PRR5_MOUSE
ID PRR5_MOUSE Reviewed; 387 AA.
AC Q812A5; Q5EAK2; Q8BIE7; Q8BIK1; Q8R1A0;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 110.
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 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] {ECO:0000305, ECO:0000312|EMBL:AAO39849.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=12559566; DOI=10.1016/s0378-1119(02)01143-5;
RA Shan Z., Haaf T., Popescu N.C.;
RT "Identification and characterization of a gene encoding a putative mouse
RT Rho GTPase activating protein gene 8, Arhgap8.";
RL Gene 303:55-61(2003).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAC38171.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC38171.1};
RC TISSUE=Corpora quadrigemina {ECO:0000312|EMBL:BAC32586.1}, and
RC Corpus striatum {ECO:0000312|EMBL:BAC38171.1};
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 [3] {ECO:0000305, ECO:0000312|EMBL:AAH24991.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH24991.1};
RC TISSUE=Kidney {ECO:0000312|EMBL:AAH24991.1};
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).
RN [4] {ECO:0000305, ECO:0000312|EMBL:DAA05653.1}
RP IDENTIFICATION.
RX PubMed=15718101; DOI=10.1016/j.ygeno.2004.11.002;
RA Johnstone C.N., Castellvi-Bel S., Chang L.M., Sung R.K., Bowser M.J.,
RA Pique J.M., Castells A., Rustgi A.K.;
RT "PRR5 encodes a conserved proline-rich protein predominant in kidney:
RT analysis of genomic organization, expression, and mutation status in breast
RT and colorectal carcinomas.";
RL Genomics 85:338-351(2005).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-253 AND SER-373, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, Spleen, and Testis;
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 [6]
RP INTERACTION WITH MTOR.
RX PubMed=20801936; DOI=10.1101/gad.1956410;
RA Takai H., Xie Y., de Lange T., Pavletich N.P.;
RT "Tel2 structure and function in the Hsp90-dependent maturation of mTOR and
RT ATR complexes.";
RL Genes Dev. 24:2019-2030(2010).
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-422'. 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). Interacts with MTOR. {ECO:0000250,
CC ECO:0000269|PubMed:20801936}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:12559566, ECO:0000269|PubMed:16141072};
CC IsoId=Q812A5-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16141072};
CC IsoId=Q812A5-2; Sequence=VSP_052580;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Expressed at high levels in
CC kidney. {ECO:0000269|PubMed:12559566}.
CC -!- SIMILARITY: Belongs to the PROTOR family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be the sequence of Arhgap8 but is
CC actually the sequence of Prr5. {ECO:0000305,
CC ECO:0000305|PubMed:12559566}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC32586.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF482997; AAO39849.1; -; mRNA.
DR EMBL; AK046057; BAC32586.1; ALT_FRAME; mRNA.
DR EMBL; AK081231; BAC38171.1; -; mRNA.
DR EMBL; BC024991; AAH24991.1; -; mRNA.
DR EMBL; BK005634; DAA05653.1; -; mRNA.
DR CCDS; CCDS27711.1; -. [Q812A5-1]
DR CCDS; CCDS84185.1; -. [Q812A5-2]
DR RefSeq; NP_001333591.1; NM_001346662.1. [Q812A5-2]
DR RefSeq; NP_666173.4; NM_146061.4. [Q812A5-1]
DR RefSeq; XP_006520344.1; XM_006520281.3. [Q812A5-2]
DR AlphaFoldDB; Q812A5; -.
DR SMR; Q812A5; -.
DR BioGRID; 224627; 1.
DR ComplexPortal; CPX-4472; mTORC2 complex.
DR STRING; 10090.ENSMUSP00000066396; -.
DR iPTMnet; Q812A5; -.
DR PhosphoSitePlus; Q812A5; -.
DR EPD; Q812A5; -.
DR jPOST; Q812A5; -.
DR PaxDb; Q812A5; -.
DR PeptideAtlas; Q812A5; -.
DR PRIDE; Q812A5; -.
DR ProteomicsDB; 291896; -. [Q812A5-1]
DR ProteomicsDB; 291897; -. [Q812A5-2]
DR Antibodypedia; 46008; 192 antibodies from 30 providers.
DR DNASU; 109270; -.
