RICTR_HUMAN
ID RICTR_HUMAN Reviewed; 1708 AA.
AC Q6R327; B2RNX0; B7ZMF7; Q68DT5; Q86UB7; Q8N3A0; Q8NCM6;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Rapamycin-insensitive companion of mTOR;
DE AltName: Full=AVO3 homolog;
DE Short=hAVO3;
GN Name=RICTOR {ECO:0000312|EMBL:EAW55980.1};
GN Synonyms=KIAA1999 {ECO:0000312|EMBL:BAC02708.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAS79796.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, IDENTIFICATION IN THE
RP TORC2 COMPLEX, AND INTERACTION WITH MTOR.
RX PubMed=15268862; DOI=10.1016/j.cub.2004.06.054;
RA Sarbassov D.D., Ali S.M., Kim D.-H., Guertin D.A., Latek R.R.,
RA Erdjument-Bromage H., Tempst P., Sabatini D.M.;
RT "Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive
RT and raptor-independent pathway that regulates the cytoskeleton.";
RL Curr. Biol. 14:1296-1302(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 932-1708 (ISOFORM 3), AND VARIANT PHE-837.
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4] {ECO:0000305, ECO:0000312|EMBL:CAH18135.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305, ECO:0000312|EMBL:AAH51729.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP PHE-837.
RC TISSUE=Brain, and Lymph {ECO:0000312|EMBL:AAH51729.1};
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 [6] {ECO:0000305, ECO:0000312|EMBL:BAC02708.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 434-1708 (ISOFORM 1).
RC TISSUE=Brain {ECO:0000312|EMBL:BAC02708.1};
RX PubMed=12056414; DOI=10.1093/dnares/9.2.47;
RA Ohara O., Nagase T., Mitsui G., Kohga H., Kikuno R., Hiraoka S.,
RA Takahashi Y., Kitajima S., Saga Y., Koseki H.;
RT "Characterization of size-fractionated cDNA libraries generated by the in
RT vitro recombination-assisted method.";
RL DNA Res. 9:47-57(2002).
RN [7]
RP FUNCTION, IDENTIFICATION IN THE TORC2 COMPLEX, AND PHOSPHORYLATION.
RX PubMed=15467718; DOI=10.1038/ncb1183;
RA Jacinto E., Loewith R., Schmidt A., Lin S., Ruegg M.A., Hall A., Hall M.N.;
RT "Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin
RT insensitive.";
RL Nat. Cell Biol. 6:1122-1128(2004).
RN [8] {ECO:0000305}
RP FUNCTION.
RX PubMed=15718470; DOI=10.1126/science.1106148;
RA Sarbassov D.D., Guertin D.A., Ali S.M., Sabatini D.M.;
RT "Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex.";
RL Science 307:1098-1101(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [10] {ECO:0000305}
RP IDENTIFICATION IN THE TORC2 COMPLEX, AND INTERACTION WITH PRR5 AND PRR5L.
RX PubMed=17461779; DOI=10.1042/bj20070540;
RA Pearce L.R., Huang X., Boudeau J., Pawlowski R., Wullschleger S., Deak M.,
RA Ibrahim A.F.M., Gourlay R., Magnuson M.A., Alessi D.R.;
RT "Identification of Protor as a novel Rictor-binding component of mTOR
RT complex-2.";
RL Biochem. J. 405:513-522(2007).
RN [11] {ECO:0000305}
RP IDENTIFICATION IN THE TORC2 COMPLEX, AND INTERACTION WITH PRR5.
RX PubMed=17599906; DOI=10.1074/jbc.m704343200;
RA Woo S.-Y., Kim D.-H., Jun C.-B., Kim Y.-M., Haar E.V., Lee S.-I.,
RA Hegg J.W., Bandhakavi S., Griffin T.J., Kim D.-H.;
RT "PRR5, a novel component of mTOR complex 2, regulates platelet-derived
RT growth factor receptor beta expression and signaling.";
RL J. Biol. Chem. 282:25604-25612(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND SER-1396, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-1282; SER-1388 AND
RP SER-1396, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-1284; SER-1388 AND
RP SER-1411, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [17]
RP PHOSPHORYLATION AT THR-1135.
