ID   LYCHS_HUMAN             Reviewed;         870 AA.
AC   Q7Z3F1; B2RCI2; D3DPE2; Q4G0Y6; Q53SJ3; Q53TA8; Q69YG8; Q86SP9; Q8N261;
AC   Q8N639; Q8N8K3; Q96MV6;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 2.
DT   27-MAR-2024, entry version 158.
DE   RecName: Full=Lysosomal cholesterol signaling protein {ECO:0000303|PubMed:36007018};
DE            Short=LYCHOS {ECO:0000303|PubMed:36007018};
DE   AltName: Full=G-protein coupled receptor PGR22 {ECO:0000303|PubMed:12679517};
GN   Name=GPR155 {ECO:0000312|HGNC:HGNC:22951};
GN   Synonyms=PGR22 {ECO:0000303|PubMed:12679517};
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]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Tongue, and Trachea;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Amygdala, and Retina;
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=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 533-675.
RX   PubMed=12679517; DOI=10.1073/pnas.0230374100;
RA   Vassilatis D.K., Hohmann J.G., Zeng H., Li F., Ranchalis J.E.,
RA   Mortrud M.T., Brown A., Rodriguez S.S., Weller J.R., Wright A.C.,
RA   Bergmann J.E., Gaitanaris G.A.;
RT   "The G protein-coupled receptor repertoires of human and mouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:4903-4908(2003).
RN   [7]
RP   FUNCTION, SUBCELLULAR LOCATION, CHOLESTEROL-BINDING, INTERACTION WITH
RP   GATOR1 COMPLEX, AND MUTAGENESIS OF 43-PHE-PRO-44; PHE-43; GLU-48; TYR-57;
RP   TYR-551; CYS-595; CYS-604; CYS-629 AND CYS-638.
RX   PubMed=36007018; DOI=10.1126/science.abg6621;
RA   Shin H.R., Citron Y.R., Wang L., Tribouillard L., Goul C.S., Stipp R.,
RA   Sugasawa Y., Jain A., Samson N., Lim C.Y., Davis O.B., Castaneda-Carpio D.,
RA   Qian M., Nomura D.K., Perera R.M., Park E., Covey D.F., Laplante M.,
RA   Evers A.S., Zoncu R.;
RT   "Lysosomal GPCR-like protein LYCHOS signals cholesterol sufficiency to
RT   mTORC1.";
RL   Science 377:1290-1298(2022).
CC   -!- FUNCTION: Cholesterol-binding protein that acts as a regulator of
CC       mTORC1 signaling pathway (PubMed:36007018). Acts as a sensor of
CC       cholesterol to signal cholesterol sufficiency to mTORC1: in presence of
CC       cholesterol, binds cholesterol, leading to disrupt interaction between
CC       the GATOR1 and KICSTOR complexes and promote mTORC1 signaling
CC       (PubMed:36007018). Upon cholesterol starvation, GPR155/LYCHOS is unable
CC       to perturb the association between GATOR1 and KICSTOR, leading to
CC       mTORC1 signaling inhibition (PubMed:36007018).
CC       {ECO:0000269|PubMed:36007018}.
CC   -!- SUBUNIT: Interacts with the GATOR1 complex; preventing interaction
CC       between GATOR1 and KICSTOR; interaction is disrupted upon cholesterol
CC       starvation. {ECO:0000269|PubMed:36007018}.
CC   -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:36007018};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB71170.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AK056381; BAB71170.1; ALT_INIT; mRNA.
DR   EMBL; AK091200; BAC03609.1; -; mRNA.
DR   EMBL; AK096665; BAC04835.1; -; mRNA.
DR   EMBL; AK315125; BAG37579.1; -; mRNA.
DR   EMBL; BX537947; CAD97915.1; -; mRNA.
DR   EMBL; AL834154; CAH10683.1; -; mRNA.
