ID NPRL3_HUMAN Reviewed; 569 AA. AC Q12980; D3DU40; Q1W6H0; Q4TT56; Q92469; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 05-FEB-2025, entry version 160. DE RecName: Full=GATOR1 complex protein NPRL3 {ECO:0000305}; DE AltName: Full=-14 gene protein {ECO:0000303|PubMed:8575760}; DE AltName: Full=Alpha-globin regulatory element-containing gene protein {ECO:0000303|PubMed:8575760}; DE AltName: Full=Nitrogen permease regulator 3-like protein {ECO:0000312|HGNC:HGNC:14124}; DE AltName: Full=Protein CGTHBA; GN Name=NPRL3 {ECO:0000303|PubMed:26505888, ECO:0000312|HGNC:HGNC:14124}; GN Synonyms=C16orf35 {ECO:0000312|HGNC:HGNC:14124}, CGTHBA, GN MARE {ECO:0000305|PubMed:8575760}; 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 [MRNA]. RX PubMed=8575760; DOI=10.1006/geno.1995.9951; RA Vyas P., Vickers M.A., Picketts D.J., Higgs D.; RT "Conservation of position and sequence of a novel, widely expressed gene RT containing the major human alpha-globin regulatory element."; RL Genomics 29:679-689(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=16728641; DOI=10.1126/science.1126431; RA De Gobbi M., Viprakasit V., Hughes J.R., Fisher C., Buckle V.J., Ayyub H., RA Gibbons R.J., Vernimmen D., Yoshinaga Y., de Jong P., Cheng J.-F., RA Rubin E.M., Wood W.G., Bowden D., Higgs D.R.; RT "A regulatory SNP causes a human genetic disease by creating a new RT transcriptional promoter."; RL Science 312:1215-1217(2006). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). 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 INTERACTION WITH NPRL2. RX PubMed=19521502; DOI=10.1371/journal.pgen.1000515; RA Neklesa T.K., Davis R.W.; RT "A genome-wide screen for regulators of TORC1 in response to amino acid RT starvation reveals a conserved Npr2/3 complex."; RL PLoS Genet. 5:E1000515-E1000515(2009). RN [6] RP FUNCTION, IDENTIFICATION IN GATOR COMPLEX, AND INTERACTION WITH RRAG RP PROTEINS. RX PubMed=23723238; DOI=10.1126/science.1232044; RA Bar-Peled L., Chantranupong L., Cherniack A.D., Chen W.W., Ottina K.A., RA Grabiner B.C., Spear E.D., Carter S.L., Meyerson M., Sabatini D.M.; RT "A Tumor suppressor complex with GAP activity for the Rag GTPases that RT signal amino acid sufficiency to mTORC1."; RL Science 340:1100-1106(2013). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-476, 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 [8] RP SUBCELLULAR LOCATION. RX PubMed=28199306; DOI=10.1038/nature21423; RA Wolfson R.L., Chantranupong L., Wyant G.A., Gu X., Orozco J.M., Shen K., RA Condon K.J., Petri S., Kedir J., Scaria S.M., Abu-Remaileh M., RA Frankel W.N., Sabatini D.M.; RT "KICSTOR recruits GATOR1 to the lysosome and is necessary for nutrients to RT regulate mTORC1."; RL Nature 543:438-442(2017). RN [9] RP INTERACTION WITH GPR155. 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). RN [10] {ECO:0007744|PDB:6CES, ECO:0007744|PDB:6CET} RP STRUCTURE BY ELECTRON MICROSCOPY (4.00 ANGSTROMS) IN COMPLEX WITH RRAGA; RP RRAGC; DEPDC5 AND NPRL2, FUNCTION, AND IDENTIFICATION IN GATOR1 COMPLEX. RX PubMed=29590090; DOI=10.1038/nature26158; RA Shen K., Huang R.K., Brignole E.J., Condon K.J., Valenstein M.L., RA Chantranupong L., Bomaliyamu A., Choe A., Hong C., Yu Z., Sabatini D.M.; RT "Architecture of the human GATOR1 and GATOR1-Rag GTPases complexes."; RL Nature 556:64-69(2018). RN [11] {ECO:0007744|PDB:7T3A, ECO:0007744|PDB:7T3B, ECO:0007744|PDB:7T3C} RP STRUCTURE BY ELECTRON MICROSCOPY (3.90 ANGSTROMS) IN COMPLEX WITH RRAGA; RP RRAGC; DEPDC5; NPRL2; LAMTOR1; LAMTOR2; LAMTOR3; LAMTOR4 AND LAMTOR5, RP FUNCTION, AND IDENTIFICATION IN GATOR1 COMPLEX. RX PubMed=35338845; DOI=10.1016/j.molcel.2022.03.002; RA Egri S.B., Ouch C., Chou H.T., Yu Z., Song K., Xu C., Shen K.; RT "Cryo-EM structures of the human GATOR1-Rag-Ragulator complex reveal a RT spatial-constraint regulated GAP mechanism."; RL Mol. Cell 82:1836-1849(2022). RN [12] RP INVOLVEMENT IN FFEVF3, VARIANTS FFEVF3 GLN-92 AND LYS-249, AND TISSUE RP SPECIFICITY. RX PubMed=26505888; DOI=10.1002/ana.24547; RG Epilepsy Electroclinical Study Group; RA Ricos M.G., Hodgson B.L., Pippucci T., Saidin A., Ong Y.S., Heron S.E., RA Licchetta L., Bisulli F., Bayly M.A., Hughes J., Baldassari S., Palombo F., RA Santucci M., Meletti S., Berkovic S.F., Rubboli G., Thomas P.Q., RA Scheffer I.E., Tinuper P., Geoghegan J., Schreiber A.W., Dibbens L.M.; RT "Mutations in the mammalian target of rapamycin pathway regulators NPRL2 RT and NPRL3 cause focal epilepsy."; RL Ann. Neurol. 79:120-131(2016). RN [13] RP INVOLVEMENT IN FFEVF3, AND VARIANT FFEVF3 GLN-92. RX PubMed=26285051; DOI=10.1002/ana.24502; RA Sim J.C., Scerri T., Fanjul-Fernandez M., Riseley J.R., Gillies G., RA Pope K., van Roozendaal H., Heng J.I., Mandelstam S.A., McGillivray G., RA MacGregor D., Kannan L., Maixner W., Harvey A.S., Amor D.J., RA Delatycki M.B., Crino P.B., Bahlo M., Lockhart P.J., Leventer R.J.; RT "Familial cortical dysplasia caused by mutation in the mammalian target of RT rapamycin regulator NPRL3."; RL Ann. Neurol. 79:132-137(2016). RN [14] RP INVOLVEMENT IN FFEVF3, VARIANT FFEVF3 LYS-249, AND TISSUE SPECIFICITY. RX PubMed=27173016; DOI=10.1111/epi.13391; RA Weckhuysen S., Marsan E., Lambrecq V., Marchal C., Morin-Brureau M., RA An-Gourfinkel I., Baulac M., Fohlen M., Kallay Zetchi C., Seeck M., RA de la Grange P., Dermaut B., Meurs A., Thomas P., Chassoux F., Leguern E., RA Picard F., Baulac S.; RT "Involvement of GATOR complex genes in familial focal epilepsies and focal RT cortical dysplasia."; RL Epilepsia 57:994-1003(2016). CC -!- FUNCTION: As a component of the GATOR1 complex functions as an CC inhibitor of the amino acid-sensing branch of the mTORC1 pathway CC (PubMed:23723238, PubMed:29590090, PubMed:35338845). In response to CC amino acid depletion, the GATOR1 complex has GTPase activating protein CC (GAP) activity and strongly increases GTP hydrolysis by RagA/RRAGA (or CC RagB/RRAGB) within heterodimeric Rag complexes, thereby turning them CC into their inactive GDP-bound form, releasing mTORC1 from lysosomal CC surface and inhibiting mTORC1 signaling (PubMed:23723238, CC PubMed:29590090, PubMed:35338845). In the presence of abundant amino CC acids, the GATOR1 complex is negatively regulated by GATOR2, the other CC GATOR subcomplex, in this amino acid-sensing branch of the TORC1 CC pathway (PubMed:23723238). {ECO:0000269|PubMed:23723238, CC ECO:0000269|PubMed:29590090, ECO:0000269|PubMed:35338845}. CC -!