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Q6QI06 (RICTR_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Rapamycin-insensitive companion of mTOR
Alternative name(s):
AVO3 homolog
Short name=mAVO3
Protein pianissimo
Gene names
Name:Rictor
Synonyms:Kiaa1999
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1708 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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'. Plays an essential role in embryonic growth and development. Ref.2 Ref.7 Ref.8 Ref.9

Subunit structure

Part of the mammalian target of rapamycin complex 2 (mTORC2) which contains MTOR, MLST8, PRR5, RICTOR, MAPKAP1 and DEPTOR. Contrary to mTORC1, mTORC2 does not bind to and is not sensitive to FKBP12-rapamycin. Binds directly to MTOR and PRR5 within the TORC2 complex. May interact with PRR5L. Ref.1 Ref.2 Ref.8

Post-translational modification

Phosphorylated by MTOR; when part of mTORC2. Phosphorylated at Thr-1135 by RPS6KB1; phosphorylation of RICTOR inhibits mTORC2 and AKT1 signaling By similarity.

Disruption phenotype

Mice develop normally until E9.5, and then display growth arrest and embryonic lethality by E11.5. Ref.2 Ref.9

Sequence similarities

Belongs to the pianissimo family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MtorQ9JLN92EBI-4286572,EBI-1571628

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.1 Ref.2 (identifier: Q6QI06-1)

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.
Isoform 2 Ref.4 (identifier: Q6QI06-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-152: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 17081708Rapamycin-insensitive companion of mTOR
PRO_0000308180

Amino acid modifications

Modified residue211Phosphoserine Ref.10 UniProtKB Q6R327
Modified residue11351Phosphothreonine; by RPS6KB1 By similarity
Modified residue11761Phosphoserine Ref.10
Modified residue12811Phosphoserine By similarity
Modified residue12831Phosphoserine By similarity
Modified residue13871Phosphoserine By similarity
Modified residue13951Phosphoserine By similarity
Modified residue14101Phosphoserine By similarity
Modified residue15911Phosphoserine By similarity

Natural variations

Alternative sequence1 – 152152Missing in isoform 2. Ref.4
VSP_052583

Experimental info

Sequence conflict151I → V in AAR89074. Ref.1
Sequence conflict1851R → Q in AAR89074. Ref.1
Sequence conflict4051L → I in AAR89074. Ref.1
Sequence conflict6981I → L in AAS46920. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 309CEE9B1404316D

FASTA1,708191,570
        10         20         30         40         50         60 
MAAIGRGRSL KNLRIRGRND SGEENVPLDL TREPSDNLRE ILQNVAKLQG VSNMRKLGHL 

        70         80         90        100        110        120 
NNFTKLLCDI GHSEEKLGFN YEDIIICLRL ALLNEAKEVR AAGLRALRYL IQDSSILQKV 

       130        140        150        160        170        180 
LKLKVDYLIA RCIDIQQSNE VERTQALRLV RKMITVNASL FPSSVANSLI AVGNDGLQER 

       190        200        210        220        230        240 
DRMVRACIAI ICELALQNPE VVALRGGLNT ILKNVIDCQL SRINEALITT ILHLLNHPKT 

       250        260        270        280        290        300 
RQYVRADVEL ERILAPYTDF HYRHSPDTAE GQLKEDREAR FLASKMGIIA TFRSWAGIIN 

       310        320        330        340        350        360 
LCKPGNSGIQ SLIGVLCIPN MEIRRGLLEV LYDIFRLPLP VVTDEFIEAL LSVDPGRFQD 

       370        380        390        400        410        420 
SWRLSDGFVA AEAKTILPHR ARSRPDLMDN YLALILSAFI RNGLLEGLVE VITNSDDHIS 

       430        440        450        460        470        480 
VRATILLGEL LHMANTILPH SHSHHLHCLP TLMNMAASFD IPKEKRLRAS AALNCLNRFH 

       490        500        510        520        530        540 
EMKKRGPKPY SLHLDHIIQK AIATHHKRDQ YLRVQKDIFV LKDTEEALLI NLRDSQVLQH 

