains of yeast SAC1, INP52, and INP53 and of human RT synaptojanin encode polyphosphoinositide phosphatases."; RL J. Biol. Chem. 274:12990-12995(1999). RN [9] RP FUNCTION. RX PubMed=10625610; DOI=10.1074/jbc.275.2.801; RA Hughes W.E., Woscholski R., Cooke F.T., Patrick R.S., Dove S.K., RA McDonald N.Q., Parker P.J.; RT "SAC1 encodes a regulated lipid phosphoinositide phosphatase, defects in RT which can be suppressed by the homologous Inp52p and Inp53p phosphatases."; RL J. Biol. Chem. 275:801-808(2000). RN [10] RP FUNCTION, AND MUTAGENESIS OF GLU-631; HIS-730 AND ASP-771. RX PubMed=10962003; DOI=10.1074/jbc.m006244200; RA Whisstock J.C., Romero S., Gurung R., Nandurkar H., Ooms L.M., RA Bottomley S.P., Mitchell C.A.; RT "The inositol polyphosphate 5-phosphatases and the apurinic/apyrimidinic RT base excision repair endonucleases share a common mechanism for RT catalysis."; RL J. Biol. Chem. 275:37055-37061(2000). RN [11] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=11094088; DOI=10.1128/mcb.20.24.9376-9390.2000; RA Ooms L.M., McColl B.K., Wiradjaja F., Wijayaratnam A.P.W., Gleeson P., RA Gething M.J., Sambrook J.F., Mitchell C.A.; RT "The yeast inositol polyphosphate 5-phosphatases inp52p and inp53p RT translocate to actin patches following hyperosmotic stress: mechanism for RT regulating phosphatidylinositol 4,5-bisphosphate at plasma membrane RT invaginations."; RL Mol. Cell. Biol. 20:9376-9390(2000). RN [12] RP FUNCTION. RX PubMed=11311145; DOI=10.1042/bj3550805; RA O'Malley C.J., McColl B.K., Kong A.M., Ellis S.L., Wijayaratnam A.P.W., RA Sambrook J., Mitchell C.A.; RT "Mammalian inositol polyphosphate 5-phosphatase II can compensate for the RT absence of all three yeast Sac1-like-domain-containing 5-phosphatases."; RL Biochem. J. 355:805-817(2001). RN [13] RP INTERACTION WITH BSP1. RX PubMed=12606027; DOI=10.1016/s0014-5793(03)00067-x; RA Wicky S., Frischmuth S., Singer-Krueger B.; RT "Bsp1p/Ypr171p is an adapter that directly links some synaptojanin family RT members to the cortical actin cytoskeleton in yeast."; RL FEBS Lett. 537:35-41(2003). RN [14] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX PubMed=14562095; DOI=10.1038/nature02026; RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., RA Weissman J.S., O'Shea E.K.; RT "Global analysis of protein localization in budding yeast."; RL Nature 425:686-691(2003). RN [15] RP FUNCTION. RX PubMed=15169871; DOI=10.1091/mbc.e04-03-0209; RA Parrish W.R., Stefan C.J., Emr S.D.; RT "Essential role for the myotubularin-related phosphatase Ymr1p and the RT synaptojanin-like phosphatases Sjl2p and Sjl3p in regulation of RT phosphatidylinositol 3-phosphate in yeast."; RL Mol. Biol. Cell 15:3567-3579(2004). RN [16] RP FUNCTION. RX PubMed=15691741; DOI=10.1016/j.femsyr.2004.09.007; RA Nguyen P.H., Hasek J., Kohlwein S.D., Romero C., Choi J.H., Vancura A.; RT "Interaction of Pik1p and Sjl proteins in membrane trafficking."; RL FEMS Yeast Res. 5:363-371(2005). RN [17] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ABP1. RX PubMed=15798181; DOI=10.1128/mcb.25.8.2910-2923.2005; RA Stefan C.J., Padilla S.M., Audhya A., Emr S.D.; RT "The phosphoinositide phosphatase Sjl2 is recruited to cortical actin RT patches in the control of vesicle formation and fission during RT endocytosis."; RL Mol. Cell. Biol. 25:2910-2923(2005). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1005, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=YAL6B; RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200; RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., RA Jensen O.N.; RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling RT pathway."; RL Mol. Cell. Proteomics 4:310-327(2005). RN [19] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=16406366; DOI=10.1016/j.febslet.2005.12.082; RA Boettcher C., Wicky S., Schwarz H., Singer-Krueger B.; RT "Sjl2p is specifically involved in early steps of endocytosis intimately RT linked to actin dynamics via the Ark1p/Prk1p kinases."; RL FEBS Lett. 580:633-641(2006). RN [20] RP FUNCTION. RX PubMed=17452534; DOI=10.1083/jcb.200611011; RA Sun Y., Carroll S., Kaksonen M., Toshima J.Y., Drubin D.G.; RT "PtdIns(4,5)P2 turnover is required for multiple stages during RT clathrin- and actin-dependent endocytic internalization."; RL J. Cell Biol. 177:355-367(2007). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1032, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=ADR376; RX PubMed=17330950; DOI=10.1021/pr060559j; RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., RA Elias J.E., Gygi S.P.; RT "Large-scale phosphorylation analysis of alpha-factor-arrested RT Saccharomyces cerevisiae."; RL J. Proteome Res. 6:1190-1197(2007). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200; RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; RT "A multidimensional chromatography technology for in-depth phosphoproteome RT analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). RN [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-522; SER-1005 AND SER-1016, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19779198; DOI=10.1126/science.1172867; RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.; RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights RT into evolution."; RL Science 325:1682-1686(2009). CC -!- FUNCTION: Dephosphorylates a number of phosphatidylinositols (PIs) like CC phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), but also CC phosphatidylinositol 3-phosphate (PtdIns(3)P), phosphatidylinositol 4- CC phosphate (PtdIns(4)P), and phosphatidylinositol 3,5-bisphosphate CC (PtdIns(3,5)P2). Controls the cellular levels and subcellular CC distribution of phosphatidylinositol 3-phosphate and CC phosphatidylinositol 4,5-bisphosphate. Specifically functions within CC the early endocytic pathway and actin organization. CC {ECO:0000269|PubMed:10224048, ECO:0000269|PubMed:10625610, CC ECO:0000269|PubMed:10962003, ECO:0000269|PubMed:11094088, CC ECO:0000269|PubMed:11311145, ECO:0000269|PubMed:15169871, CC ECO:0000269|PubMed:15691741, ECO:0000269|PubMed:15798181, CC ECO:0000269|PubMed:16406366, ECO:0000269|PubMed:17452534, CC ECO:0000269|PubMed:9265642, ECO:0000269|PubMed:9560389, CC ECO:0000269|PubMed:9788876}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5- CC bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo- CC inositol 4-phosphate) + phosphate; Xref=Rhea:RHEA:22764, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58178, CC ChEBI:CHEBI:58456; EC=3.1.3.36; CC Evidence={ECO:0000269|PubMed:10224048}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU01427}; CC -!- SUBUNIT: Interacts (via SAC domain) with BSP1; the interaction is CC direct (PubMed:12606027). Interacts with ABP1 (PubMed:15798181). CC {ECO:0000269|PubMed:12606027, ECO:0000269|PubMed:15798181}. CC -!