- SUBUNIT: Within the GATOR complex, component of the GATOR1 subcomplex, CC made of DEPDC5, NPRL2 and NPRL3 (PubMed:23723238, PubMed:29590090, CC PubMed:35338845). GATOR1 mediates the strong interaction of the GATOR CC complex with small GTPases Rag (RagA/RRAGA, RagB/RRAGB, RagC/RRAGC CC and/or RagD/RRAGD) heterodimers (PubMed:23723238). GATOR1 interacts CC with GPR155/LYCHOS; interaction takes place in presence of cholesterol CC and prevents interaction between GATOR1 and KICSTOR (PubMed:36007018). CC {ECO:0000269|PubMed:23723238, ECO:0000269|PubMed:29590090, CC ECO:0000269|PubMed:35338845, ECO:0000269|PubMed:36007018}. CC -!- INTERACTION: CC Q12980; Q8WTW4: NPRL2; NbExp=9; IntAct=EBI-2650314, EBI-1043552; CC Q12980; Q5T011: SZT2; NbExp=5; IntAct=EBI-2650314, EBI-10749411; CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:28199306}. CC Note=Localization to lysosomes is mediated by the KICSTOR complex and CC is amino acid-independent. {ECO:0000269|PubMed:28199306}. CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in the frontal lobe CC cortex as well as in the temporal, parietal, and occipital lobes CC (PubMed:26505888, PubMed:27173016). {ECO:0000269|PubMed:26505888, CC ECO:0000269|PubMed:27173016}. CC -!- DISEASE: Note=Inactivating mutations and truncating deletions in the CC genes encoding GATOR1 proteins are detected in glioblastoma and ovarian CC tumors and are associated with loss of heterozygosity events. CC Inactivation of GATOR1 proteins promotes constitutive localization of CC mTORC1 to the lysosomal membrane and blocks mTORC1 inactivation CC following amino acid withdrawal (PubMed:23723238). CC {ECO:0000269|PubMed:23723238}. CC -!- DISEASE: Epilepsy, familial focal, with variable foci 3 (FFEVF3) CC [MIM:617118]: An autosomal dominant form of epilepsy characterized by CC focal seizures arising from different cortical regions, including the CC temporal, frontal, parietal, and occipital lobes. Seizure types CC commonly include temporal lobe epilepsy, frontal lobe epilepsy, and CC nocturnal frontal lobe epilepsy. Some patients may have intellectual CC disability or autism spectrum disorders. Seizure onset usually occurs CC in the first or second decades, although later onset has been reported, CC and there is phenotypic variability within families. A subset of CC patients have structural brain abnormalities. Penetrance of the CC disorder is incomplete. {ECO:0000269|PubMed:26285051, CC ECO:0000269|PubMed:26505888, ECO:0000269|PubMed:27173016}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the NPR3 family. {ECO:0000305}. CC -!- CAUTION: Ser-489 is missing in the human genome assembly but is present CC in all available mRNAs and ESTs. {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; X90857; CAA62368.1; -; mRNA. DR EMBL; DQ431198; ABD95907.1; -; Genomic_DNA. DR EMBL; Z69666; CAI94885.1; -; Genomic_DNA. DR EMBL; Z69720; CAI94885.1; JOINED; Genomic_DNA. DR EMBL; Z84722; CAI94885.1; JOINED; Genomic_DNA. DR EMBL; Z69720; CAI95611.1; -; Genomic_DNA. DR EMBL; Z69666; CAI95611.1; JOINED; Genomic_DNA. DR EMBL; Z84722; CAI95611.1; JOINED; Genomic_DNA. DR EMBL; CH471112; EAW85865.1; -; Genomic_DNA. DR EMBL; CH471112; EAW85867.1; -; Genomic_DNA. DR CCDS; CCDS73795.1; -. DR RefSeq; NP_001070818.1; NM_001077350.2. DR PDB; 6CES; EM; 4.00 A; M=1-569. DR PDB; 6CET; EM; 4.40 A; M=1-569. DR PDB; 7T3A; EM; 4.00 A; C=1-569. DR PDB; 7T3B; EM; 3.90 A; C=1-569. DR PDB; 7T3C; EM; 4.00 A; C=1-569. DR PDB; 8FW5; EM; 3.08 A; C=1-569. DR PDBsum; 6CES; -. DR PDBsum; 6CET; -. DR PDBsum; 7T3A; -. DR PDBsum; 7T3B; -. DR PDBsum; 7T3C; -. DR PDBsum; 8FW5; -. DR AlphaFoldDB; Q12980; -. DR EMDB; EMD-25652; -. DR