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Protein

Proline-rich protein 5

Gene

Prr5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Subunit of mTORC2, which regulates cell growth and survival in response to hormonal signals. mTORC2 is activated by growth factors, but, in contrast to mTORC1, seems to be nutrient-insensitive. mTORC2 seems to function upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors. mTORC2 promotes the serum-induced formation of stress-fibers or F-actin. mTORC2 plays a critical role in AKT1 'Ser-473' phosphorylation, which may facilitate the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDK1 which is a prerequisite for full activation. mTORC2 regulates the phosphorylation of SGK1 at 'Ser-422'. mTORC2 also modulates the phosphorylation of PRKCA on 'Ser-657'. PRR5 plays an important role in regulation of PDGFRB expression and in modulation of platelet-derived growth factor signaling. May act as a tumor suppressor in breast cancer (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

  • actin cytoskeleton organization Source: MGI
  • cell cycle Source: UniProtKB-KW
  • positive regulation of cell migration Source: MGI
  • positive regulation of phosphatidylinositol 3-kinase signaling Source: MGI
  • positive regulation of protein phosphorylation Source: MGI
Complete GO annotation...

Keywords - Biological processi

Cell cycle

Enzyme and pathway databases

ReactomeiR-MMU-1257604. PIP3 activates AKT signaling.
R-MMU-389357. CD28 dependent PI3K/Akt signaling.
R-MMU-5218920. VEGFR2 mediated vascular permeability.
R-MMU-6804757. Regulation of TP53 Degradation.

Names & Taxonomyi

Protein namesi
Recommended name:
Proline-rich protein 5
Alternative name(s):
Protein observed with Rictor-1
Short name:
Protor-1
Gene namesi
Name:Prr5By similarity
Synonyms:Protor1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:1924714. Prr5.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 387387Proline-rich protein 5PRO_0000308163Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei253 – 2531PhosphoserineCombined sources
Modified residuei373 – 3731PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ812A5.
PaxDbiQ812A5.
PeptideAtlasiQ812A5.
PRIDEiQ812A5.

PTM databases

iPTMnetiQ812A5.
PhosphoSiteiQ812A5.

Expressioni

Tissue specificityi

Ubiquitously expressed. Expressed at high levels in kidney.1 Publication

Gene expression databases

BgeeiQ812A5.
CleanExiMM_PRR5.
GenevisibleiQ812A5. MM.

Interactioni

Subunit structurei

Part of the mammalian target of rapamycin complex 2 (mTORC2) which contains MTOR, MLST8, PRR5, RICTOR, MAPKAP1 and DEPTOR (By similarity). Contrary to mTORC1, mTORC2 does not bind to and is not sensitive to FKBP12-rapamycin. Binds directly to MTOR and RICTOR within the TORC2 complex (By similarity). Interacts with MTOR.By similarity1 Publication

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000066396.

Structurei

3D structure databases

ProteinModelPortaliQ812A5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni10 – 9687Interaction with RICTORBy similarityAdd
BLAST
Regioni189 – 21931Interaction with RICTORBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the PROTOR family.Curated

Phylogenomic databases

eggNOGiKOG4406. Eukaryota.
ENOG410XR4J. LUCA.
GeneTreeiENSGT00530000063981.
HOGENOMiHOG000290687.
HOVERGENiHBG067971.
InParanoidiQ812A5.
OMAiEYETEGM.
OrthoDBiEOG771278.
PhylomeDBiQ812A5.
TreeFamiTF314826.

Family and domain databases

InterProiIPR013745. Bit61/PRR5.
IPR016159. Cullin_repeat-like_dom.
[Graphical view]
PfamiPF08539. HbrB. 1 hit.
[Graphical view]
SUPFAMiSSF74788. SSF74788. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 12 Publications (identifier: Q812A5-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MRTLRRLKFM SSPSLSDLGK REPGAAGTDE RGTQQRRACA NATWNSIHNG
60 70 80 90 100
VIAVFQRKGL PDQELFILNE GVRQLLKTEL GSFFTEYLQN QLLTKGMVIL
110 120 130 140 150
RDKIRFYEGQ KLLDSLAETW DFFFSDVLPT LQAIFYPVQG KEPSVRQLAL
160 170 180 190 200
LHFRNTITLS VKLEDALARS HARVPPAIAQ MLLVLQGVHE SRGVTEDYLR
210 220 230 240 250
LETLIQKVVS PYLGTYGLYS NEGPCTHSCI LEKRFLRRSR SGDILAKNPV
260 270 280 290 300
VRSKSYNTPL LNPVAEHEAE GTAASGTSIR RHSVSEMTSC PEPQGFVDTP
310 320 330 340 350
GQGPSGTFRS SPTPHSGPCP SRLYPPAHSP EQGPGHGSPS TSSPETLVDQ
360 370 380
ILESADSDSE GIFIDFGRGS RSSVSDFEAP GGRPSVV
Length:387
Mass (Da):42,523
Last modified:October 23, 2007 - v2
Checksum:iCDF8984591BE2102
GO
Isoform 22 Publications (identifier: Q812A5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-9: Missing.