DR   EMBL; AC010894; AAY14707.1; -; Genomic_DNA.
DR   EMBL; AC018470; AAY24218.1; -; Genomic_DNA.
DR   EMBL; CH471058; EAX11137.1; -; Genomic_DNA.
DR   EMBL; CH471058; EAX11138.1; -; Genomic_DNA.
DR   EMBL; CH471058; EAX11139.1; -; Genomic_DNA.
DR   EMBL; BC028730; AAH28730.1; -; mRNA.
DR   EMBL; BC035037; AAH35037.1; -; mRNA.
DR   EMBL; AY255528; AAO85040.1; -; mRNA.
DR   CCDS; CCDS2259.1; -.
DR   RefSeq; NP_001028217.1; NM_001033045.3.
DR   RefSeq; NP_001253979.1; NM_001267050.1.
DR   RefSeq; NP_001253980.1; NM_001267051.1.
DR   RefSeq; NP_689742.4; NM_152529.6.
DR   RefSeq; XP_016858974.1; XM_017003485.1.
DR   RefSeq; XP_016858975.1; XM_017003486.1.
DR   RefSeq; XP_016858976.1; XM_017003487.1.
DR   AlphaFoldDB; Q7Z3F1; -.
DR   SMR; Q7Z3F1; -.
DR   BioGRID; 127389; 4.
DR   IntAct; Q7Z3F1; 1.
DR   STRING; 9606.ENSP00000376335; -.
DR   TCDB; 2.A.69.3.8; the auxin efflux carrier (aec) family.
DR   GlyCosmos; Q7Z3F1; 8 sites, No reported glycans.
DR   GlyGen; Q7Z3F1; 8 sites.
DR   iPTMnet; Q7Z3F1; -.
DR   PhosphoSitePlus; Q7Z3F1; -.
DR   SwissPalm; Q7Z3F1; -.
DR   BioMuta; GPR155; -.
DR   DMDM; 68052330; -.
DR   EPD; Q7Z3F1; -.
DR   jPOST; Q7Z3F1; -.
DR   MassIVE; Q7Z3F1; -.
DR   MaxQB; Q7Z3F1; -.
DR   PaxDb; 9606-ENSP00000376335; -.
DR   PeptideAtlas; Q7Z3F1; -.
DR   ProteomicsDB; 69044; -.
DR   Antibodypedia; 50637; 172 antibodies from 13 providers.
DR   DNASU; 151556; -.
DR   Ensembl; ENST00000295500.8; ENSP00000295500.4; ENSG00000163328.14.
DR   Ensembl; ENST00000392551.6; ENSP00000376334.2; ENSG00000163328.14.
DR   Ensembl; ENST00000392552.7; ENSP00000376335.2; ENSG00000163328.14.
DR   GeneID; 151556; -.
DR   KEGG; hsa:151556; -.
DR   MANE-Select; ENST00000392552.7; ENSP00000376335.2; NM_152529.7; NP_689742.4.
DR   UCSC; uc002uit.5; human.
DR   AGR; HGNC:22951; -.
DR   CTD; 151556; -.
DR   DisGeNET; 151556; -.
DR   GeneCards; GPR155; -.
DR   HGNC; HGNC:22951; GPR155.
DR   HPA; ENSG00000163328; Tissue enhanced (choroid plexus, stomach).
DR   neXtProt; NX_Q7Z3F1; -.
DR   OpenTargets; ENSG00000163328; -.
DR   PharmGKB; PA134943679; -.
DR   VEuPathDB; HostDB:ENSG00000163328; -.
DR   eggNOG; ENOG502QQ69; Eukaryota.
DR   GeneTree; ENSGT00390000004153; -.
DR   HOGENOM; CLU_018490_0_0_1; -.
DR   InParanoid; Q7Z3F1; -.
DR   OMA; DIRMTCT; -.
DR   OrthoDB; 4259952at2759; -.