EMDB; EMD-25653; -. DR EMDB; EMD-25654; -. DR EMDB; EMD-29497; -. DR EMDB; EMD-7464; -. DR EMDB; EMD-7465; -. DR SMR; Q12980; -. DR BioGRID; 113796; 118. DR ComplexPortal; CPX-6226; GATOR1 complex. DR CORUM; Q12980; -. DR DIP; DIP-62051N; -. DR IntAct; Q12980; 58. DR STRING; 9606.ENSP00000483814; -. DR GlyConnect; 2060; 1 N-Linked glycan (1 site). DR GlyCosmos; Q12980; 1 site, 2 glycans. DR GlyGen; Q12980; 2 sites, 2 N-linked glycans (1 site), 1 O-linked glycan (1 site). DR iPTMnet; Q12980; -. DR PhosphoSitePlus; Q12980; -. DR BioMuta; NPRL3; -. DR DMDM; 18202492; -. DR jPOST; Q12980; -. DR MassIVE; Q12980; -. DR PaxDb; 9606-ENSP00000483814; -. DR PeptideAtlas; Q12980; -. DR ProteomicsDB; 59074; -. DR Pumba; Q12980; -. DR Antibodypedia; 1565; 112 antibodies from 27 providers. DR DNASU; 8131; -. DR Ensembl; ENST00000611875.5; ENSP00000478273.1; ENSG00000103148.17. DR GeneID; 8131; -. DR KEGG; hsa:8131; -. DR MANE-Select; ENST00000611875.5; ENSP00000478273.1; NM_001077350.3; NP_001070818.1. DR UCSC; uc032dmr.2; human. DR AGR; HGNC:14124; -. DR CTD; 8131; -. DR DisGeNET; 8131; -. DR GeneCards; NPRL3; -. DR GeneReviews; NPRL3; -. DR HGNC; HGNC:14124; NPRL3. DR HPA; ENSG00000103148; Low tissue specificity. DR MalaCards; NPRL3; -. DR MIM; 600928; gene. DR MIM; 617118; phenotype. DR neXtProt; NX_Q12980; -. DR OpenTargets; ENSG00000103148; -. DR Orphanet; 98820; Familial focal epilepsy with variable foci. DR PharmGKB; PA25550; -. DR VEuPathDB; HostDB:ENSG00000103148; -. DR eggNOG; KOG3830; Eukaryota. DR GeneTree; ENSGT00390000015916; -. DR HOGENOM; CLU_014030_1_0_1; -. DR InParanoid; Q12980; -. DR OMA; CNLAFRY; -. DR OrthoDB; 18648at2759; -. DR PhylomeDB; Q12980; -. DR TreeFam; TF105965; -. DR PathwayCommons; Q12980; -. DR Reactome; R-HSA-9639288; Amino acids regulate mTORC1. DR SignaLink; Q12980; -. DR SIGNOR; Q12980; -. DR BioGRID-ORCS; 8131; 42 hits in 325 CRISPR screens. DR ChiTaRS; NPRL3; human. DR GenomeRNAi; 8131; -. DR Pharos; Q12980; Tbio. DR PRO; PR:Q12980; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; Q12980; protein. DR Bgee; ENSG00000103148; Expressed in blood and 195 other cell types or tissues. DR ExpressionAtlas; Q12980; baseline and differential. DR GO; GO:1990130; C:GATOR1 complex; IDA:UniProtKB. DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB. DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW. DR GO; GO:0035909; P:aorta morphogenesis; IEA:Ensembl. DR GO; GO:0048738; P:cardiac muscle tissue development; IEA:Ensembl. DR GO; GO:0034198; P:cellular response to amino acid starvation; IDA:UniProtKB. DR GO; GO:1904262; P:negative regulation of TORC1 signaling; IDA:UniProtKB. DR GO; GO:0010508; P:positive regulation of autophagy; IBA:GO_Central. DR GO; GO:0060021; P:roof of mouth development; IEA:Ensembl. DR GO; GO:0038202; P:TORC1 signaling; IBA:GO_Central. DR GO; GO:0003281; P:ventricular septum development; IEA:Ensembl. DR InterPro; IPR005365; Npr3. DR PANTHER; PTHR13153; CGTHBA PROTEIN -14 GENE PROTEIN; 1. DR PANTHER; PTHR13153:SF5; GATOR COMPLEX PROTEIN NPRL3; 1. DR Pfam; PF03666; NPR3; 1. PE 1: Evidence at protein level; KW 3D-structure; Disease variant; Epilepsy; GTPase activation; Lysosome; KW Membrane; Phosphoprotein; Proteomics identification; Reference proteome. FT CHAIN 1..569 FT /note="GATOR1 complex protein NPRL3" FT /id="PRO_0000220638" FT REGION 27..60 