RX PubMed=19995915; DOI=10.1128/mcb.00601-09;
RA Julien L.A., Carriere A., Moreau J., Roux P.P.;
RT "mTORC1-activated S6K1 phosphorylates Rictor on threonine 1135 and
RT regulates mTORC2 signaling.";
RL Mol. Cell. Biol. 30:908-921(2010).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND SER-1591, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [21]
RP INTERACTION WITH PRR5L.
RX PubMed=21964062; DOI=10.1016/j.cellsig.2011.09.015;
RA Holmes B., Artinian N., Anderson L., Martin J., Masri J., Cloninger C.,
RA Bernath A., Bashir T., Benavides-Serrato A., Gera J.;
RT "Protor-2 interacts with tristetraprolin to regulate mRNA stability during
RT stress.";
RL Cell. Signal. 24:309-315(2012).
RN [22]
RP INTERACTION WITH CCDC28B.
RX PubMed=23727834; DOI=10.1093/hmg/ddt253;
RA Cardenas-Rodriguez M., Irigoin F., Osborn D.P., Gascue C., Katsanis N.,
RA Beales P.L., Badano J.L.;
RT "The Bardet-Biedl syndrome-related protein CCDC28B modulates mTORC2
RT function and interacts with SIN1 to control cilia length independently of
RT the mTOR complex.";
RL Hum. Mol. Genet. 22:4031-4042(2013).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; THR-1103; THR-1135;
RP SER-1162; SER-1278; SER-1282; THR-1295; SER-1302; SER-1313; THR-1332;
RP SER-1346; SER-1353 AND SER-1385, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [24]
RP INTERACTION WITH NBN.
RX PubMed=23762398; DOI=10.1371/journal.pone.0065586;
RA Wang J.Q., Chen J.H., Chen Y.C., Chen M.Y., Hsieh C.Y., Teng S.C., Wu K.J.;
RT "Interaction between NBS1 and the mTOR/Rictor/SIN1 complex through specific
RT domains.";
RL PLoS ONE 8:E65586-E65586(2013).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1385, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [26]
RP INTERACTION WITH FBXW7; GSK3A AND GSK3B, PHOSPHORYLATION AT THR-1695,
RP UBIQUITINATION, AND MUTAGENESIS OF THR-1695.
RX PubMed=25897075; DOI=10.1074/jbc.m114.633057;
RA Koo J., Wu X., Mao Z., Khuri F.R., Sun S.Y.;
RT "Rictor Undergoes Glycogen Synthase Kinase 3 (GSK3)-dependent, FBXW7-
RT mediated Ubiquitination and Proteasomal Degradation.";
RL J. Biol. Chem. 290:14120-14129(2015).
RN [27]
RP INTERACTION WITH VACCINIA VIRUS PROTEIN F17.
RX PubMed=30078703; DOI=10.1016/j.cell.2018.06.053;
RA Meade N., Furey C., Li H., Verma R., Chai Q., Rollins M.G., DiGiuseppe S.,
RA Naghavi M.H., Walsh D.;
RT "Poxviruses Evade Cytosolic Sensing through Disruption of an mTORC1-mTORC2
RT Regulatory Circuit.";
RL Cell 0:0-0(2018).
RN [28]
RP INTERACTION WITH SIK3.
RX PubMed=30232230; DOI=10.1126/scitranslmed.aat9356;
RA Csukasi F., Duran I., Barad M., Barta T., Gudernova I., Trantirek L.,
RA Martin J.H., Kuo C.Y., Woods J., Lee H., Cohn D.H., Krejci P., Krakow D.;
RT "The PTH/PTHrP-SIK3 pathway affects skeletogenesis through altered mTOR
RT signaling.";
RL Sci. Transl. Med. 10:0-0(2018).
RN [29]
RP INTERACTION WITH USP9X; MTOR AND MAPKAP1, UBIQUITINATION AT LYS-274,
RP DEUBIQUITINATION BY USP9X, AND MUTAGENESIS OF LYS-274.
