GLMP_MOUSE
ID GLMP_MOUSE Reviewed; 404 AA.
AC Q9JHJ3; Q3TUF5; Q3UBV7; Q8C6H7;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Glycosylated lysosomal membrane protein {ECO:0000312|MGI:MGI:1913318};
DE AltName: Full=Lysosomal protein NCU-G1 {ECO:0000305};
DE Flags: Precursor;
GN Name=Glmp {ECO:0000312|MGI:MGI:1913318};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=11444019; DOI=10.1023/a:1002745202344;
RA Kawamura T., Kuroda N., Kimura Y., Lazoura E., Okada N., Okada H.;
RT "cDNA of a novel mRNA expressed predominantly in mouse kidney.";
RL Biochem. Genet. 39:33-42(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Bone marrow, Dendritic cell, Head, Liver, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 [4]
RP SUBCELLULAR LOCATION, GLYCOSYLATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP TYR-400.
RX PubMed=19489740; DOI=10.1042/bj20090567;
RA Schieweck O., Damme M., Schroeder B., Hasilik A., Schmidt B., Lubke T.;
RT "NCU-G1 is a highly glycosylated integral membrane protein of the
RT lysosome.";
RL Biochem. J. 422:83-90(2009).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-133 AND ASN-185.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [6]
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=24487409; DOI=10.1242/dmm.014050;
RA Kong X.Y., Nesset C.K., Damme M., Loberg E.M., Lubke T., Maehlen J.,
RA Andersson K.B., Lorenzo P.I., Roos N., Thoresen G.H., Rustan A.C.,
RA Kase E.T., Eskild W.;
RT "Loss of lysosomal membrane protein NCU-G1 in mice results in spontaneous
RT liver fibrosis with accumulation of lipofuscin and iron in Kupffer cells.";
RL Dis. Model. Mech. 7:351-362(2014).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=26047317; DOI=10.1371/journal.pone.0129402;
RA Kong X.Y., Kase E.T., Herskedal A., Schjalm C., Damme M., Nesset C.K.,
RA Thoresen G.H., Rustan A.C., Eskild W.;
RT "Lack of the Lysosomal Membrane Protein, GLMP, in Mice Results in Metabolic
RT Dysregulation in Liver.";
RL PLoS ONE 10:e0129402-e0129402(2015).
RN [8]
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=26707125; DOI=10.3109/13813455.2015.1120752;
RA Kong X.Y., Feng Y.Z., Eftestoel E., Kase E.T., Haugum H., Eskild W.,
RA Rustan A.C., Thoresen G.H.;
RT "Increased glucose utilization and decreased fatty acid metabolism in
RT myotubes from Glmp(gt/gt) mice.";
RL Arch. Physiol. Biochem. 122:36-45(2016).
RN [9]
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=27141234; DOI=10.1186/s13069-016-0042-4;
RA Nesset C.K., Kong X.Y., Damme M., Schjalm C., Roos N., Loeberg E.M.,
RA Eskild W.;
RT "Age-dependent development of liver fibrosis in Glmp (gt/gt) mice.";
RL Fibrogenesis Tissue Repair 9:5-5(2016).
RN [10]
RP FUNCTION, INTERACTION WITH MFSD1, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=31661432; DOI=10.7554/elife.50025;
RA Massa Lopez D., Thelen M., Stahl F., Thiel C., Linhorst A., Sylvester M.,
RA Hermanns-Borgmeyer I., Luellmann-Rauch R., Eskild W., Saftig P., Damme M.;
RT "The lysosomal transporter MFSD1 is essential for liver homeostasis and
RT critically depends on its accessory subunit GLMP.";
RL Elife 8:e50025-e50025(2019).
RN [11]
RP FUNCTION, INTERACTION WITH MFSD1, GLYCOSYLATION AT ASN-85; ASN-94; ASN-133;
RP ASN-157; ASN-185; ASN-228 AND ASN-331, AND MUTAGENESIS OF ASN-85; ASN-94;
RP ASN-133; ASN-157; ASN-166; ASN-185; ASN-228; ASN-331 AND TYR-400.
RX PubMed=32959924; DOI=10.1096/fj.202000912rr;
RA Lopez D.M., Kaehlau L., Jungnickel K.E.J., Loew C., Damme M.;
RT "Characterization of the complex of the lysosomal membrane transporter
RT MFSD1 and its accessory subunit GLMP.";
RL FASEB J. 34:14695-14709(2020).
RN [12] {ECO:0007744|PDB:6NYQ}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
RA Manzanillo P., Huang C.S., Boenig G., Calses P., Scherl A., Reichelt M.,
RA Katakam A.K., Martin F., Hymowitz S.G., Ouyang W.;
RT "GLMP is essential for bone-marrow hematopoiesis and lysosomal glycolipid
RT metabolism.";
RL Submitted (FEB-2019) to the PDB data bank.
CC -!- FUNCTION: Required to protect lysosomal transporter MFSD1 from
CC lysosomal proteolysis and for MFSD1 lysosomal localization.
CC {ECO:0000269|PubMed:31661432, ECO:0000269|PubMed:32959924}.