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 416..477 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 34..52 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 438..468 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 476 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT VARIANT 92 FT /note="R -> Q (in FFEVF3; uncertain significance; FT dbSNP:rs367729589)" FT /evidence="ECO:0000269|PubMed:26285051, FT ECO:0000269|PubMed:26505888" FT /id="VAR_077126" FT VARIANT 249 FT /note="E -> K (in FFEVF3; uncertain significance; FT dbSNP:rs200041907)" FT /evidence="ECO:0000269|PubMed:26505888, FT ECO:0000269|PubMed:27173016" FT /id="VAR_077127" FT CONFLICT 489 FT /note="Missing (in Ref. 2; CAI94885/CAI95611)" FT /evidence="ECO:0000305" FT STRAND 8..16 FT /evidence="ECO:0007829|PDB:8FW5" FT STRAND 21..26 FT /evidence="ECO:0007829|PDB:8FW5" FT HELIX 66..73 FT /evidence="ECO:0007829|PDB:8FW5" FT HELIX 77..79 FT /evidence="ECO:0007829|PDB:8FW5" FT STRAND 84..95 FT /evidence="ECO:0007829|PDB:8FW5" FT STRAND 121..131 FT /evidence="ECO:0007829|PDB:8FW5" FT HELIX 136..160 FT /evidence="ECO:0007829|PDB:8FW5" FT HELIX 162..172 FT /evidence="ECO:0007829|PDB:8FW5" FT HELIX 194..197 FT /evidence="ECO:0007829|PDB:8FW5" FT HELIX 199..212 FT /evidence="ECO:0007829|PDB:8FW5" FT STRAND 260..265 FT /evidence="ECO:0007829|PDB:8FW5" FT HELIX 267..273 FT /evidence="ECO:0007829|PDB:8FW5" FT HELIX 280..288 FT /evidence="ECO:0007829|PDB:8FW5" FT STRAND 291..293 FT /evidence="ECO:0007829|PDB:8FW5" FT HELIX 295..301 FT /evidence="ECO:0007829|PDB:8FW5" FT HELIX 306..318 FT /evidence="ECO:0007829|PDB:8FW5" FT STRAND 321..325 FT /evidence="ECO:0007829|PDB:8FW5" FT STRAND 333..336 FT /evidence="ECO:0007829|PDB:8FW5" FT HELIX 347..355 FT /evidence="ECO:0007829|PDB:8FW5" FT HELIX 361..367 FT /evidence="ECO:0007829|PDB:8FW5" FT HELIX 374..377 FT /evidence="ECO:0007829|PDB:8FW5" FT STRAND 380..382 FT /evidence="ECO:0007829|PDB:8FW5" FT HELIX 384..399 FT /evidence="ECO:0007829|PDB:8FW5" FT STRAND 403..412 FT /evidence="ECO:0007829|PDB:8FW5" FT HELIX 481..487 FT /evidence="ECO:0007829|PDB:8FW5" FT STRAND 488..490 FT /evidence="ECO:0007829|PDB:8FW5" FT HELIX 492..500 FT /evidence="ECO:0007829|PDB:8FW5" FT HELIX 502..505 FT /evidence="ECO:0007829|PDB:8FW5" FT HELIX 507..515 FT /evidence="ECO:0007829|PDB:8FW5" FT TURN 516..521 FT /evidence="ECO:0007829|PDB:8FW5" FT STRAND 522..525 FT /evidence="ECO:0007829|PDB:8FW5" FT HELIX 526..532 FT /evidence="ECO:0007829|PDB:8FW5" FT HELIX 537..546 FT /evidence="ECO:0007829|PDB:8FW5" FT TURN 547..550 FT /evidence="ECO:0007829|PDB:8FW5" FT STRAND 551..557 FT /evidence="ECO:0007829|PDB:8FW5" FT TURN 559..563 FT /evidence="ECO:0007829|PDB:8FW5" SQ SEQUENCE 569 AA; 63605 MW; 44BEF42AA7F2841D CRC64; MRDNTSPISV ILVSSGSRGN KLLFRYPFQR SQEHPASQTS KPRSRYAASN TGDHADEQDG DSRFSDVILA TILATKSEMC GQKFELKIDN VRFVGHPTLL QHALGQISKT DPSPKREAPT MILFNVVFAL RANADPSVIN CLHNLSRRIA TVLQHEERRC QYLTREAKLI LALQDEVSAM ADGNEGPQSP FHHILPKCKL ARDLKEAYDS LCTSGVVRLH INSWLEVSFC LPHKIHYAAS SLIPPEAIER SLKAIRPYHA LLLLSDEKSL LGELPIDCSP ALVRVIKTTS AVKNLQQLAQ DADLALLQVF QLAAHLVYWG KAIIIYPLCE NNVYMLSPNA SVCLYSPLAE QFSHQFPSHD LPSVLAKFSL PVSLSEFRNP LAPAVQETQL IQMVVWMLQR RLLIQLHTYV CLMASPSEEE PRPREDDVPF TARVGGRSLS TPNALSFGSP TSSDDMTLTS PSMDNSSAEL LPSGDSPLNQ RMTENLLASL SEHERAAILS VPAAQNPEDL RMFARLLHYF RGRHHLEEIM YNENTRRSQL LMLFDKFRSV LVVTTHEDPV IAVFQALLP //