RX PubMed=33378666; DOI=10.1016/j.celrep.2020.108564;
RA Wrobel L., Siddiqi F.H., Hill S.M., Son S.M., Karabiyik C., Kim H.,
RA Rubinsztein D.C.;
RT "mTORC2 Assembly Is Regulated by USP9X-Mediated Deubiquitination of
RT RICTOR.";
RL Cell Rep. 33:108564-108564(2020).
RN [30]
RP INTERACTION WITH NCKAP1L.
RX PubMed=32647003; DOI=10.1126/science.aay5663;
RA Cook S.A., Comrie W.A., Poli M.C., Similuk M., Oler A.J., Faruqi A.J.,
RA Kuhns D.B., Yang S., Vargas-Hernandez A., Carisey A.F., Fournier B.,
RA Anderson D.E., Price S., Smelkinson M., Abou Chahla W., Forbes L.R.,
RA Mace E.M., Cao T.N., Coban-Akdemir Z.H., Jhangiani S.N., Muzny D.M.,
RA Gibbs R.A., Lupski J.R., Orange J.S., Cuvelier G.D.E., Al Hassani M.,
RA Al Kaabi N., Al Yafei Z., Jyonouchi S., Raje N., Caldwell J.W., Huang Y.,
RA Burkhardt J.K., Latour S., Chen B., ElGhazali G., Rao V.K., Chinn I.K.,
RA Lenardo M.J.;
RT "HEM1 deficiency disrupts mTORC2 and F-actin control in inherited
RT immunodysregulatory disease.";
RL Science 369:202-207(2020).
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'. Plays an essential role in
CC embryonic growth and development. {ECO:0000269|PubMed:15268862,
CC ECO:0000269|PubMed:15467718, ECO:0000269|PubMed:15718470}.
CC -!- SUBUNIT: Part of the mammalian target of rapamycin complex 2 (mTORC2)
CC which contains MTOR, MLST8, PRR5, RICTOR, MAPKAP1 and DEPTOR
CC (PubMed:15268862, PubMed:15467718, PubMed:17461779, PubMed:17599906).
CC Contrary to mTORC1, mTORC2 does not bind to and is not sensitive to
CC FKBP12-rapamycin. Binds directly to MTOR and PRR5 within the TORC2
CC complex; interaction with MTOR is enhanced by deubiquitination of
CC RICTOR by USP9X (PubMed:15268862, PubMed:17461779, PubMed:17599906,
CC PubMed:33378666). Interaction with MAPKAP1 is not enhanced by RICTOR
CC deubiquitination by USP9X (PubMed:33378666). Interacts with CCDC28B
CC (PubMed:23727834). Interacts with NBN (PubMed:23762398). Interacts with
CC PRR5L (PubMed:17461779, PubMed:21964062). Interacts with SIK3
CC (PubMed:30232230). Interacts with NCKAP1L (PubMed:32647003). Interacts
CC with kinases GSK3A and GSK3B; the interactions lead to phosphorylation
CC of RICTOR at 'Thr-1695' which facilitates its FBXW7-mediated
CC ubiquitination and subsequent degradation (PubMed:25897075). Interacts
CC with FBXW7; the interaction is enhanced by GSK3-mediated
CC phosphorylation of 'Thr-1695' and results in RICTOR ubiquitination and
CC degradation (PubMed:25897075). Interacts with USP9X; the interaction
CC results in deubiquitination of RICTOR and protection from proteasomal
CC degradation, thus promoting mTORC2 complex assembly (PubMed:33378666).
CC {ECO:0000269|PubMed:15268862, ECO:0000269|PubMed:15467718,
CC ECO:0000269|PubMed:17461779, ECO:0000269|PubMed:17599906,
CC ECO:0000269|PubMed:21964062, ECO:0000269|PubMed:23727834,
CC ECO:0000269|PubMed:23762398, ECO:0000269|PubMed:25897075,
CC ECO:0000269|PubMed:30232230, ECO:0000269|PubMed:32647003,
CC ECO:0000269|PubMed:33378666}.
