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PHLPP_CAEEL
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   03-AUG-2022, entry version 148.
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};
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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; -.
DR   PaxDb; Q09564; -.
DR   EnsemblMetazoa; F43C1.1.1; F43C1.1.1; WBGene00009647.
DR   UCSC; F43C1.1; c. elegans.
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   PhylomeDB; Q09564; -.
DR   Reactome; R-CEL-6803207; TP53 Regulates Transcription of Caspase Activators and Caspases.
DR   PRO; PR:Q09564; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00009647; Expressed in embryo and 3 other tissues.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.60.40.10; -; 1.
DR   Gene3D; 3.80.10.10; -; 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_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase_dom.
DR   Pfam; PF13855; LRR_8; 2.
DR   Pfam; PF00481; PP2C; 1.
DR   SMART; SM00369; LRR_TYP; 11.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; SSF81606; 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
 
 
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