PRR5_RAT
ID PRR5_RAT Reviewed; 387 AA.
AC Q5FVG6;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Proline-rich protein 5;
DE AltName: Full=Protein observed with Rictor-1;
DE Short=Protor-1;
GN Name=Prr5 {ECO:0000250|UniProtKB:P85299}; Synonyms=Protor1;
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] {ECO:0000312|EMBL:AAH90007.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver {ECO:0000312|EMBL:AAH90007.1};
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: Subunit of mTORC2, which regulates cell growth and survival
CC in response to hormonal signals. mTORC2 is activated by growth factors,
CC but, in contrast to mTORC1, seems to be nutrient-insensitive. mTORC2
CC seems to function upstream of Rho GTPases to regulate the actin
CC cytoskeleton, probably by activating one or more Rho-type guanine
CC nucleotide exchange factors. mTORC2 promotes the serum-induced
CC formation of stress-fibers or F-actin. mTORC2 plays a critical role in
CC AKT1 'Ser-473' phosphorylation, which may facilitate the
CC phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDK1
CC which is a prerequisite for full activation. mTORC2 regulates the
CC phosphorylation of SGK1 at 'Ser-421'. mTORC2 also modulates the
CC phosphorylation of PRKCA on 'Ser-657'. PRR5 plays an important role in
CC regulation of PDGFRB expression and in modulation of platelet-derived
CC growth factor signaling. May act as a tumor suppressor in breast cancer
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Part of the mammalian target of rapamycin complex 2 (mTORC2)
CC which contains MTOR, MLST8, PRR5, RICTOR, MAPKAP1 and DEPTOR (By
CC similarity). Contrary to mTORC1, mTORC2 does not bind to and is not
CC sensitive to FKBP12-rapamycin. Binds directly to MTOR and RICTOR within
CC the TORC2 complex (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PROTOR family. {ECO:0000305}.
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DR EMBL; BC090007; AAH90007.1; -; mRNA.
DR RefSeq; NP_001012121.1; NM_001012121.1.
DR AlphaFoldDB; Q5FVG6; -.
DR SMR; Q5FVG6; -.
DR STRING; 10116.ENSRNOP00000016679; -.
DR iPTMnet; Q5FVG6; -.
DR PhosphoSitePlus; Q5FVG6; -.
DR PaxDb; Q5FVG6; -.
DR PRIDE; Q5FVG6; -.
DR Ensembl; ENSRNOT00000117245; ENSRNOP00000095214; ENSRNOG00000069507.
DR GeneID; 315189; -.
DR KEGG; rno:315189; -.
DR CTD; 55615; -.
DR RGD; 1307954; Prr5.
DR eggNOG; KOG4406; Eukaryota.
DR GeneTree; ENSGT00530000063981; -.
DR HOGENOM; CLU_046146_0_0_1; -.
DR InParanoid; Q5FVG6; -.
DR OrthoDB; 1260193at2759; -.
DR PhylomeDB; Q5FVG6; -.
DR TreeFam; TF314826; -.
DR Reactome; R-RNO-1257604; PIP3 activates AKT signaling.
DR Reactome; R-RNO-389357; CD28 dependent PI3K/Akt signaling.
DR Reactome; R-RNO-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-RNO-6804757; Regulation of TP53 Degradation.
DR PRO; PR:Q5FVG6; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Genevisible; Q5FVG6; RN.
DR GO; GO:0031932; C:TORC2 complex; ISO:RGD.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; IEA:Ensembl.
DR GO; GO:0016310; P:phosphorylation; ISO:RGD.
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:0006468; P:protein phosphorylation; IEA:Ensembl.
DR GO; GO:0038203; P:TORC2 signaling; IBA:GO_Central.
DR InterPro; IPR013745; Bit61/PRR5.
DR PANTHER; PTHR32428; PTHR32428; 1.
DR Pfam; PF08539; HbrB; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Phosphoprotein; Reference proteome; Tumor suppressor.
FT CHAIN 1..387
FT /note="Proline-rich protein 5"
FT /id="PRO_0000308164"
FT REGION 10..96
FT /note="Interaction with RICTOR"
FT /evidence="ECO:0000250|UniProtKB:P85299"
FT REGION 11..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..219
FT /note="Interaction with RICTOR"
FT /evidence="ECO:0000250|UniProtKB:P85299"
FT REGION 262..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q812A5"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q812A5"
SQ SEQUENCE 387 AA; 42540 MW; C99EAEF90A8B32C0 CRC64;
MRTLRRLKFM SSPSLSDLGK REPGAAGADE RGTQQRRACA NATWNSIHNG VIAVFQRKGL
PDQELFILNE GVRQLLKTEL GSFFTEYLQN QLLTKGMVIL RDKIRFYEGQ KLLDSLAETW
DFFFSDVLPT LQAIFYPVQG KEPSVRQLAL LHFRNTITLS VKLEDALARS HACVPPAIAQ
MLLVLQGVHE SRGVTEDYLR LETLIQKVVS PYLGTYGLYS NEGPCTHSCI LEKRFLRRSR
SGDILAKNPV VRSKSYNTPL LNPVAEHEAE GTASGGTSIR RHSVSEMTSC PEPQGFVDTP
DQGPSGTFRS SPSPHSGPCP SRLYPPAHSP EQGPDHGSPP TSSPETLVDQ ILESVDSDSE
GIFIDFGRGS RSSVSDFEAA GGRPSVV
