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PH domain leucine-rich repeat protein phosphatase 1 (EC 3.1.3.16) (Pleckstrin homology domain-containing family E member 1) (PH domain-containing family E member 1) (Suprachiasmatic nucleus circadian oscillatory protein)

 PHLP1_RAT               Reviewed;        1696 AA.
Q9WTR8;
07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
25-OCT-2017, entry version 121.
RecName: Full=PH domain leucine-rich repeat protein phosphatase 1;
EC=3.1.3.16;
AltName: Full=Pleckstrin homology domain-containing family E member 1;
Short=PH domain-containing family E member 1;
AltName: Full=Suprachiasmatic nucleus circadian oscillatory protein;
Name=Phlpp1; Synonyms=Phlpp, Plekhe1, Scop;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
STAGE.
TISSUE=Brain;
PubMed=10570941; DOI=10.1016/S0014-5793(99)01190-4;
Shimizu K., Okada M., Takano A., Nagai K.;
"SCOP, a novel gene product expressed in a circadian manner in rat
suprachiasmatic nucleus.";
FEBS Lett. 458:363-369(1999).
[2]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH KRAS.
PubMed=12594205; DOI=10.1074/jbc.M213214200;
Shimizu K., Okada M., Nagai K., Fukada Y.;
"Suprachiasmatic nucleus circadian oscillatory protein, a novel
binding partner of K-Ras in the membrane rafts, negatively regulates
MAPK pathway.";
J. Biol. Chem. 278:14920-14925(2003).
[3]
FUNCTION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY (ISOFORMS 1 AND 2),
AND INDUCTION BY INSULIN.
PubMed=20089132; DOI=10.1111/j.1471-4159.2010.06609.x;
Kanan Y., Matsumoto H., Song H., Sokolov M., Anderson R.E.,
Rajala R.V.;
"Serine/threonine kinase akt activation regulates the activity of
retinal serine/threonine phosphatases, PHLPP and PHLPPL.";
J. Neurochem. 113:477-488(2010).
[4]
ALTERNATIVE SPLICING, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
FUNCTION.
PubMed=20819118; DOI=10.1111/j.1471-4159.2010.06984.x;
Jackson T.C., Verrier J.D., Semple-Rowland S., Kumar A., Foster T.C.;
"PHLPP1 splice variants differentially regulate AKT and PKCalpha
signaling in hippocampal neurons: characterization of PHLPP proteins
in the adult hippocampus.";
J. Neurochem. 115:941-955(2010).
-!- FUNCTION: Protein phosphatase involved in regulation of Akt and
PKC signaling. Mediates dephosphorylation in the C-terminal domain
hydrophobic motif of members of the AGC Ser/Thr protein kinase
family; specifically acts on 'Ser-473' of AKT2 and AKT3, 'Ser-660'
of PRKCB and 'Ser-657' of PRKCA (PubMed:20819118). Isoform 2 seems
to have a major role in regulating Akt signaling in hippocampal
neurons while isoform 1 may promote Akt and PKC activation and
inhibit ERK signaling (PubMed:20819118). Akt regulates the balance
between cell survival and apoptosis through a cascade that
primarily alters the function of transcription factors that
regulate pro- and antiapoptotic genes. Dephosphorylation of 'Ser-
473' of Akt triggers apoptosis and suppression of tumor growth.
Dephosphorylation of PRKCA and PRKCB leads to their
destabilization and degradation. Dephosphorylates STK4 on 'Thr-
387' leading to STK4 activation and apoptosis (By similarity).
Dephosphorylates RPS6KB1 and is involved in regulation of cap-
dependent translation (By similarity). Inhibits cancer cell
proliferation and may act as a tumor suppressor (By similarity).
Dephosphorylates RAF1 inhibiting its kinase activity (By
similarity). May act as a negative regulator of K-Ras signaling in
membrane rafts (PubMed:12594205). Involved in the hippocampus-
dependent long-term memory formation (By similarity). Involved in
circadian control by regulating the consolidation of circadian
periodicity after resetting (By similarity). Involved in
development and function of regulatory T-cells (By similarity).
{ECO:0000250|UniProtKB:O60346, ECO:0000250|UniProtKB:Q8CHE4,
ECO:0000269|PubMed:12594205, ECO:0000269|PubMed:20819118}.