CC -!- SUBUNIT: (Microbial infection) Interacts with vaccinia virus protein
CC F17; this interaction dysregulates mTOR. {ECO:0000269|PubMed:30078703}.
CC -!- INTERACTION:
CC Q6R327; Q13418: ILK; NbExp=8; IntAct=EBI-1387196, EBI-747644;
CC Q6R327; P42345: MTOR; NbExp=34; IntAct=EBI-1387196, EBI-359260;
CC Q6R327; Q8TCU6: PREX1; NbExp=3; IntAct=EBI-1387196, EBI-1046542;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1 {ECO:0000269|PubMed:15268862};
CC IsoId=Q6R327-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6R327-4; Sequence=VSP_038362, VSP_038363;
CC Name=3;
CC IsoId=Q6R327-3; Sequence=VSP_052581;
CC -!- PTM: Phosphorylated by MTOR; when part of mTORC2 (PubMed:15467718).
CC Phosphorylated at Thr-1135 by RPS6KB1; phosphorylation of RICTOR
CC inhibits mTORC2 and AKT1 signaling (PubMed:19995915). Phosphorylated at
CC Thr-1695 by GSK3A and GSK3B which facilitates RICTOR ubiquitination and
CC subsequent degradation (PubMed:25897075). {ECO:0000269|PubMed:15467718,
CC ECO:0000269|PubMed:19995915, ECO:0000269|PubMed:25897075}.
CC -!- PTM: Ubiquitinated by the SCF(FBXW7) complex, leading to its
CC degradation by the proteasome (PubMed:25897075). Deubiquitinated by
CC USP9X; deubiquitination stabilizes RICTOR and enhances its binding to
CC MTOR, thus promoting mTORC2 complex assembly (PubMed:33378666).
CC {ECO:0000269|PubMed:25897075, ECO:0000269|PubMed:33378666}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the RICTOR family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAH18135.1; Type=Miscellaneous discrepancy; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
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DR EMBL; AY515854; AAS79796.1; -; mRNA.
DR EMBL; AL834497; CAD39155.1; -; mRNA.
DR EMBL; CR749280; CAH18135.1; ALT_SEQ; mRNA.
DR EMBL; AC008964; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC109467; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471119; EAW55980.1; -; Genomic_DNA.
DR EMBL; BC051729; AAH51729.1; -; mRNA.
DR EMBL; BC137163; AAI37164.1; -; mRNA.
DR EMBL; BC137164; AAI37165.1; -; mRNA.
DR EMBL; BC144509; AAI44510.1; -; mRNA.
DR EMBL; AB082530; BAC02708.1; -; mRNA.
DR CCDS; CCDS34148.1; -. [Q6R327-1]
DR CCDS; CCDS68861.1; -. [Q6R327-3]
DR RefSeq; NP_001272368.1; NM_001285439.1. [Q6R327-3]
DR RefSeq; NP_001272369.1; NM_001285440.1.
DR RefSeq; NP_689969.2; NM_152756.4. [Q6R327-1]
DR PDB; 5ZCS; EM; 4.90 A; E/F=1-1018.
DR PDB; 6ZWM; EM; 3.20 A; E/F=1-1708.
DR PDB; 6ZWO; EM; 3.00 A; F=1-1708.
DR PDB; 7PE7; EM; 3.41 A; E/F=1-1708.
DR PDB; 7PE8; EM; 3.20 A; E=1-1708.
DR PDB; 7PE9; EM; 3.70 A; E=1-1708.
DR PDBsum; 5ZCS; -.
DR PDBsum; 6ZWM; -.
DR PDBsum; 6ZWO; -.
DR PDBsum; 7PE7; -.
DR PDBsum; 7PE8; -.
DR PDBsum; 7PE9; -.
DR AlphaFoldDB; Q6R327; -.
DR SMR; Q6R327; -.
DR BioGRID; 128962; 289.
DR ComplexPortal; CPX-4402; mTORC2 complex.
DR CORUM; Q6R327; -.
DR DIP; DIP-39479N; -.
DR IntAct; Q6R327; 79.
DR MINT; Q6R327; -.
DR STRING; 9606.ENSP00000296782; -.
DR BindingDB; Q6R327; -.