- INTERACTION: CC P50942; P15891: ABP1; NbExp=3; IntAct=EBI-28834, EBI-2036; CC P50942; Q06604: BSP1; NbExp=4; IntAct=EBI-28834, EBI-37047; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch CC {ECO:0000269|PubMed:11094088, ECO:0000269|PubMed:14562095, CC ECO:0000269|PubMed:15798181, ECO:0000269|PubMed:16406366}. CC -!- DOMAIN: The SAC domain is capable of hydrolyzing phosphatidylinositol CC 3-phosphate (PtdIns(3)P), phosphatidylinositol 4-phosphate CC (PtdIns(4)P), and phosphatidylinositol 3,5-bisphosphate CC (PtdIns(3,5)P2). {ECO:0000269|PubMed:10224048}. CC -!- SIMILARITY: Belongs to the synaptojanin family. {ECO:0000305}. CC -!- SIMILARITY: In the central section; belongs to the inositol 1,4,5- CC trisphosphate 5-phosphatase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z71382; CAA95982.1; -; Genomic_DNA. DR EMBL; Z69382; CAA93402.1; -; Genomic_DNA. DR EMBL; Z50161; CAA90520.1; -; Genomic_DNA. DR EMBL; BK006947; DAA10440.1; -; Genomic_DNA. DR PIR; S63046; S63046. DR RefSeq; NP_014293.1; NM_001182944.1. DR AlphaFoldDB; P50942; -. DR BMRB; P50942; -. DR SMR; P50942; -. DR BioGRID; 35718; 207. DR DIP; DIP-2764N; -. DR FunCoup; P50942; 379. DR IntAct; P50942; 27. DR MINT; P50942; -. DR STRING; 4932.YNL106C; -. DR iPTMnet; P50942; -. DR PaxDb; 4932-YNL106C; -. DR PeptideAtlas; P50942; -. DR EnsemblFungi; YNL106C_mRNA; YNL106C; YNL106C. DR GeneID; 855618; -. DR KEGG; sce:YNL106C; -. DR AGR; SGD:S000005050; -. DR SGD; S000005050; INP52. DR VEuPathDB; FungiDB:YNL106C; -. DR eggNOG; KOG0566; Eukaryota. DR HOGENOM; CLU_003016_2_0_1; -. DR InParanoid; P50942; -. DR OMA; AACTWNL; -. DR OrthoDB; 405996at2759; -. DR BioCyc; YEAST:MONOMER3O-69; -. DR Reactome; R-SCE-1660499; Synthesis of PIPs at the plasma membrane. DR Reactome; R-SCE-1855183; Synthesis of IP2, IP, and Ins in the cytosol. DR Reactome; R-SCE-1855204; Synthesis of IP3 and IP4 in the cytosol. DR BioGRID-ORCS; 855618; 0 hits in 10 CRISPR screens. DR PRO; PR:P50942; -. DR Proteomes; UP000002311; Chromosome XIV. DR RNAct; P50942; protein. DR GO; GO:0030479; C:actin cortical patch; IDA:SGD. DR GO; GO:0005737; C:cytoplasm; IDA:SGD. DR GO; GO:0043332; C:mating projection tip; HDA:SGD. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0052658; F:inositol-1,4,5-trisphosphate 5-phosphatase activity; IBA:GO_Central. DR GO; GO:0043813; F:phosphatidylinositol-3,5-bisphosphate 5-phosphatase activity; IDA:SGD. DR GO; GO:0004438; F:phosphatidylinositol-3-phosphate phosphatase activity; IDA:SGD. DR GO; GO:0004439; F:phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; IDA:SGD. DR GO; GO:0043812; F:phosphatidylinositol-4-phosphate phosphatase activity; IDA:SGD. DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IDA:SGD. DR CDD; cd09090; INPP5c_ScInp51p-like; 1. DR FunFam; 3.60.10.10:FF:000029; Inositol polyphosphate 5-phosphatase; 1. DR Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1. DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf. DR InterPro; IPR046985; IP5. DR InterPro; IPR000300; IPPc. DR InterPro; IPR002013; SAC_dom. DR PANTHER; PTHR11200; INOSITOL 5-PHOSPHATASE; 1. DR PANTHER; PTHR11200:SF257; PHOSPHOINOSITIDE 5-PHOSPHATASE; 1. DR Pfam; PF22669; Exo_endo_phos2; 1. DR Pfam; PF02383; Syja_N; 1. DR SMART; SM00128; IPPc; 1. DR SUPFAM; SSF56219; DNase I-like; 1. DR