-!- CATALYTIC ACTIVITY: [a protein]-serine/threonine phosphate + H(2)O
= [a protein]-serine/threonine + phosphate.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
Note=Binds 2 manganese ions per subunit. {ECO:0000250};
-!- ENZYME REGULATION: Insensitive to okadaic acid. Deubiquitination
by WDR48-USP12 complex positively regulates PHLPP1 stability.
{ECO:0000250|UniProtKB:O60346}.
-!- SUBUNIT: Interacts with the nucleotide free form of K-Ras (KRAS)
via its LRR repeats (PubMed:12594205). Interacts with AKT2, AKT3
and PRKCB isoform beta-II. Interacts with WDR48 and USP12 (By
similarity). {ECO:0000250|UniProtKB:O60346,
ECO:0000269|PubMed:12594205}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12594205}.
Membrane {ECO:0000269|PubMed:12594205}; Peripheral membrane
protein {ECO:0000269|PubMed:12594205}.
-!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasm
{ECO:0000269|PubMed:20819118}. Cell membrane
{ECO:0000269|PubMed:20819118}.
-!- SUBCELLULAR LOCATION: Isoform 2: Nucleus, nucleoplasm
{ECO:0000269|PubMed:20819118}. Nucleus membrane
{ECO:0000269|PubMed:20819118}. Cytoplasm
{ECO:0000269|PubMed:20819118}. Cell membrane
{ECO:0000269|PubMed:20819118}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=beta;
IsoId=Q9WTR8-1; Sequence=Displayed;
Name=2; Synonyms=alpha;
IsoId=Q9WTR8-2; Sequence=VSP_057811;
-!- TISSUE SPECIFICITY: Mainly present in brain (at protein level)
(PubMed:10570941). Isoform 2 is more abundant in adult brain
neurons than isoform 1 in (PubMed:20819118). Isoforms 1 and 2 are
expressed in the retina but not found in rod outer segments
(PubMed:20089132). {ECO:0000269|PubMed:10570941,
ECO:0000269|PubMed:20089132, ECO:0000269|PubMed:20819118}.
-!- DEVELOPMENTAL STAGE: In the suprachiasmatic nucleus, it increases
during subjective night with a peak at midnight under constant
dark conditions. Expressed at a constant level in neurons
throughout the brain (at protein level) (PubMed:10570941). Isoform
2 expression increases over development and maturation in the
hippocampus. Isoform 1 expression is low in embryonic stages,
increases during postnatal development and is falling back to low
embryonic levels in adulthood (PubMed:20819118).
{ECO:0000269|PubMed:10570941, ECO:0000269|PubMed:20819118}.
-!- INDUCTION: Inhibited by insulin in a PI3K-dependent manner.
{ECO:0000269|PubMed:20089132}.
-!- DOMAIN: The PH domain is required for interaction with PRKCB and
its dephosphorylation. {ECO:0000250}.
-----------------------------------------------------------------------
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EMBL; AB023624; BAA77767.1; -; mRNA.
RefSeq; NP_067689.1; NM_021657.1. [Q9WTR8-1]
UniGene; Rn.163214; -.
ProteinModelPortal; Q9WTR8; -.
BioGrid; 248740; 1.
IntAct; Q9WTR8; 3.
STRING; 10116.ENSRNOP00000003840; -.
PaxDb; Q9WTR8; -.
PRIDE; Q9WTR8; -.
GeneID; 59265; -.
KEGG; rno:59265; -.
UCSC; RGD:621308; rat. [Q9WTR8-1]
CTD; 23239; -.
RGD; 621308; Phlpp1.
eggNOG; KOG0619; Eukaryota.
eggNOG; COG0631; LUCA.
eggNOG; COG4886; LUCA.
HOGENOM; HOG000115529; -.
InParanoid; Q9WTR8; -.
KO; K16340; -.
PhylomeDB; Q9WTR8; -.
PRO; PR:Q9WTR8; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:RGD.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0007623; P:circadian rhythm; IEP:RGD.
GO; GO:0021766; P:hippocampus development; IEP:RGD.
GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
GO; GO:0051898; P:negative regulation of protein kinase B signaling; IMP:UniProtKB.