DR ChEMBL; CHEMBL1795179; -.
DR TCDB; 8.A.188.1.1; the rictor/mtorc2 (rictor) family.
DR GlyGen; Q6R327; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q6R327; -.
DR PhosphoSitePlus; Q6R327; -.
DR BioMuta; RICTOR; -.
DR DMDM; 74710068; -.
DR CPTAC; CPTAC-1337; -.
DR EPD; Q6R327; -.
DR jPOST; Q6R327; -.
DR MassIVE; Q6R327; -.
DR MaxQB; Q6R327; -.
DR PaxDb; Q6R327; -.
DR PeptideAtlas; Q6R327; -.
DR PRIDE; Q6R327; -.
DR ProteomicsDB; 67310; -. [Q6R327-1]
DR ProteomicsDB; 67311; -. [Q6R327-3]
DR ProteomicsDB; 67312; -. [Q6R327-4]
DR Antibodypedia; 23075; 685 antibodies from 41 providers.
DR DNASU; 253260; -.
DR Ensembl; ENST00000296782.9; ENSP00000296782.5; ENSG00000164327.13. [Q6R327-3]
DR Ensembl; ENST00000357387.8; ENSP00000349959.3; ENSG00000164327.13. [Q6R327-1]
DR Ensembl; ENST00000511516.5; ENSP00000423019.1; ENSG00000164327.13. [Q6R327-4]
DR GeneID; 253260; -.
DR KEGG; hsa:253260; -.
DR MANE-Select; ENST00000357387.8; ENSP00000349959.3; NM_152756.5; NP_689969.2.
DR UCSC; uc003jlo.4; human. [Q6R327-1]
DR CTD; 253260; -.
DR DisGeNET; 253260; -.
DR GeneCards; RICTOR; -.
DR HGNC; HGNC:28611; RICTOR.
DR HPA; ENSG00000164327; Low tissue specificity.
DR MIM; 609022; gene.
DR neXtProt; NX_Q6R327; -.
DR OpenTargets; ENSG00000164327; -.
DR PharmGKB; PA165660455; -.
DR VEuPathDB; HostDB:ENSG00000164327; -.
DR eggNOG; KOG3694; Eukaryota.
DR GeneTree; ENSGT00390000002096; -.
DR HOGENOM; CLU_001013_2_0_1; -.
DR InParanoid; Q6R327; -.
DR OMA; VFEYLIT; -.
DR OrthoDB; 128601at2759; -.
DR PhylomeDB; Q6R327; -.
DR TreeFam; TF343656; -.
DR PathwayCommons; Q6R327; -.
DR Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
DR Reactome; R-HSA-389357; CD28 dependent PI3K/Akt signaling.
DR Reactome; R-HSA-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-HSA-5674400; Constitutive Signaling by AKT1 E17K in Cancer.
DR Reactome; R-HSA-6804757; Regulation of TP53 Degradation.
DR SignaLink; Q6R327; -.
DR SIGNOR; Q6R327; -.
DR BioGRID-ORCS; 253260; 283 hits in 1094 CRISPR screens.
DR ChiTaRS; RICTOR; human.
DR GeneWiki; RICTOR; -.
DR GenomeRNAi; 253260; -.
DR Pharos; Q6R327; Tbio.
DR PRO; PR:Q6R327; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q6R327; protein.
DR Bgee; ENSG00000164327; Expressed in kidney epithelium and 193 other tissues.
DR ExpressionAtlas; Q6R327; baseline and differential.
DR Genevisible; Q6R327; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0031932; C:TORC2 complex; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; IBA:GO_Central.
DR GO; GO:0043022; F:ribosome binding; IEA:Ensembl.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; IMP:UniProtKB.
DR GO; GO:0031669; P:cellular response to nutrient levels; IC:ComplexPortal.
DR GO; GO:0007010; P:cytoskeleton organization; IC:ComplexPortal.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IC:ComplexPortal.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IGI:ParkinsonsUK-UCL.
DR GO; GO:0016310; P:phosphorylation; IDA:ComplexPortal.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IEA:Ensembl.