DR   PhylomeDB; Q7Z3F1; -.
DR   TreeFam; TF324034; -.
DR   PathwayCommons; Q7Z3F1; -.
DR   SignaLink; Q7Z3F1; -.
DR   BioGRID-ORCS; 151556; 13 hits in 1150 CRISPR screens.
DR   ChiTaRS; GPR155; human.
DR   GeneWiki; GPR155; -.
DR   GenomeRNAi; 151556; -.
DR   Pharos; Q7Z3F1; Tbio.
DR   PRO; PR:Q7Z3F1; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; Q7Z3F1; Protein.
DR   Bgee; ENSG00000163328; Expressed in dorsal root ganglion and 188 other cell types or tissues.
DR   ExpressionAtlas; Q7Z3F1; baseline and differential.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR   GO; GO:0015485; F:cholesterol binding; IDA:UniProtKB.
DR   GO; GO:0034198; P:cellular response to amino acid starvation; IDA:UniProtKB.
DR   GO; GO:0071397; P:cellular response to cholesterol; IDA:UniProtKB.
DR   GO; GO:0050890; P:cognition; IMP:UniProtKB.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0030514; P:negative regulation of BMP signaling pathway; IBA:GO_Central.
DR   GO; GO:1904263; P:positive regulation of TORC1 signaling; IDA:UniProtKB.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   CDD; cd04443; DEP_GPR155; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR000591; DEP_dom.
DR   InterPro; IPR037368; GPR155_DEP.
DR   InterPro; IPR004776; Mem_transp_PIN-like.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR22829; DEP DOMAIN PROTEIN; 1.
DR   PANTHER; PTHR22829:SF5; INTEGRAL MEMBRANE PROTEIN GPR155; 1.
DR   Pfam; PF00610; DEP; 1.
DR   Pfam; PF03547; Mem_trans; 1.
DR   SMART; SM00049; DEP; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS50186; DEP; 1.
DR   Genevisible; Q7Z3F1; HS.
PE   1: Evidence at protein level;
KW   Glycoprotein; Lipid-binding; Lysosome; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..870
FT                   /note="Lysosomal cholesterol signaling protein"
FT                   /id="PRO_0000087551"
FT   TRANSMEM        39..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        80..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        105..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        134..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        168..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        214..234
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        244..264
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        274..294
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        316..336
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        347..367
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        382..402
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        415..435
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        439..459
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        481..501
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        521..541
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        661..681
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        692..712
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          757..835
FT                   /note="DEP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00066"
FT   BINDING         43
FT                   /ligand="cholesterol"
FT                   /ligand_id="ChEBI:CHEBI:16113"
FT                   /evidence="ECO:0000305|PubMed:36007018"
FT   BINDING         57
FT                   /ligand="cholesterol"
FT                   /ligand_id="ChEBI:CHEBI:16113"
FT                   /evidence="ECO:0000305|PubMed:36007018"
FT   CARBOHYD        9
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        15
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        29
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        198
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        309
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        381
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        543
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        612
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         43..44
FT                   /note="FP->IA: Nearly abolished cholesterol-binding."
FT                   /evidence="ECO:0000269|PubMed:36007018"
FT   MUTAGEN         43
FT                   /note="F->I: Strongly reduced cholesterol-binding."
FT                   /evidence="ECO:0000269|PubMed:36007018"
FT   MUTAGEN         48
FT                   /note="E->Q: Does not affect cholesterol-binding."
FT                   /evidence="ECO:0000269|PubMed:36007018"
FT   MUTAGEN         57
FT                   /note="Y->A: Strongly reduced cholesterol-binding."
FT                   /evidence="ECO:0000269|PubMed:36007018"
FT   MUTAGEN         551
FT                   /note="Y->A: Abolished ability to regulate mTORC1."