GO; GO:0090038; P:negative regulation of protein kinase C signaling; IMP:UniProtKB.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IMP:UniProtKB.
GO; GO:0090037; P:positive regulation of protein kinase C signaling; IMP:UniProtKB.
GO; GO:0006470; P:protein dephosphorylation; IDA:RGD.
GO; GO:0046328; P:regulation of JNK cascade; IBA:GO_Central.
GO; GO:1900744; P:regulation of p38MAPK cascade; IBA:GO_Central.
GO; GO:0001932; P:regulation of protein phosphorylation; IMP:RGD.
CDD; cd00143; PP2Cc; 1.
Gene3D; 2.30.29.30; -; 1.
Gene3D; 3.60.40.10; -; 1.
Gene3D; 3.80.10.10; -; 3.
InterPro; IPR032675; L_dom-like.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
InterPro; IPR011993; PH_dom-like.
InterPro; IPR001849; PH_domain.
InterPro; IPR036457; PPM-type_dom_sf.
InterPro; IPR001932; PPM-type_phosphatase_dom.
Pfam; PF13516; LRR_6; 1.
Pfam; PF13855; LRR_8; 2.
Pfam; PF00169; PH; 1.
Pfam; PF00481; PP2C; 1.
SMART; SM00369; LRR_TYP; 9.
SMART; SM00332; PP2Cc; 1.
SUPFAM; SSF50729; SSF50729; 2.
SUPFAM; SSF52058; SSF52058; 2.
SUPFAM; SSF81606; SSF81606; 1.
PROSITE; PS51450; LRR; 17.
PROSITE; PS50003; PH_DOMAIN; 1.
PROSITE; PS51746; PPM_2; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Apoptosis; Cell membrane;
Complete proteome; Cytoplasm; Hydrolase; Leucine-rich repeat;
Manganese; Membrane; Metal-binding; Nucleus; Phosphoprotein;
Protein phosphatase; Reference proteome; Repeat; Tumor suppressor.
CHAIN 1 1696 PH domain leucine-rich repeat protein
phosphatase 1.
/FTId=PRO_0000057783.
DOMAIN 499 599 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
REPEAT 601 622 LRR 1.
REPEAT 624 645 LRR 2.
REPEAT 655 676 LRR 3.
REPEAT 678 699 LRR 4.
REPEAT 701 722 LRR 5.
REPEAT 724 746 LRR 6.
REPEAT 836 857 LRR 7.
REPEAT 858 879 LRR 8.
REPEAT 881 902 LRR 9.
REPEAT 904 925 LRR 10.
REPEAT 926 947 LRR 11.
REPEAT 950 971 LRR 12.
REPEAT 976 996 LRR 13.
REPEAT 1000 1021 LRR 14.
REPEAT 1024 1045 LRR 15.
REPEAT 1047 1068 LRR 16.
REPEAT 1069 1090 LRR 17.
REPEAT 1092 1113 LRR 18.
DOMAIN 1138 1385 PPM-type phosphatase.
{ECO:0000255|PROSITE-ProRule:PRU01082}.
MOTIF 1694 1696 PDZ-binding.
COMPBIAS 4 9 Poly-Ala.
COMPBIAS 21 28 Poly-Ala.
COMPBIAS 116 126 Poly-Ser.
COMPBIAS 339 343 Poly-Ser.
COMPBIAS 405 410 Poly-Ala.
COMPBIAS 1431 1434 Poly-Ser.
COMPBIAS 1645 1661 Poly-Gln.
COMPBIAS 1662 1669 Poly-Pro.
METAL 1173 1173 Manganese 1.
{ECO:0000250|UniProtKB:P35813}.
METAL 1173 1173 Manganese 2.
{ECO:0000250|UniProtKB:P35813}.
METAL 1174 1174 Manganese 1; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P35813}.
METAL 1337 1337 Manganese 2.
{ECO:0000250|UniProtKB:P35813}.
METAL 1376 1376 Manganese 2.
{ECO:0000250|UniProtKB:P35813}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:O60346}.
MOD_RES 378 378 Phosphoserine.
{ECO:0000250|UniProtKB:O60346}.
VAR_SEQ 1 475 Missing (in isoform 2).
/FTId=VSP_057811.
