PRR5L_MOUSE
ID PRR5L_MOUSE Reviewed; 370 AA.
AC A2AVJ5; B7ZWM2; Q80Y78; Q8BIT0;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 91.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Placenta;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Olfactory epithelium;
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).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION IN MTORC2 SIGNALING.
RX PubMed=22609986; DOI=10.1038/ncb2507;
RA Gan X., Wang J., Wang C., Sommer E., Kozasa T., Srinivasula S., Alessi D.,
RA Offermanns S., Simon M.I., Wu D.;
RT "PRR5L degradation promotes mTORC2-mediated PKC-delta phosphorylation and
RT cell migration downstream of Galpha12.";
RL Nat. Cell Biol. 14:686-696(2012).
CC -!- FUNCTION: Associates with the mTORC2 complex that regulates cellular
CC processes including survival and organization of the cytoskeleton (By
CC similarity). Regulates the activity of the mTORC2 complex in a
CC substrate-specific manner preventing for instance the specific
CC phosphorylation of PKCs and thereby controlling cell migration
CC (PubMed:22609986). Plays a role in the stimulation of ZFP36-mediated
CC mRNA decay of several ZFP36-associated mRNAs, such as TNF-alpha and GM-
CC CSF, in response to stress. Required for ZFP36 localization to
CC cytoplasmic stress granule (SG) and P-body (PB) in response to stress.
CC {ECO:0000250|UniProtKB:Q6MZQ0, ECO:0000269|PubMed:22609986}.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAH48394.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC25324.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE26803.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK011178; BAC25324.1; ALT_INIT; mRNA.
DR EMBL; AK145981; BAE26803.1; ALT_INIT; mRNA.
DR EMBL; AL929534; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL929571; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC048394; AAH48394.1; ALT_INIT; mRNA.
DR EMBL; BC172132; AAI72132.1; -; mRNA.
DR CCDS; CCDS38186.1; -.
DR RefSeq; NP_001077279.1; NM_001083810.2.
DR RefSeq; NP_001104319.1; NM_001110849.1.
DR RefSeq; NP_780390.3; NM_175181.5.
DR RefSeq; XP_006500301.1; XM_006500238.3.
DR RefSeq; XP_006500303.1; XM_006500240.3.
DR RefSeq; XP_006500304.1; XM_006500241.3.
DR RefSeq; XP_017174768.1; XM_017319279.1.
DR AlphaFoldDB; A2AVJ5; -.
DR STRING; 10090.ENSMUSP00000130152; -.
DR iPTMnet; A2AVJ5; -.
DR PhosphoSitePlus; A2AVJ5; -.
DR EPD; A2AVJ5; -.
DR MaxQB; A2AVJ5; -.
DR PaxDb; A2AVJ5; -.
DR PRIDE; A2AVJ5; -.
DR ProteomicsDB; 291567; -.
DR Antibodypedia; 13120; 82 antibodies from 25 providers.
DR DNASU; 72446; -.
DR Ensembl; ENSMUST00000043845; ENSMUSP00000042167; ENSMUSG00000032841.
DR Ensembl; ENSMUST00000163762; ENSMUSP00000127530; ENSMUSG00000032841.
DR Ensembl; ENSMUST00000171088; ENSMUSP00000130152; ENSMUSG00000032841.
DR GeneID; 72446; -.
DR KEGG; mmu:72446; -.
DR UCSC; uc008lho.2; mouse.
DR CTD; 79899; -.
DR MGI; MGI:1919696; Prr5l.
DR VEuPathDB; HostDB:ENSMUSG00000032841; -.
DR eggNOG; ENOG502QSM7; Eukaryota.
DR GeneTree; ENSGT00530000063981; -.
DR HOGENOM; CLU_046146_1_0_1; -.
DR InParanoid; A2AVJ5; -.
DR OMA; MASMMHS; -.
DR OrthoDB; 1260193at2759; -.
DR PhylomeDB; A2AVJ5; -.
DR TreeFam; TF314826; -.
DR BioGRID-ORCS; 72446; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Prr5l; mouse.
DR PRO; PR:A2AVJ5; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; A2AVJ5; protein.
DR Bgee; ENSMUSG00000032841; Expressed in humerus cartilage element and 220 other tissues.
DR ExpressionAtlas; A2AVJ5; baseline and differential.
DR Genevisible; A2AVJ5; MM.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0031932; C:TORC2 complex; ISS:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
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:0014065; P:phosphatidylinositol 3-kinase signaling; IGI:MGI.
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; IGI:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IGI:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IGI:MGI.
DR GO; GO:0010762; P:regulation of fibroblast migration; IMP:UniProtKB.
DR GO; GO:0038203; P:TORC2 signaling; IMP:UniProtKB.
DR InterPro; IPR013745; Bit61/PRR5.
DR PANTHER; PTHR32428; PTHR32428; 1.
DR Pfam; PF08539; HbrB; 1.
PE 1: Evidence at protein 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_0000332710"
FT REGION 312..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 351..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 293
FT /note="A -> D (in Ref. 1; BAC25324)"
FT /evidence="ECO:0000305"
FT CONFLICT 317
FT /note="G -> A (in Ref. 1; BAC25324)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 370 AA; 40982 MW; 2273461DCCA5D17F CRC64;
MTRGLAPLLP IEFHKMGSFR RPRPRFMSSP VLSELPRFQA ARQALQLSSN SAWNSVQTAV
INVFKGGGLQ SNELYALNES IRRLLKSELG SFITDYFQNQ LLAKGLSFVE EKIKLCEGDN
RIEVLAEVWD HFFTETLPTL QAIFYPVQGQ ELTIRQISLL GFRDLVLLKV KLGDVLLLAQ
SKLPSSVIQM LLILQSVHEP TGPSEGYLQL EELVKQVVSP FLSISGDRSC SGPTYSLARR
HSRVRPKVTV LNYASLMTTV GRPLNEMVLT PLTEQEGEAY LEKCGSVRRH TVANAHSDIQ
LLAMATMMHS GLGEEAGGED KHLLLPPSFP PPHRQCSSEP SILDSPDELE LEDVASGSQE
DSELNCASLS