FT                   /evidence="ECO:0000269|PubMed:36007018"
FT   MUTAGEN         595
FT                   /note="C->A: In 4CA, abolished ability to regulate mTORC1;
FT                   when associated with A-604, A-629 and A-638."
FT                   /evidence="ECO:0000269|PubMed:36007018"
FT   MUTAGEN         604
FT                   /note="C->A: In 4CA, abolished ability to regulate mTORC1;
FT                   when associated with A-595, A-629 and A-638."
FT                   /evidence="ECO:0000269|PubMed:36007018"
FT   MUTAGEN         629
FT                   /note="C->A: In 4CA, abolished ability to regulate mTORC1;
FT                   when associated with A-595, A-604 and A-638."
FT                   /evidence="ECO:0000269|PubMed:36007018"
FT   MUTAGEN         638
FT                   /note="C->A: In 4CA, abolished ability to regulate mTORC1;
FT                   when associated with A-595, A-604 and A-629."
FT                   /evidence="ECO:0000269|PubMed:36007018"
FT   CONFLICT        33
FT                   /note="D -> G (in Ref. 1; BAC03609)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        194
FT                   /note="K -> E (in Ref. 5; AAH28730)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        260
FT                   /note="L -> H (in Ref. 1; BAB71170)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        460
FT                   /note="W -> R (in Ref. 2; CAD97915)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        517
FT                   /note="G -> A (in Ref. 2; CAH10683)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        550
FT                   /note="S -> G (in Ref. 5; AAH28730)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        638
FT                   /note="C -> R (in Ref. 2; CAD97915)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        674
FT                   /note="S -> Y (in Ref. 5; AAH28730)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        693
FT                   /note="Q -> R (in Ref. 2; CAH10683)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   870 AA;  96919 MW;  91A6CFC79B669ACB CRC64;
     MNSNLPAENL TIAVNMTKTL PTAVTHGFNS TNDPPSMSIT RLFPALLECF GIVLCGYIAG
     RANVITSTQA KGLGNFVSRF ALPALLFKNM VVLNFSNVDW SFLYSILIAK ASVFFIVCVL
     TLLVASPDSR FSKAGLFPIF ATQSNDFALG YPIVEALYQT TYPEYLQYIY LVAPISLMML
     NPIGFIFCEI QKWKDTQNAS QNKIKIVGLG LLRVLQNPIV FMVFIGIAFN FILDRKVPVY
     VENFLDGLGN SFSGSALFYL GLTMVGKIKR LKKSAFVVLI LLITAKLLVL PLLCREMVEL
     LDKGDSVVNH TSLSNYAFLY GVFPVAPGVA IFATQFNMEV EIITSGMVIS TFVSAPIMYV
     SAWLLTFPTM DPKPLAYAIQ NVSFDISIVS LISLIWSLAI LLLSKKYKQL PHMLTTNLLI
     AQSIVCAGMM IWNFVKEKNF VGQILVFVLL YSSLYSTYLW TGLLAISLFL LKKRERVQIP
     VGIIIISGWG IPALLVGVLL ITGKHNGDSI DSAFFYGKEQ MITTAVTLFC SILIAGISLM
     CMNQTAQAGS YEGFDQSQSH KVVEPGNTAF EESPAPVNEP ELFTSSIPET SCCSCSMGNG
     ELHCPSIEPI ANTSTSEPVI PSFEKNNHCV SRCNSQSCIL AQEEEQYLQS GDQQLTRHVL
     LCLLLIIGLF ANLSSCLWWL FNQEPGRLYV ELQFFCAVFN FGQGFISFGI FGLDKHLIIL
     PFKRRLEFLW NNKDTAENRD SPVSEEIKMT CQQFIHYHRD LCIRNIVKER RCGAKTSAGT
     FCGCDLVSWL IEVGLASDRG EAVIYGDRLV QGGVIQHITN EYEFRDEYLF YRFLQKSPEQ
     SPPAINANTL QQERYKEIEH SSPPSHSPKT
//