DR GO; GO:0030307; P:positive regulation of cell growth; IC:ComplexPortal.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IBA:GO_Central.
DR GO; GO:0032008; P:positive regulation of TOR signaling; IMP:UniProtKB.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:2000114; P:regulation of establishment of cell polarity; IEA:Ensembl.
DR GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl.
DR GO; GO:0043087; P:regulation of GTPase activity; IEA:Ensembl.
DR GO; GO:0050727; P:regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:0033135; P:regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
DR GO; GO:0051896; P:regulation of protein kinase B signaling; IDA:UniProtKB.
DR GO; GO:0038203; P:TORC2 signaling; IBA:GO_Central.
DR DisProt; DP02692; -.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR028268; Pianissimo_fam.
DR InterPro; IPR028267; Pianissimo_N.
DR InterPro; IPR029453; Rictor_IV.
DR InterPro; IPR029451; RICTOR_M.
DR InterPro; IPR029259; RICTOR_phospho.
DR InterPro; IPR029452; RICTOR_V.
DR PANTHER; PTHR13298; PTHR13298; 1.
DR Pfam; PF14663; RasGEF_N_2; 1.
DR Pfam; PF14666; RICTOR_M; 1.
DR Pfam; PF14664; RICTOR_N; 1.
DR Pfam; PF14665; RICTOR_phospho; 1.
DR Pfam; PF14668; RICTOR_V; 1.
DR SMART; SM01307; RICTOR_M; 1.
DR SMART; SM01308; RICTOR_N; 1.
DR SMART; SM01309; RICTOR_phospho; 1.
DR SMART; SM01310; RICTOR_V; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Developmental protein;
KW Host-virus interaction; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..1708
FT /note="Rapamycin-insensitive companion of mTOR"
FT /id="PRO_0000308179"
FT REGION 1..789
FT /note="Interaction with NBN"
FT /evidence="ECO:0000269|PubMed:23762398"
FT REGION 1022..1041
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1103..1134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1204..1252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1275..1298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1103
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1135
FT /note="Phosphothreonine; by RPS6KB1"
FT /evidence="ECO:0000269|PubMed:19995915,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1162
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1235
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6QI06"
FT MOD_RES 1278
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1282
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1284
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 1295
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1302
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1313
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1332
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1346
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1353
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1385
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1388
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 1396
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976"
FT MOD_RES 1411
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 1591
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1695
FT /note="Phosphothreonine; by GSK3-alpha and GSK3-beta"
FT /evidence="ECO:0000269|PubMed:25897075"
FT CROSSLNK 274
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:33378666"
FT VAR_SEQ 252..257
FT /note="RILAPY -> NFSTLY (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_038362"
FT VAR_SEQ 258..1708
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_038363"
FT VAR_SEQ 1379
FT /note="R -> RIDFKKKHVGGIRSLRPTITNNLFR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_052581"
FT VARIANT 837
FT /note="S -> F (in dbSNP:rs2043112)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_051320"
FT MUTAGEN 274
FT /note="K->G: Abolishes deubiquitination by USP9X and
FT increases interaction with MTOR. No effect on interaction
FT with SIN1."
FT /evidence="ECO:0000269|PubMed:33378666"
FT MUTAGEN 1695
FT /note="T->G: Reduced GSK3-mediated phosphorylation, reduced
FT interaction with FBXW7, reduced FBXW7-mediated
FT ubiquitination and increased stability."