DR Ensembl; ENSMUST00000065499; ENSMUSP00000066396; ENSMUSG00000036106. [Q812A5-1]
DR Ensembl; ENSMUST00000171460; ENSMUSP00000127890; ENSMUSG00000036106. [Q812A5-2]
DR GeneID; 109270; -.
DR KEGG; mmu:109270; -.
DR UCSC; uc007xcd.1; mouse. [Q812A5-1]
DR CTD; 55615; -.
DR MGI; MGI:1924714; Prr5.
DR VEuPathDB; HostDB:ENSMUSG00000036106; -.
DR eggNOG; KOG4406; Eukaryota.
DR GeneTree; ENSGT00530000063981; -.
DR HOGENOM; CLU_046146_0_0_1; -.
DR InParanoid; Q812A5; -.
DR OMA; TSCMEQQ; -.
DR OrthoDB; 1260193at2759; -.
DR PhylomeDB; Q812A5; -.
DR TreeFam; TF314826; -.
DR Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
DR Reactome; R-MMU-389357; CD28 dependent PI3K/Akt signaling.
DR Reactome; R-MMU-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-MMU-6804757; Regulation of TP53 Degradation.
DR BioGRID-ORCS; 109270; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Prr5; mouse.
DR PRO; PR:Q812A5; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q812A5; protein.
DR Bgee; ENSMUSG00000036106; Expressed in yolk sac and 105 other tissues.
DR Genevisible; Q812A5; MM.
DR GO; GO:0031932; C:TORC2 complex; ISO:MGI.
DR GO; GO:0005096; F:GTPase activator activity; ISO:MGI.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISO:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0031669; P:cellular response to nutrient levels; IC:ComplexPortal.
DR GO; GO:0007010; P:cytoskeleton organization; IC:ComplexPortal.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IC:ComplexPortal.
DR GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; IMP:MGI.
DR GO; GO:0016310; P:phosphorylation; ISO:MGI.
DR GO; GO:0030307; P:positive regulation of cell growth; IC:ComplexPortal.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IMP:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IMP:MGI.
DR GO; GO:0038203; P:TORC2 signaling; IBA:GO_Central.
DR InterPro; IPR013745; Bit61/PRR5.
DR InterPro; IPR016159; Cullin_repeat-like_dom_sf.
DR PANTHER; PTHR32428; PTHR32428; 1.
DR Pfam; PF08539; HbrB; 1.
DR SUPFAM; SSF74788; SSF74788; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Phosphoprotein; Reference proteome;
KW Tumor suppressor.
FT CHAIN 1..387
FT /note="Proline-rich protein 5"
FT /id="PRO_0000308163"
FT REGION 10..96
FT /note="Interaction with RICTOR"
FT /evidence="ECO:0000250|UniProtKB:P85299"
FT REGION 13..34
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..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 COMPBIAS 334..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..9
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_052580"
FT CONFLICT 49
FT /note="N -> K (in Ref. 2; BAC38171)"
FT /evidence="ECO:0000305"
FT CONFLICT 301..303
FT /note="GQG -> ATR (in Ref. 1; AAO39849)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="S -> F (in Ref. 1; AAO39849)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="S -> P (in Ref. 1; AAO39849)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 387 AA; 42523 MW; CDF8984591BE2102 CRC64;
MRTLRRLKFM SSPSLSDLGK REPGAAGTDE RGTQQRRACA NATWNSIHNG VIAVFQRKGL
PDQELFILNE GVRQLLKTEL GSFFTEYLQN QLLTKGMVIL RDKIRFYEGQ KLLDSLAETW
DFFFSDVLPT LQAIFYPVQG KEPSVRQLAL LHFRNTITLS VKLEDALARS HARVPPAIAQ
MLLVLQGVHE SRGVTEDYLR LETLIQKVVS PYLGTYGLYS NEGPCTHSCI LEKRFLRRSR
SGDILAKNPV VRSKSYNTPL LNPVAEHEAE GTAASGTSIR RHSVSEMTSC PEPQGFVDTP
GQGPSGTFRS SPTPHSGPCP SRLYPPAHSP EQGPGHGSPS TSSPETLVDQ ILESADSDSE
GIFIDFGRGS RSSVSDFEAP GGRPSVV