       550        560        570        580        590        600 
KENLDWDWNL IGTILKWPNV NLRNYKDEQL HRFVRRLLYF YKPSSKLYAS LDLDLAKSKQ 

       610        620        630        640        650        660 
LTVVGCQFTE FLLESEEDGQ GYLEDLVKDI VQWLNASSGV KPERSLQNNG LLTTLSQHYF 

       670        680        690        700        710        720 
LFIGTLSCHP HGVKMLEKCS VFQCLLNLCS LKNQDHLIKL TVSSLDYSRD GLARVILSKI 

       730        740        750        760        770        780 
LTAATDACRL YATKHLRVLL RANVEFFNNW GIELLVTQLH DKNKTISSEA LDILDEACED 

       790        800        810        820        830        840 
KANLHALIQM KPALSHLGDK GLLLLLRFLS IPKGFSYLNE RGYVAKQLEK WHKEYNSKYV 

       850        860        870        880        890        900 
DLIEEQLNEA LTTYRKPIDG DNYVRRSNQR LQRPHVYLPV HLYGQLVHHK TGCHLLEVQS 

       910        920        930        940        950        960 
IITELCHNVR TPDLDKWEDI KKLKASLWAL GNIGSSNWGL NLLQEENVIP DILKLAKQCE 

       970        980        990       1000       1010       1020 
VLSIRGTCVY VLGLIAKTKQ GCDILKCHSW DSVRHSRKHL WPVVPDDVEQ LCNELSSVPS 

      1030       1040       1050       1060       1070       1080 
TLSLNSESTS SRHNSESESA PSSMFMLEDD RFGSTSTSTF FLDINEDAEP AFYDRPGPIK 

      1090       1100       1110       1120       1130       1140 
DKNSFPFFGS SKLVKNRILN SLTLPTKKHR SSSDPKGGKL SSENKTSNRR IRTLTEPSVD 

      1150       1160       1170       1180       1190       1200 
LNHSEDFTSS SAQKSLQLEP SFVGNKHLED AGSTPSIGEN DLKFPKSFGT ETHRENTSRE 

      1210       1220       1230       1240       1250       1260 
RLVVEGSASS HIKIRSQSFN TDTTTSGISS MSSSPSRETV AVDPTAMDTD CGSLSTVVST 

      1270       1280       1290       1300       1310       1320 
KTVKTSHYLT PQSNHLSLSK SNSVSLVPPG SSHTLPRRAQ SLKAPSIATI KSLADCNFSY 

      1330       1340       1350       1360       1370       1380 
TSSRDAFGYA TLKRLQQQRM HPSLSHSEAL ASPAKDVLFT DTITMKANSF ESRLTPSRFM 

      1390       1400       1410       1420       1430       1440 
KALSYASLDK EDLLSPINHN TLQRSSSVRS MVSSATYGGS DDYIGLALPV DINDIFQIKD 

      1450       1460       1470       1480       1490       1500 
VPYFQSKHVP PPDDRGARMF SHDGAGLSSG AGGLVKNSFH LLRQQMSLTE IMNSVHSDAS 

      1510       1520       1530       1540       1550       1560 
LFLESTEDTG LQEHTDDNCL YCVCIELLGF QPSNQLSSIC SHSDLQDIPY SDWCEQTIHN 

      1570       1580       1590       1600       1610       1620 
PLEVVPSKFS GISGCSDGAS QEEGSASSTK STELLLGVKT IPDDTPMCRI LLRKEVLRLV 

      1630       1640       1650       1660       1670       1680 
VNLSSSVSTK CHETGLLTIK EKYPQTFDDI CLYSEVSHLL SHCTFRLQCR RFIQELFQDV 

      1690       1700 
QFLQMHEEAE AVLAIPPIQP IVDESAES 

« Hide

Isoform 2 [UniParc].