Show »
Length:378
Mass (Da):41,321
Checksum:i4856C69398AC9BA8
GO

Sequence cautioni

The sequence BAC32586.1 differs from that shown. Reason: Frameshift at position 296. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti49 – 491N → K in BAC38171 (PubMed:16141072).Curated
Sequence conflicti301 – 3033GQG → ATR in AAO39849 (PubMed:12559566).Curated
Sequence conflicti305 – 3051S → F in AAO39849 (PubMed:12559566).Curated
Sequence conflicti340 – 3401S → P in AAO39849 (PubMed:12559566).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 99Missing in isoform 2. 2 PublicationsVSP_052580

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF482997 mRNA. Translation: AAO39849.1.
AK046057 mRNA. Translation: BAC32586.1. Frameshift.
AK081231 mRNA. Translation: BAC38171.1.
BC024991 mRNA. Translation: AAH24991.1.
BK005634 mRNA. Translation: DAA05653.1.
CCDSiCCDS27711.1. [Q812A5-1]
RefSeqiNP_666173.4. NM_146061.4. [Q812A5-1]
XP_006520341.2. XM_006520278.2. [Q812A5-2]
XP_006520344.1. XM_006520281.2. [Q812A5-2]
UniGeneiMm.291372.

Genome annotation databases

EnsembliENSMUST00000065499; ENSMUSP00000066396; ENSMUSG00000036106. [Q812A5-1]
ENSMUST00000171460; ENSMUSP00000127890; ENSMUSG00000036106. [Q812A5-2]
GeneIDi109270.
KEGGimmu:109270.
UCSCiuc007xcd.1. mouse. [Q812A5-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF482997 mRNA. Translation: AAO39849.1.
AK046057 mRNA. Translation: BAC32586.1. Frameshift.
AK081231 mRNA. Translation: BAC38171.1.
BC024991 mRNA. Translation: AAH24991.1.
BK005634 mRNA. Translation: DAA05653.1.
CCDSiCCDS27711.1. [Q812A5-1]
RefSeqiNP_666173.4. NM_146061.4. [Q812A5-1]
XP_006520341.2. XM_006520278.2. [Q812A5-2]
XP_006520344.1. XM_006520281.2. [Q812A5-2]
UniGeneiMm.291372.

3D structure databases

ProteinModelPortaliQ812A5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000066396.

PTM databases

iPTMnetiQ812A5.
PhosphoSiteiQ812A5.

Proteomic databases

MaxQBiQ812A5.
PaxDbiQ812A5.
PeptideAtlasiQ812A5.
PRIDEiQ812A5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000065499; ENSMUSP00000066396; ENSMUSG00000036106. [Q812A5-1]
ENSMUST00000171460; ENSMUSP00000127890; ENSMUSG00000036106. [Q812A5-2]
GeneIDi109270.
KEGGimmu:109270.
UCSCiuc007xcd.1. mouse. [Q812A5-1]

Organism-specific databases

CTDi55615.
MGIiMGI:1924714. Prr5.

Phylogenomic databases

eggNOGiKOG4406. Eukaryota.
ENOG410XR4J. LUCA.
GeneTreeiENSGT00530000063981.
HOGENOMiHOG000290687.
HOVERGENiHBG067971.
InParanoidiQ812A5.
OMAiEYETEGM.
OrthoDBiEOG771278.
PhylomeDBiQ812A5.
TreeFamiTF314826.

Enzyme and pathway databases

ReactomeiR-MMU-1257604. PIP3 activates AKT signaling.
R-MMU-389357. CD28 dependent PI3K/Akt signaling.
R-MMU-5218920. VEGFR2 mediated vascular permeability.
R-MMU-6804757. Regulation of TP53 Degradation.

Miscellaneous databases

PROiQ812A5.
SOURCEiSearch...

Gene expression databases

BgeeiQ812A5.
CleanExiMM_PRR5.
GenevisibleiQ812A5. MM.

Family and domain databases

InterProiIPR013745. Bit61/PRR5.
IPR016159. Cullin_repeat-like_dom.
[Graphical view]
PfamiPF08539. HbrB. 1 hit.
[Graphical view]
SUPFAMiSSF74788. SSF74788. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of a gene encoding a putative mouse Rho GTPase activating protein gene 8, Arhgap8."
    Shan Z., Haaf T., Popescu N.C.
    Gene 303:55-61(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6JImported.
    Tissue: Corpora quadrigeminaImported and Corpus striatumImported.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: FVB/NImported.
    Tissue: KidneyImported.
  4. "PRR5 encodes a conserved proline-rich protein predominant in kidney: analysis of genomic organization, expression, and mutation status in breast and colorectal carcinomas."
    Johnstone C.N., Castellvi-Bel S., Chang L.M., Sung R.K., Bowser M.J., Pique J.M., Castells A., Rustgi A.K.
    Genomics 85:338-351(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-253 AND SER-373, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Kidney, Lung, Spleen and Testis.
  6. "Tel2 structure and function in the Hsp90-dependent maturation of mTOR and ATR complexes."
    Takai H., Xie Y., de Lange T., Pavletich N.P.
    Genes Dev. 24:2019-2030(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MTOR.

Entry informationi

Entry nameiPRR5_MOUSE
AccessioniPrimary (citable) accession number: Q812A5
Secondary accession number(s): Q5EAK2
, Q8BIE7, Q8BIK1, Q8R1A0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: October 23, 2007
Last modified: July 6, 2016
This is version 78 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Was originally thought to be the sequence of Arhgap8 but is actually the sequence of Prr5.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.