ID PHLPP_CAEEL Reviewed; 1126 AA. AC Q09564; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 25-APR-2018, sequence version 3. DT 27-MAR-2024, entry version 156. DE RecName: Full=Protein phosphatase PHLPP-like protein; DE EC=3.1.3.16 {ECO:0000250|UniProtKB:Q6ZVD8}; DE AltName: Full=PH domain and leucine-rich repeat-containing protein phosphatase phlp-2 {ECO:0000312|WormBase:F43C1.1}; GN Name=phlp-2 {ECO:0000312|WormBase:F43C1.1}; GN ORFNames=F43C1.1 {ECO:0000312|WormBase:F43C1.1}; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; OC Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RT "Genome sequence of the nematode C. elegans: a platform for investigating RT biology."; RL Science 282:2012-2018(1998). CC -!- FUNCTION: Probable protein phosphatase. {ECO:0000250|UniProtKB:Q6ZVD8}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:83421; EC=3.1.3.16; CC Evidence={ECO:0000250|UniProtKB:Q6ZVD8}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA- CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:61977; EC=3.1.3.16; CC Evidence={ECO:0000250|UniProtKB:Q6ZVD8}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; 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; BX284603; CAA87056.2; -; Genomic_DNA. DR PIR; T22117; T22117. DR AlphaFoldDB; Q09564; -. DR SMR; Q09564; -. DR BioGRID; 50450; 4. DR STRING; 6239.F43C1.1.1; -. DR PaxDb; 6239-F43C1-1; -. DR EnsemblMetazoa; F43C1.1.1; F43C1.1.1; WBGene00009647. DR UCSC; F43C1.1; c. elegans. DR AGR; WB:WBGene00009647; -. DR WormBase; F43C1.1; CE51952; WBGene00009647; phlp-2. DR eggNOG; KOG0618; Eukaryota. DR GeneTree; ENSGT00960000189222; -. DR HOGENOM; CLU_010874_0_0_1; -. DR InParanoid; Q09564; -. DR OrthoDB; 3677323at2759; -. DR PhylomeDB; Q09564; -. DR Reactome; R-CEL-199418; Negative regulation of the PI3K/AKT network. DR PRO; PR:Q09564; -. DR Proteomes; UP000001940; Chromosome III. DR Bgee; WBGene00009647; Expressed in embryo and 3 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0007165; P:signal transduction; IBA:GO_Central. DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1. DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 3. DR InterPro; IPR001611; Leu-rich_rpt. DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp. DR InterPro; IPR032675; LRR_dom_sf. DR InterPro; IPR036457; PPM-type-like_dom_sf. DR InterPro; IPR001932; PPM-type_phosphatase-like_dom. DR PANTHER; PTHR45752; LEUCINE-RICH REPEAT-CONTAINING; 1. DR PANTHER; PTHR45752:SF191; PROTEIN PHOSPHATASE PHLPP-LIKE PROTEIN; 1. DR Pfam; PF00560; LRR_1; 1. DR Pfam; PF13855; LRR_8; 2. DR Pfam; PF00481; PP2C; 1. DR SMART; SM00364; LRR_BAC; 11. DR SMART; SM00369; LRR_TYP; 11. DR SMART; SM00332; PP2Cc; 1. DR SUPFAM; SSF52058; L domain-like; 1. DR SUPFAM; SSF81606; PP2C-like; 1. DR SUPFAM; SSF52047; RNI-like; 1. DR PROSITE; PS51450; LRR; 18. DR PROSITE; PS51746; PPM_2; 1. PE 3: Inferred from homology; KW Hydrolase; Leucine-rich repeat; Manganese; Metal-binding; KW Protein phosphatase; Reference proteome; Repeat. FT CHAIN 1..1126 FT /note="Protein phosphatase PHLPP-like protein" FT /evidence="ECO:0000305" FT /id="PRO_0000057786" FT REPEAT 56..79 FT /note="LRR 1" FT /evidence="ECO:0000255" FT REPEAT 192..213 FT /note="LRR 2" FT /evidence="ECO:0000255" FT REPEAT 227..250 FT /note="LRR 3" FT /evidence="ECO:0000255" FT REPEAT 251..276 FT /note="LRR 4" FT /evidence="ECO:0000255" FT REPEAT 286..309 FT /note="LRR 5" FT /evidence="ECO:0000255" FT REPEAT 310..332 FT /note="LRR 6" FT /evidence="ECO:0000255" FT REPEAT 333..355 FT /note="LRR 7" FT /evidence="ECO:0000255" FT REPEAT 356..378 FT /note="LRR 8" FT /evidence="ECO:0000255" FT REPEAT 380..403 FT /note="LRR 9" FT /evidence="ECO:0000255" FT REPEAT 419..445 FT /note="LRR 10" FT /evidence="ECO:0000255" FT REPEAT 451..476 FT /note="LRR 11" FT /evidence="ECO:0000255" FT REPEAT 483..506 FT /note="LRR 12" FT /evidence="ECO:0000255" FT REPEAT 507..529 FT /note="LRR 13" FT /evidence="ECO:0000255" FT REPEAT 531..551 FT /note="LRR 14" FT /evidence="ECO:0000255" FT REPEAT 552..574 FT /note="LRR 15" FT /evidence="ECO:0000255" FT REPEAT 576..601 FT /note="LRR 16" FT /evidence="ECO:0000255" FT REPEAT 623..646 FT /note="LRR 17" FT /evidence="ECO:0000255" FT REPEAT 648..672 FT /note="LRR 18" FT /evidence="ECO:0000255" FT REPEAT 674..692 FT /note="LRR 19" FT /evidence="ECO:0000255" FT REPEAT 693..714 FT /note="LRR 20" FT /evidence="ECO:0000255" FT REPEAT 716..743 FT /note="LRR 21" FT /evidence="ECO:0000255" FT DOMAIN 761..987 FT /note="PPM-type phosphatase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082" FT REGION 1038..1077 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1038..1062 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1063..1077 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 1126 AA; 128125 MW; 76A5EC60808F9672 CRC64; MNNEQLQSTS SSPSTLLKPI EKKSRFLRLY SSDGQRSTRI ECDEHTTCAQ ICQQFSCDVI TLQIGNYHFR QLKSDTSPLA ILQDFCRILT MSDENLETES TSKALEDILS YTDSPAFRHI FSFFLGRPRI RAKSTLNLDI LSEEVVIRKG KLIHTWQNAR AVFYNSNIRL QTKNNQDEAL QIRNMKVDVH ESKRGRALRL KDDDVCYLII FQRPNILEAW LTRAQQVEKS NHVDASDEQL TLIPEQILNN EARVQILNLR RNSLISRPPT EKSMAPLGYI DDLYRVHSLQ VIDLSANQIL SFPIQLTLLS HLRQLNLSSN YISSVPSECS NMRRLQYLNL SNNQLDTLPD SISELQNLQS LDISFNQFSQ IPPCLFHLTL EMWRLAGNNI EKIDRVGEMQ IQKIDLRRNV LDTSFRLDIE NITHLDLRDN SMISTVHLTN LRFLKVIHCE RLQLSSLHLS GESLTHVYAD HNLLDSLVVM PLPQNLQTLS LSFNHFRNLP DWISDCPNLT FLRANNNSLV ALPERIFYSQ SLRSIFAFIN EIEHIPDFGE ENCLETLILY KNKLSSLPKH FFSILPRLRQ LNISSNFIEL LPYFDGSSFC RLQILRCANN YLTENSVPVI VNMKHLKIID LSHNRLNSFD DSALSSLELL EDLNLSSNRL TRLADCLALL PCLQVLRAHS NQLVHVPEFR ASNQLHTIDV SSNNISLGTL QFKAPPNLRH FDVTCNSGDF DTENFPENAK MHSKMNTINI SEGSQNLFGF QIGVSGSRGM KNKQCIRQVR VENTFGFIDG GSNSYMSSSI CRFMTSYLKE NVSMDIRSIL LRCHCELGEE GERLGASVMI IRVHEKRLEI ASTGTMSAAI ARNQKLKMII NGRYEIDDDE YSRIREAHGF VDEENRINGV IGSSRQIGHF STFPVVLPTH SYRNIQLNEQ IEGLIVGNNM IWNMLSIDDL NSTFHNNRSP IVVAKKIQDQ LQSYDYGGNS NILVLRRIKP QMTFNGFSTS STKNQVTPDI AIPKIDEQLV LAVPALILPE YHPSPPVPPP IPAIRHRTPS PPPPPLPSST PPPVSSEHEE INVRQSSTLS GGYTLSIDRF YSSSSTVSSR KQFNETRDLL SKSLKLSPPN TVTFNI //