PROSITE; PS52082; 5_PPASE; 1. DR PROSITE; PS50275; SAC; 1. PE 1: Evidence at protein level; KW Cytoplasm; Cytoskeleton; Endocytosis; Hydrolase; Lipid metabolism; KW Magnesium; Metal-binding; Phosphoprotein; Protein transport; KW Reference proteome; Transport. FT CHAIN 1..1183 FT /note="Polyphosphatidylinositol phosphatase INP52" FT /id="PRO_0000209745" FT DOMAIN 167..507 FT /note="SAC" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00183" FT DOMAIN 586..888 FT /note="5-PPase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01427" FT REGION 133..161 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 955..1183 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 133..153 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 955..968 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1046..1057 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1082..1100 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1130..1145 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 771 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01427" FT BINDING 601 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01427" FT BINDING 631 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01427" FT MOD_RES 152 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956" FT MOD_RES 522 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT MOD_RES 1005 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:15665377, FT ECO:0007744|PubMed:19779198" FT MOD_RES 1016 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT MOD_RES 1032 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:17330950" FT MOD_RES 1095 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q12271" FT MUTAGEN 631 FT /note="E->A: Impairs completely enzyme activity." FT /evidence="ECO:0000269|PubMed:10962003" FT MUTAGEN 730 FT /note="H->A: Impairs completely enzyme activity." FT /evidence="ECO:0000269|PubMed:10962003" FT MUTAGEN 771 FT /note="D->A: Impairs completely enzyme activity." FT /evidence="ECO:0000269|PubMed:10962003" SQ SEQUENCE 1183 AA; 133331 MW; 97B279870DFE6F65 CRC64; MKILLSKQQT RKIAIVSETH GLVFRPINSK NSRRSTCAVE LVPKAELNGN GFRRLSNHEI YGFIGLIEIE GLMFIATITG KSKVAQPIPN KTVNKIYAVD FFCLNNSKWD FMDIDSSGYP IVTNDGDFAI SSPPSISTHS SRSSLRSSSS RSLNAQEQAP KHPCHELRKL LSNGSFYYST DFDLTCTLQK RGFTEHSLSF DDFDREFMWN SFLMDEIITY RDRLDVTAKE LLDQRGFLTT VIRGFAETIF SYINRLKVGL TIISRQSWKR AGTRFNARGI DDDGHVANFV ETEMIMYSSQ YCYAFTQIRG SLPIFWEQDT SLISPKIQIT RSVEATQPTF DEHFIRLFKK YGPVHIINLL STKSSEIQLS RRYKEQLKNS EKMKIGRDVF LTSFDFHRET SQDGFAAASR IIPKIRNTIL DAGYFSYDVK EGRLISEQDG VFRTNCLDCL DRTNLIQQTI SLAVFKLFLE DFRLVKPSSF IDDNEFVQKV NALWADNGDQ ISQIYTGTNA LKSSYSRKGK MSFSGALSDA TKSVSRMYIN NFVDKGKQQN IDTLLGKLPH QQVVELYDPI CEYVNERLLE SEEKFTTHSN INLFVGTFNV NGNSRRADLS KWLFPIGDKF KPDVVVLGLQ EVIELTAGSI LNADYTKSSF WETMVTDCLN QYEEKYLLLR VEQMSSLLIL FFARSDRAYN IKEVGGSTKK TGFGGITGNK GAVAIRFDYG ATSFCFVNTH LSAGASNIDE RRNDYNNIYR NITFPRSKTI PHHDSLFWLG DLNYRITLTN DEVRRELRAQ KDGYIDRLLQ YDQLTQEINE GVVFQGFKEP TLQFRPTYKY DYGTDNYDTS EKARTPSWTD RIIYKGENLH PLAYSDAPLK ISDHKPVYAA YRANVKFVDE KEKLNLVEKL YAEYKNTHPE ALTTGPDELS HARMEKQKES IPLDATVQSA GIKLIDLDDT SSCVSPLLSG PSPQPSVVGP GGLSNVSPDK SKLNVLPPPP PTSRHNKEPS SKLLSPTKEI SIVSVSPRKG ESNLPALERH STPKPLPPVP ALSLSKPVSL QKSSSELQHA KETIDNGKIV PRPCPPIRRK SSTAPDEIST STKNSGVSTT EDPEPAKAST KPEKPPVVKK PHYLSVAANK LNTSQEHSIK VSPSNSKSEE ELPCKKKSKP KVPAKNPELE KLSVHPLKPC DPN //