ID   PRR5L_BOVIN             Reviewed;         368 AA.
AC   Q5E9R0; B0JYP4;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 60.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BT020860; AAX08877.1; -; mRNA.
DR   EMBL; BC151482; AAI51483.1; -; mRNA.
DR   RefSeq; NP_001015519.1; NM_001015519.1.
DR   AlphaFoldDB; Q5E9R0; -.
DR   STRING; 9913.ENSBTAP00000028004; -.
DR   PaxDb; Q5E9R0; -.
DR   GeneID; 505048; -.
DR   KEGG; bta:505048; -.
DR   CTD; 79899; -.
DR   eggNOG; ENOG502QSM7; Eukaryota.
DR   InParanoid; Q5E9R0; -.
DR   OrthoDB; 1260193at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0031932; C:TORC2 complex; ISS:UniProtKB.
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: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..368
FT                   /note="Proline-rich protein 5-like"
FT                   /id="PRO_0000332708"
FT   REGION          312..368
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        353..368
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         28
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:A2AVJ5"
FT   CONFLICT        6
FT                   /note="T -> A (in Ref. 2; AAI51483)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        309
FT                   /note="H -> R (in Ref. 2; AAI51483)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   368 AA;  40826 MW;  8C75D4DF4E0BDD79 CRC64;
     MTRGFTPSLP VEFPKMGSFR RPRPRFMSSP ALSDLPRFQA ARQALQLSSN SAWNSVQTAV
     INVFKGGGLQ SNELYALNEN IRRLLKSELG SFITDYFQNQ LLAKGLLFVE EKIKLCEGEN
     RIEVLAEVWD HFFTETLPTL QAIFYPVQGQ ELTIRQISLL GFRDLVLLKV KLEDLLLLAQ
     PQLPSSIVQM LLILQSVHEP TGPSEGYLQL EELVKQVVSP FLGISEDRGL SGPTYTLARR
     HSRVRPKVTL LNYASPITPV SRPLNEMALT PLTEQEGEAY LEKCGSVRRH TVANAHSDIQ
     LLAMATMMHS GLGEESGGED KCLLLQPSFP PPHRQCSSEP NITDGPDEPE QGATGSQEDS
     ELNCASLS