FT /evidence="ECO:0000269|PubMed:25897075"
FT CONFLICT 545
FT /note="E -> G (in Ref. 2; CAH18135)"
FT /evidence="ECO:0000305"
FT CONFLICT 815
FT /note="F -> L (in Ref. 2; CAH18135)"
FT /evidence="ECO:0000305"
FT CONFLICT 1283
FT /note="N -> S (in Ref. 2; CAH18135)"
FT /evidence="ECO:0000305"
FT CONFLICT 1699
FT /note="Q -> R (in Ref. 5; AAH51729)"
FT /evidence="ECO:0000305"
FT HELIX 33..45
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 53..69
FT /evidence="ECO:0007829|PDB:6ZWO"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:6ZWO"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 81..88
FT /evidence="ECO:0007829|PDB:6ZWO"
FT TURN 89..93
FT /evidence="ECO:0007829|PDB:6ZWM"
FT HELIX 97..108
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 114..122
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 125..133
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 142..156
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 163..174
FT /evidence="ECO:0007829|PDB:6ZWO"
FT TURN 177..180
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 184..195
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 199..204
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 207..214
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 221..234
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 238..241
FT /evidence="ECO:0007829|PDB:6ZWO"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 250..254
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 255..258
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 274..291
FT /evidence="ECO:0007829|PDB:6ZWO"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:7PE7"
FT HELIX 295..301
FT /evidence="ECO:0007829|PDB:6ZWO"
FT TURN 304..306
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 310..314
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 315..317
FT /evidence="ECO:0007829|PDB:6ZWO"
FT TURN 321..323
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 324..334
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 346..352
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 360..362
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 364..367
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 370..376
FT /evidence="ECO:0007829|PDB:6ZWO"
FT STRAND 382..384
FT /evidence="ECO:0007829|PDB:7PE8"
FT HELIX 387..401
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 404..413
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 417..437
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 440..443
FT /evidence="ECO:0007829|PDB:6ZWO"
FT STRAND 444..446
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 450..456
FT /evidence="ECO:0007829|PDB:6ZWO"
FT STRAND 459..461
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 463..485
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 493..508
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 526..534
FT /evidence="ECO:0007829|PDB:6ZWO"
FT TURN 537..539
FT /evidence="ECO:0007829|PDB:6ZWO"
FT STRAND 542..546
FT /evidence="ECO:0007829|PDB:7PE8"
FT HELIX 548..556
FT /evidence="ECO:0007829|PDB:6ZWO"
FT STRAND 561..564
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 568..581
FT /evidence="ECO:0007829|PDB:6ZWO"
FT TURN 583..586
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 588..590
FT /evidence="ECO:0007829|PDB:6ZWM"
FT STRAND 591..594
FT /evidence="ECO:0007829|PDB:6ZWM"
FT HELIX 599..614
FT /evidence="ECO:0007829|PDB:6ZWO"
FT TURN 616..618
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 620..638
FT /evidence="ECO:0007829|PDB:6ZWO"
FT STRAND 641..643
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 648..651
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 655..658
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 659..667
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 670..678
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 682..688
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 696..702
FT /evidence="ECO:0007829|PDB:6ZWO"
FT STRAND 708..711
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 712..722
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 726..734
