ID A0A2K6GJE0_PROCO Unreviewed; 1710 AA.
AC A0A2K6GJE0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=PH domain and leucine rich repeat protein phosphatase 1 {ECO:0000313|Ensembl:ENSPCOP00000026366.1};
GN Name=PHLPP1 {ECO:0000313|Ensembl:ENSPCOP00000026366.1};
OS Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS coquereli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Indriidae; Propithecus.
OX NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000026366.1, ECO:0000313|Proteomes:UP000233160};
RN [1] {ECO:0000313|Ensembl:ENSPCOP00000026366.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR STRING; 379532.ENSPCOP00000026366; -.
DR Ensembl; ENSPCOT00000037104.1; ENSPCOP00000026366.1; ENSPCOG00000025545.1.
DR GeneTree; ENSGT00940000158137; -.
DR OMA; GHNQICD; -.
DR Proteomes; UP000233160; Unplaced.
DR GO; GO:0009649; P:entrainment of circadian clock; IEA:Ensembl.
DR GO; GO:0051898; P:negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0046328; P:regulation of JNK cascade; IEA:Ensembl.
DR GO; GO:1900744; P:regulation of p38MAPK cascade; IEA:Ensembl.
DR GO; GO:0002667; P:regulation of T cell anergy; IEA:Ensembl.
DR CDD; cd13322; PH_PHLPP-like; 1.
DR CDD; cd00143; PP2Cc; 1.
DR CDD; cd17240; RA_PHLPP1; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
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; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR036457; PPM-type-like_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR PANTHER; PTHR48051; -; 1.
DR PANTHER; PTHR48051:SF37; PH DOMAIN AND LEUCINE-RICH REPEAT PROTEIN PHOSPHATASE 2; 1.
DR Pfam; PF13516; LRR_6; 2.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00364; LRR_BAC; 10.
DR SMART; SM00369; LRR_TYP; 9.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF52058; L domain-like; 2.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF81606; PP2C-like; 1.
DR PROSITE; PS51450; LRR; 3.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 4: Predicted;
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Reference proteome {ECO:0000313|Proteomes:UP000233160};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 534..634
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1173..1420
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 41..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1456..1507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1674..1710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..284
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..412
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1462..1507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1681..1697
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1710 AA; 184100 MW; 26B96B1094971DBD CRC64;
MEPAAAATAQ RLPETSREDR ASAPAAAAAA AAVAAAAAAL AAAAGGSRSP EPALTLAAPS
GGNGGSGGAR EEAAGEAPPG PLPVRAGGTG RRRRRGAPQP TAGGVAPVSG VGSGANSLLL
RRGRLKRNLS AAAAAASSSS SSSSSSSAAA ASHSAGASGL PASCSASASL CTRSLDRKTL
LLKHRQIMQL QPSDRDWVRH QLQRGCVHVF DRHMASTYLR PVLCTLDTTA GEVAARLLQQ
GHKGGGVVKV LGQGFGPAAA RSGAELPPDA GPRLAPPEPR DLEPPPARSA LGAVGDTPRA
PPADLALPGG GRGGWARCTS RASPAPSDSS PGEPFARGPA SPPGTPRPLA SDTESFSLSP
SAESVSDRLD PYSSGGGSSS SSEELDTDPA PAPAPTGAPG QTRRPAPASP PWPQQKARRG
VDSPGGVARD ETWGEKVAAA AAPSGPQSTP GRSGAAAEKA PPPPPPPTLY VQLHGETTRR
LEADEKPLQI QNDYLFQLGF GELWRVQEEG MDSEIGCLIR FYAGKPHSTG SSERIQLSGM
YNVRKGKMQL PVNRWTRRQV ILCGTCLIVS SVKDSLTGKM HVLPLIGGKV EEVKKHQHCL
AFSSSGPQSQ TYYICFDTFA EYLRWLRQVS KVASQRISSV DLSCCSLEHL PANLFYSQDL
THLNLKQNFL RQNPSLPAAR GLNELQRFTK LKSLNLSNNH LGDFPLAVCS IPTLAELNVS
CNALRAVPAA VGDMHNLQTF LLDGNFLQSL PAELENMQQL SYLGLSFNEF TDIPEVLEKL
TAVDKLCMSG NCMETLRLQA LRKMPHIKHV DLRLNVIRKL IADEVDFLQH VTQLDLRDNK
LGDLDAMIFN NIEVLHCERN QLVTLNICGY FLKALYASSN ELVQLDVYPV PNYLSYMDVS
RNRLENVPEW VCESRKLEVL DIGHNEICEL PARLFCNSSL RKLLAGHNQL ARLPERLERT
SVEVLDVQHN QLLELPPNLL MKADSLRFLN ASANKLETLP PATLCEETNS ILQELYLTNN
SLTDKCVPLL TGHPHLKILH MAYNRLQSFP ASKMAKLEEL EEIDISGNKL KAIPTTIMNC
RRMHTVIAHS NCIEVFPEVM QLPEIKCVDL SCNELSEVTL PENLPPKLQE LDLTGNPRLV
LDHKTLELLN NIRCFKIDQP SAGDTSGAPA VWSHGYTEAS GVKNKLCVAA LSVNNFCDNR
EALYGVFDGD RNVEVPYLLQ CTMSDILAEE LQKTKNEEEY MVNTFIVMQR KLGTAGQKLG
GAAVLCHIKH DPVDPGGSFT LTSANVGKCQ TVLCRNGKPL PLSRSYVMSC EEELKRIKQH
KAIITEDGKV NGVTESTRIL GYTFLHPSVV PRPHVQSVLL TPQDEFFILG SKGLWDSLSV
EEAVEAVRNV PDALAAAKKL CTLAQSYGCH DSISAVVVQL SVTEDSFCCC ELSAGGSVPP
PSPGIFPPSV NMVIKDRPSD GLGVPSSSSG MASEISSELS TSEMSSEVGS TASDEPPSGA
LNESSPACPS EQRCMLHPVC LSNSFQRQLS SATFSSAFSD NGLDSDDEEP IEGVFINGSR
VEVEVDIHCS RAKEKEKQQH LLQVPAEASD EGIVISANED ELGLPRKADF SAVGTIGRRR
ANGSVAPQER SHNVIEVATD APLRKPGGYF AAPAQPDPDD QFIIPPELEE EVKEIMKHHQ
EQQQQPQLQQ PQPQRHYQAD QLPDYYDTPL
//