SEQUENCE 1696 AA; 183364 MW; B4C3CC777B8BB6A9 CRC64;
MEPAAAAPAQ RLADPTGEDR APAAAAAAEG GRSPDSVLSA AAPSGGNGGA AREEAPCEAP
PGPLPGRAGG TGRRRRRGVP QPAAGGAAPV TAAGGGANSL LLRRGRLKRN LSAAASSSSS
PSSASSAAGG LPASCSASAS LCTRSLDRKT LLQKHRQLLQ LQPSDRDWVR HQLQRGCVHV
FDRHMASSYL RPVLCTLDTT AAEVAARLLQ LGHKGGGVVK VLGHGPPPAA APAASDQTPA
TELGRDVEPP PSSSTVGAVR GPARAPPADL PLPGGAWTRC APRVNPAPSD SSPGELFAGG
PCSPSRAPRP ASDTESFSLS PSAESVSDRL DPYSSGGGSS SSSEELEADP ATVLTGPSGP
PHHPVRSSQP RPPSPKTSAL LQPKAPTGVD GTGLVVGEGP GDDKAVAAAA PGVPLWTPGR
IRETVQKTSS PPSLYVQLHG ETTRRLEADE KPLQIQNDYL FQLGFGELWR VQEEGMDSEI
GCLIRFYAGK PHSTGSSERI QLSGMYNVRK GKMQLPVNRW TRRQVILCGT CLIVSSVKDS
SSGKMHVLPL IGGKVEEVKK HQHCLAFSSS GPQSQTYYIC FDTFTEYLRW LRQVSKVASQ
RISSVDLSCC SLEHLPANLF YSQDLTHLNL KQNFLRQNPS LPAARGLGEL QRFTKLKSLN
LSNNHLGAFP SAVCSIPTLA ELNVSCNALQ EVPAAVGAMQ NLQTFLLDGN FLQSLPAELE
NMHQLSYLGL SFNEFTDIPE VLEKLTAVDK LCMAGNCMET LRLQALRRMP HIKHVDLRLN
ILRKLITDEV DFLQHVTQLD LRDNKLGDLD AMIFNNIEVL HCERNQLVTL NICGYFLKAL
YASSNELVQL DVYPVPNYLS YMDVSRNCLE SVPEWVCESR KLEVLDIGHN QICELPARLF
CNSSLRKLLA GHNRLARLPE RLERTSVEVL DVQHNQIIEL PPNLLMKADS LRFLNASANK
LETLPPATLS EETSSILQEL YLTNNSLTDK CVPLLTGHPR LKILHMAYNR LQSFPASKMA
KLEELEEIDI SGNKLKAIPT TIMNCRRMHT VIAHSNCIEV FPEVMQLPEV KCVDLSCNEL
SEITLPENLP PKLQELDLTG NPRLALDHKS LELLNNIRCF KIDQPSAGDA SGAPAVWSHG
YTEASGVKNK LCVAALSVNN FRDNREALYG VFDGDRNVEV PYLLQCTMSD ILAEELQKTK
NEEEYMVNTF IVMQRKLGTA GQKLGGAAVL CHIRHDPVDL GGSFTLTSAN VGKCQTVLCR
NGKPLSLSRS YTMSCEEERK RIKQHKAIIT EDGKVNGVTE STRILGYTFL HPSVVPRPHV
QSVLLTPQDE FFILGSKGLW DSLSIEEAVE AVRNVPDALA AAKKLCTLAQ SYGCHDSISA
VVVQLSVTED SFCCCELSVG GSMPPPSPGI FPPSVSMVIK DRPSDGLGVP SSSSGMASEI
SSELSTSEMS SEVGSTASDE PPSGALSESS PAYPSEQRCM LHPVCLSNSF QRQLSSATFS
SAFSDNGLDS DDEEPIEGVF SNGSRVEVEV DIHCSRAKEK ERQQHLLQVP AEASDEGIVI
SANEDESGLS KKTDISAVGT IGRRRANGSV PPQERSHNVI EVATDAPLRK PGGYFAAPAQ
PDPDDQFIIP PELEEEVKEI MKHHQEQQQQ QQQQQQQQQQ QPPPPPQPPQ AQAQAQAQAQ
RPFQMDHLPD CYDTPL


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