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 737..740
FT /evidence="ECO:0007829|PDB:6ZWO"
FT TURN 741..743
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 747..758
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 764..777
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 781..788
FT /evidence="ECO:0007829|PDB:6ZWO"
FT STRAND 795..797
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 799..805
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 806..810
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 812..820
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 824..833
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 836..851
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 882..886
FT /evidence="ECO:0007829|PDB:6ZWO"
FT TURN 887..889
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 891..897
FT /evidence="ECO:0007829|PDB:6ZWO"
FT TURN 898..900
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 902..910
FT /evidence="ECO:0007829|PDB:6ZWO"
FT STRAND 915..917
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 918..933
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 937..944
FT /evidence="ECO:0007829|PDB:6ZWO"
FT TURN 945..947
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 949..958
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 962..975
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 979..987
FT /evidence="ECO:0007829|PDB:6ZWO"
FT STRAND 990..992
FT /evidence="ECO:0007829|PDB:6ZWO"
FT STRAND 1428..1432
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 1433..1435
FT /evidence="ECO:0007829|PDB:6ZWO"
FT TURN 1445..1447
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 1480..1486
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 1489..1492
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 1523..1528
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 1610..1622
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 1629..1642
FT /evidence="ECO:0007829|PDB:6ZWO"
FT TURN 1644..1647
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 1650..1660
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 1667..1676
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 1683..1693
FT /evidence="ECO:0007829|PDB:6ZWO"
SQ SEQUENCE 1708 AA; 192218 MW; DB7B1E4A45DAE2AB CRC64;
MAAIGRGRSL KNLRVRGRND SGEENVPLDL TREPSDNLRE ILQNVARLQG VSNMRKLGHL
NNFTKLLCDI GHSEEKLGFH YEDIIICLRL ALLNEAKEVR AAGLRALRYL IQDSSILQKV
LKLKVDYLIA RCIDIQQSNE VERTQALRLV RKMITVNASL FPSSVTNSLI AVGNDGLQER
DRMVRACIAI ICELALQNPE VVALRGGLNT ILKNVIDCQL SRINEALITT ILHLLNHPKT
RQYVRADVEL ERILAPYTDF HYRHSPDTAE GQLKEDREAR FLASKMGIIA TFRSWAGIIN
LCKPGNSGIQ SLIGVLCIPN MEIRRGLLEV LYDIFRLPLP VVTEEFIEAL LSVDPGRFQD
SWRLSDGFVA AEAKTILPHR ARSRPDLMDN YLALILSAFI RNGLLEGLVE VITNSDDHIS
VRATILLGEL LHMANTILPH SHSHHLHCLP TLMNMAASFD IPKEKRLRAS AALNCLKRFH
EMKKRGPKPY SLHLDHIIQK AIATHQKRDQ YLRVQKDIFI LKDTEEALLI NLRDSQVLQH
KENLEWNWNL IGTILKWPNV NLRNYKDEQL HRFVRRLLYF YKPSSKLYAN LDLDFAKAKQ
LTVVGCQFTE FLLESEEDGQ GYLEDLVKDI VQWLNASSGM KPERSLQNNG LLTTLSQHYF
LFIGTLSCHP HGVKMLEKCS VFQCLLNLCS LKNQDHLLKL TVSSLDYSRD GLARVILSKI
LTAATDACRL YATKHLRVLL RANVEFFNNW GIELLVTQLH DKNKTISSEA LDILDEACED
KANLHALIQM KPALSHLGDK GLLLLLRFLS IPKGFSYLNE RGYVAKQLEK WHREYNSKYV
DLIEEQLNEA LTTYRKPVDG DNYVRRSNQR LQRPHVYLPI HLYGQLVHHK TGCHLLEVQN
IITELCRNVR TPDLDKWEEI KKLKASLWAL GNIGSSNWGL NLLQEENVIP DILKLAKQCE
VLSIRGTCVY VLGLIAKTKQ GCDILKCHNW DAVRHSRKHL WPVVPDDVEQ LCNELSSIPS
TLSLNSESTS SRHNSESESV PSSMFILEDD RFGSSSTSTF FLDINEDTEP TFYDRSGPIK
DKNSFPFFAS SKLVKNRILN SLTLPNKKHR SSSDPKGGKL SSESKTSNRR IRTLTEPSVD
FNHSDDFTPI STVQKTLQLE TSFMGNKHIE DTGSTPSIGE NDLKFTKNFG TENHRENTSR
ERLVVESSTS SHMKIRSQSF NTDTTTSGIS SMSSSPSRET VGVDATTMDT DCGSMSTVVS
TKTIKTSHYL TPQSNHLSLS KSNSVSLVPP GSSHTLPRRA QSLKAPSIAT IKSLADCNFS
YTSSRDAFGY ATLKRLQQQR MHPSLSHSEA LASPAKDVLF TDTITMKANS FESRLTPSRF
MKALSYASLD KEDLLSPINQ NTLQRSSSVR SMVSSATYGG SDDYIGLALP VDINDIFQVK
DIPYFQTKNI PPHDDRGARA FAHDAGGLPS GTGGLVKNSF HLLRQQMSLT EIMNSIHSDA
SLFLESTEDT GLQEHTDDNC LYCVCIEILG FQPSNQLSAI CSHSDFQDIP YSDWCEQTIH
NPLEVVPSKF SGISGCSDGV SQEGSASSTK STELLLGVKT IPDDTPMCRI LLRKEVLRLV
INLSSSVSTK CHETGLLTIK EKYPQTFDDI CLYSEVSHLL SHCTFRLPCR RFIQELFQDV
QFLQMHEEAE AVLATPPKQP IVDTSAES
