ID   PRR5L_RAT               Reviewed;         370 AA.
AC   A1L1K1;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=Proline-rich protein 5-like;
DE   AltName: Full=Protein observed with Rictor-2;
DE            Short=Protor-2;
GN   Name=Prr5l; Synonyms=Protor2;
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: Associates with the mTORC2 complex that regulates cellular
CC       processes including survival and organization of the cytoskeleton.
CC       Regulates the activity of the mTORC2 complex in a substrate-specific
CC       manner preventing for instance the specific phosphorylation of PKCs and
CC       thereby controlling cell migration. Plays a role in the stimulation of
CC       ZFP36-mediated mRNA decay of several ZFP36-associated mRNAs, such as
CC       TNF-alpha and GM-CSF, in response to stress. Required for ZFP36
CC       localization to cytoplasmic stress granule (SG) and P-body (PB) in
CC       response to stress. {ECO:0000250|UniProtKB:Q6MZQ0}.
CC   -!- SUBUNIT: Interacts with the mammalian target of rapamycin complex 2
CC       (mTORC2) which contains MTOR, MLST8, PRR5, RICTOR, MAPKAP1 and DEPTOR.
CC       Interacts with RFFL. Interacts (via C-terminus) with ZFP36 (via C-
CC       terminus); this interaction may accelerate ZFP36-mediated mRNA decay
CC       during stress. Interacts with RICTOR. {ECO:0000250|UniProtKB:Q6MZQ0}.
CC   -!- PTM: Ubiquitinated. Ubiquitination by RFFL promotes proteasomal
CC       degradation of PRR5L thereby modifying the substrate-specific activity
CC       of the mTORC2 complex. Ubiquitination by RFFL is stimulated by
CC       LPA/lysophosphatidic acid (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PROTOR family. {ECO:0000305}.
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DR   EMBL; BC129104; AAI29105.1; -; mRNA.
DR   RefSeq; NP_001073619.1; NM_001080150.1.
DR   AlphaFoldDB; A1L1K1; -.
DR   SMR; A1L1K1; -.
DR   STRING; 10116.ENSRNOP00000006291; -.
DR   PaxDb; A1L1K1; -.
DR   PRIDE; A1L1K1; -.
DR   GeneID; 362171; -.
DR   KEGG; rno:362171; -.
DR   UCSC; RGD:1309969; rat.
DR   CTD; 79899; -.
DR   RGD; 1309969; Prr5l.
DR   eggNOG; ENOG502QSM7; Eukaryota.
DR   InParanoid; A1L1K1; -.
DR   PhylomeDB; A1L1K1; -.
DR   PRO; PR:A1L1K1; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0031932; C:TORC2 complex; ISS:UniProtKB.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR   GO; GO:0034599; P:cellular response to oxidative stress; ISS:UniProtKB.
DR   GO; GO:0001933; P:negative regulation of protein phosphorylation; ISS:UniProtKB.
DR   GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR   GO; GO:0090316; P:positive regulation of intracellular protein transport; ISS:UniProtKB.
DR   GO; GO:0061014; P:positive regulation of mRNA catabolic process; ISS:UniProtKB.
DR   GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISO:RGD.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:RGD.
DR   GO; GO:0010762; P:regulation of fibroblast migration; ISS:UniProtKB.
DR   GO; GO:0038203; P:TORC2 signaling; ISS:UniProtKB.
DR   InterPro; IPR013745; Bit61/PRR5.
DR   PANTHER; PTHR32428; PTHR32428; 1.
DR   Pfam; PF08539; HbrB; 1.
PE   2: Evidence at transcript level;
KW   Phosphoprotein; Reference proteome; Signal transduction inhibitor;
KW   Ubl conjugation.
FT   CHAIN           1..370
FT                   /note="Proline-rich protein 5-like"
FT                   /id="PRO_0000332711"
FT   REGION          327..370
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         28
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:A2AVJ5"
SQ   SEQUENCE   370 AA;  41162 MW;  38F897C72643884A CRC64;
     MTRGLAPLLP IEFHKMGSFR RPRPRFMSSP LLSELPRFQA ARQALQLSSN SAWNSVQTAV
     INVFKGGGLQ SNELYALNES IRRLLKSELG SFITDYFQNQ LLAKGLSFVE EKIKQCEGDN
     RIEVLAEVWD HFFTETLPTL QAIFYPVQGQ ELTIRQISLL GFRDLVLLKV KLGDLLLLSQ
     SKLPSSVIQM LLILQSVHEP TGPSEGYLQL EELVKQVVSP FLGLSGDRSC SRPTHSLARR
     HSRVRPKVTV LNYASLMTTV GRPLNEMVLT PLTEQEGEAY LEKCGSVRRH TVANAHSDIQ
     LLAMATMMHS GLGEESGSED KHLLLPPTFP PPHRQCSSEP SILDSPDEME LEDVASGSQE
     DSELNCASLS