ID   PHLA2_SALSA             Reviewed;         138 AA.
AC   B5XG43;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=Pleckstrin homology-like domain family A member 2;
DE   AltName: Full=Imprinted in placenta and liver protein;
GN   Name=phlda2; Synonyms=ipl;
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=20433749; DOI=10.1186/1471-2164-11-279;
RA   Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A., Messmer A.M.,
RA   Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., Davidson W.S.,
RA   Koop B.F.;
RT   "Salmo salar and Esox lucius full-length cDNA sequences reveal changes in
RT   evolutionary pressures on a post-tetraploidization genome.";
RL   BMC Genomics 11:279-279(2010).
CC   -!- FUNCTION: Plays a role in regulating placenta growth. May act via its
CC       PH domain that competes with other PH domain-containing proteins,
CC       thereby preventing their binding to membrane lipids (By similarity).
CC       {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 may compete with the PH domain of some other proteins, thereby
CC       interfering with their binding to phosphatidylinositol 4,5-bisphosphate
CC       (PIP2) and phosphatidylinositol 3,4,5-trisphosphate (PIP3) (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PHLDA2 family. {ECO:0000305}.
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DR   EMBL; BT050012; ACI69813.1; -; mRNA.
DR   RefSeq; NP_001134998.1; NM_001141526.1.
DR   AlphaFoldDB; B5XG43; -.
DR   SMR; B5XG43; -.
DR   STRING; 8030.ENSSSAP00000067955; -.
DR   Ensembl; ENSSSAT00000099957; ENSSSAP00000067955; ENSSSAG00000060970.
DR   Ensembl; ENSSSAT00000195995; ENSSSAP00000179984; ENSSSAG00000060970.
DR   Ensembl; ENSSSAT00000246943; ENSSSAP00000142060; ENSSSAG00000060970.
DR   GeneID; 100196497; -.
DR   KEGG; sasa:100196497; -.
DR   CTD; 7262; -.
DR   OrthoDB; 1412115at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa10.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:1901981; F:phosphatidylinositol phosphate binding; IEA:InterPro.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IEA:InterPro.
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   Pfam; PF00169; PH; 1.
DR   SMART; SM00233; PH; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Membrane; Reference proteome.
FT   CHAIN           1..138
FT                   /note="Pleckstrin homology-like domain family A member 2"
FT                   /id="PRO_0000369388"
FT   DOMAIN          11..105
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   REGION          117..138
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   138 AA;  15962 MW;  746A06B7B3E38AB7 CRC64;
     MKMSAEQISE VLKEGELEKR SDNLLQFWKR KTCVLTTDSL NIYADTQKRT KSKELKLQSI
     KKVDCVERTG KFVYFTIVTT DNKEIDFRCS GDDNCWNAVI TMALIDFQNR KAIQDFKTRQ
     DDESGSPGQH ESRMARAP