ID   PHLA3_RAT               Reviewed;         125 AA.
AC   Q5PQT7;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Pleckstrin homology-like domain family A member 3;
DE   AltName: Full=TDAG51/Ipl homolog 1;
GN   Name=Phlda3; Synonyms=Tih1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: p53/TP53-regulated repressor of Akt/AKT1 signaling. Represses
CC       AKT1 by preventing AKT1-binding to membrane lipids, thereby inhibiting
CC       AKT1 translocation to the cellular membrane and activation. Contributes
CC       to p53/TP53-dependent apoptosis by repressing AKT1 activity. Its direct
CC       transcription regulation by p53/TP53 may explain how p53/TP53 can
CC       negatively regulate AKT1. May act as a tumor suppressor (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}.
CC   -!- DOMAIN: The PH domain binds phosphoinositides with a broad specificity.
CC       It competes with the PH domain of AKT1 and directly interferes with
CC       AKT1 binding to phosphatidylinositol 4,5-bisphosphate (PIP2) and
CC       phosphatidylinositol 3,4,5-trisphosphate (PIP3), preventing AKT1
CC       association to membrane lipids and subsequent activation of AKT1
CC       signaling (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PHLDA3 family. {ECO:0000305}.
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DR   EMBL; BC087038; AAH87038.1; -; mRNA.
DR   RefSeq; NP_001012206.1; NM_001012206.2.
DR   AlphaFoldDB; Q5PQT7; -.
DR   SMR; Q5PQT7; -.
DR   STRING; 10116.ENSRNOP00000011999; -.
DR   iPTMnet; Q5PQT7; -.
DR   PhosphoSitePlus; Q5PQT7; -.
DR   PaxDb; Q5PQT7; -.
DR   PRIDE; Q5PQT7; -.
DR   Ensembl; ENSRNOT00000011999; ENSRNOP00000011999; ENSRNOG00000009068.
DR   GeneID; 363989; -.
DR   KEGG; rno:363989; -.
DR   UCSC; RGD:1310502; rat.
DR   CTD; 23612; -.
DR   RGD; 1310502; Phlda3.
DR   eggNOG; ENOG502S2UN; Eukaryota.
DR   GeneTree; ENSGT00440000039564; -.
DR   HOGENOM; CLU_062639_1_0_1; -.
DR   InParanoid; Q5PQT7; -.
DR   OMA; TLWNAEI; -.
DR   OrthoDB; 1412115at2759; -.
DR   PhylomeDB; Q5PQT7; -.
DR   TreeFam; TF332320; -.
DR   PRO; PR:Q5PQT7; -.
DR   Proteomes; UP000002494; Chromosome 13.
DR   Bgee; ENSRNOG00000009068; Expressed in esophagus and 19 other tissues.
DR   Genevisible; Q5PQT7; RN.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; ISS:UniProtKB.
DR   GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; ISS:UniProtKB.
DR   GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; ISS:UniProtKB.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; ISS:UniProtKB.
DR   GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:UniProtKB.
DR   GO; GO:0010314; F:phosphatidylinositol-5-phosphate binding; ISS:UniProtKB.
DR   GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; ISS:UniProtKB.
DR   GO; GO:0051898; P:negative regulation of protein kinase B signaling; ISS:UniProtKB.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR042832; PHLA1/2/3.
DR   PANTHER; PTHR15478; PTHR15478; 1.
DR   SMART; SM00233; PH; 1.
PE   2: Evidence at transcript level;
KW   Apoptosis; Cytoplasm; Membrane; Reference proteome; Tumor suppressor.
FT   CHAIN           1..125
FT                   /note="Pleckstrin homology-like domain family A member 3"
FT                   /id="PRO_0000053904"
FT   DOMAIN          6..125
FT                   /note="PH"
SQ   SEQUENCE   125 AA;  13735 MW;  1F3E58A6F3C036BC CRC64;
     MTAAATVLKE GVLEKRSGGL LQLWKRKRCV LTERGLQLFE AKGTGGRPKE LSFSRIKAVE
     CVESTGRHIY FTLVTEGGGE IDFRCPLEDP GWNAQITLGL VKFKNQQAIQ TVRARQSLGT
     GTLVS