Checksum: 80A368FADB2B90EC
Show »

FASTA1,556174,268

References

« Hide 'large scale' references
[1]"Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive."
Jacinto E., Loewith R., Schmidt A., Lin S., Ruegg M.A., Hall A., Hall M.N.
Nat. Cell Biol. 6:1122-1128(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION IN TORC2 COMPLEX.
Strain: C3H.
[2]"Multiallelic disruption of the rictor gene in mice reveals that mTOR complex 2 is essential for fetal growth and viability."
Shiota C., Woo J.-T., Lindner J., Shelton K.D., Magnuson M.A.
Dev. Cell 11:583-589(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, IDENTIFICATION IN TORC2 COMPLEX, DISRUPTION PHENOTYPE.
Strain: LAF1.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"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: C57BL/6.
Tissue: Brain.
[5]"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. expand/collapse author list , 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] OF 1-825 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1347-1708 (ISOFORM 1/2).
Strain: C57BL/6J.
Tissue: Cerebellum and Embryo.
[6]"Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 826-1708 (ISOFORM 1/2).
Tissue: Thymus.
[7]"mTOR.RICTOR is the Ser473 kinase for Akt/protein kinase B in 3T3-L1 adipocytes."
Hresko R.C., Mueckler M.
J. Biol. Chem. 280:40406-40416(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"SIN1/MIP1 maintains rictor-mTOR complex integrity and regulates Akt phosphorylation and substrate specificity."
Jacinto E., Facchinetti V., Liu D., Soto N., Wei S., Jung S.Y., Huang Q., Qin J., Su B.
Cell 127:125-137(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN TORC2 COMPLEX.
[9]"Ablation in mice of the mTORC components raptor, rictor, or mLST8 reveals that mTORC2 is required for signaling to Akt-FOXO and PKCalpha, but not S6K1."
Guertin D.A., Stevens D.M., Thoreen C.C., Burds A.A., Kalaany N.Y., Moffat J., Brown M., Fitzgerald K.J., Sabatini D.M.
Dev. Cell 11:859-871(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[10]"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry."
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M.
J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND SER-1176, MASS SPECTROMETRY.
Tissue: Melanoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY497009 mRNA. Translation: AAR89074.1.
AY540053 mRNA. Translation: AAS46920.1.
AC102825 Genomic DNA. No translation available.
AC158901 Genomic DNA. No translation available.
BC058643 mRNA. Translation: AAH58643.1.
BC120903 mRNA. Translation: AAI20904.1.
AK036149 mRNA. Translation: BAC29321.2.
AK075662 mRNA. Translation: BAC35882.1.
AK173326 mRNA. Translation: BAD32604.1.
IPIIPI00399440.
IPI00869420.
RefSeqNP_084444.3. NM_030168.3.
UniGeneMm.275811.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

DIPDIP-46323N.
IntActQ6QI06. 2 interactions.

PTM databases

PhosphoSiteQ6QI06.

Proteomic databases

PaxDbQ6QI06.
PRIDEQ6QI06.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000061656; ENSMUSP00000051809; ENSMUSG00000050310.
GeneID78757.
KEGGmmu:78757.
UCSCuc007vdr.2. mouse.
uc011zrb.1. mouse.

Organism-specific databases

CTD253260.
MGIMGI:1926007. Rictor.
RougeSearch...

Phylogenomic databases

eggNOGNOG305760.
GeneTreeENSGT00390000002096.
HOVERGENHBG060827.
InParanoidQ6QI06.
KOK08267.
OMARFHEMKK.
OrthoDBEOG43XV2K.

Gene expression databases

BgeeQ6QI06.
CleanExMM_4921505C17RIK.
GenevestigatorQ6QI06.

Family and domain databases

InterProIPR016024. ARM-type_fold.
[Graphical view]
SUPFAMSSF48371. ARM-type_fold. 2 hits.
ProtoNetSearch...

Other

NextBio349448.
SOURCESearch...

Entry information

Entry nameRICTR_MOUSE
AccessionPrimary (citable) accession number: Q6QI06
Secondary accession number(s): E9QPE0 expand/collapse secondary AC list , Q0VAV4, Q69Z40, Q6PDL2, Q6RI74, Q8BPH9, Q8CBF2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: July 27, 2011
Last modified: May 1, 2013
This is version 70 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families