CC -!- SUBUNIT: Interacts (via lumenal domain) with lysosomal protein MFSD1;
CC the interaction starts while both proteins are still in the endoplasmic
CC reticulum and is required for stability and lysosomal localization of
CC MFSD1. {ECO:0000269|PubMed:31661432, ECO:0000269|PubMed:32959924}.
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:19489740,
CC ECO:0000269|PubMed:31661432}; Single-pass type I membrane protein
CC {ECO:0000255}; Lumenal side {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Detected in brain, heart, liver, kidney, lung,
CC intestine, testis and spleen (PubMed:11444019, PubMed:19489740,
CC PubMed:24487409). Expressed at highest levels in kidney cortex
CC (PubMed:11444019, PubMed:19489740). However, another study reports
CC highest expression levels in lung (PubMed:24487409). Expressed in
CC myoblasts with expression increasing during differentiation into
CC myotubes (PubMed:26707125). {ECO:0000269|PubMed:11444019,
CC ECO:0000269|PubMed:19489740, ECO:0000269|PubMed:24487409,
CC ECO:0000269|PubMed:26707125}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout embryogenesis
CC (PubMed:11444019). After birth, there is a rapid increase in expression
CC within the first week of life, reaching adult levels by week 2
CC (PubMed:27141234). {ECO:0000269|PubMed:11444019,
CC ECO:0000269|PubMed:27141234}.
CC -!- PTM: Highly N-glycosylated (PubMed:19489740, PubMed:19349973). N-
CC glycosylation is essential for GLMP stability and for MFSD1 lysosomal
CC localization (PubMed:32959924). {ECO:0000269|PubMed:19349973,
CC ECO:0000269|PubMed:19489740, ECO:0000269|PubMed:32959924}.
CC -!- DISRUPTION PHENOTYPE: Viable and fertile (PubMed:24487409).
CC Significantly reduced levels of Mfsd1 (PubMed:31661432). Splenomegaly
CC (PubMed:24487409, PubMed:26047317). Reduced size of epididymal fat pads
CC (PubMed:26047317). Enlargement of liver and spontaneous development of
CC liver fibrosis which is not present at birth but develops shortly after
CC and reaches a peak at 4 months of age (PubMed:24487409,
CC PubMed:26047317, PubMed:27141234). The liver phenotype is associated
CC with increased expression of markers for inflammatory responses,
CC apoptosis and oxidative stress (PubMed:24487409, PubMed:27141234).
CC Livers show local foci where hepatocytes are lost and liver sinusoidal
CC endothelial cells are replaced by ordinary capillary endothelium
CC (PubMed:31661432). Reduced liver function (PubMed:27141234). Kupffer
CC cells have increased accumulation of iron and lipofuscin
CC (PubMed:24487409). Decreased blood glucose and serum lipids and
CC increased liver triacylglycerol (PubMed:26047317). Altered liver
CC expression of genes involved in metabolism including decreased
CC expression of Acox1, Angptl4, Fabp1, Slc2a2/Glut2, Ppara, Plin2 and
CC Plin5 and increased expression of Apoc3, Cd36, Fasn, Pdk4, Ppard,
CC Pparg, Scd1 and Scd2 (PubMed:26047317). Increased liver expression of
CC Pecam31/Cd31 and Vwf (PubMed:31661432). Increased glucose and fatty
CC acid uptake in hepatocytes and increased glucose oxidation
CC (PubMed:26047317). Increased de novo lipogenesis in hepatocytes
CC (PubMed:26047317). Increased hepatocyte proliferation and oval cell
CC mobilization up to 6 months of age (PubMed:27141234). Increased
CC frequency of liver tumors after 12 months of age (PubMed:27141234).
CC Anemia, thrombocytopenia, and reduced levels of white blood cells
CC (PubMed:27141234). No effect on composition of muscle fibers but
CC myotubes metabolize glucose faster and have a larger pool of
CC intracellular glycogen while oleic acid uptake, storage and oxidation
CC are significantly reduced (PubMed:26707125). Increased myotube
CC expression of Myh2, Myh4 and Scd1 and decreased expression of Cd36,
CC Myh7, Plin2, Ppara, Ppard, Pparg, Pgc1a and Scd2 (PubMed:26707125).
CC {ECO:0000269|PubMed:24487409, ECO:0000269|PubMed:26047317,
CC ECO:0000269|PubMed:26707125, ECO:0000269|PubMed:27141234,
CC ECO:0000269|PubMed:31661432}.
CC -!- SIMILARITY: Belongs to the GLMP family. {ECO:0000305}.
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DR EMBL; AB027141; BAA92527.1; -; mRNA.
DR EMBL; AB027142; BAA95676.1; -; mRNA.
DR EMBL; AK075614; BAC35859.1; -; mRNA.
DR EMBL; AK150794; BAE29857.1; -; mRNA.
DR EMBL; AK154340; BAE32526.1; -; mRNA.
DR EMBL; AK160793; BAE36016.1; -; mRNA.
DR EMBL; AK170696; BAE41960.1; -; mRNA.
DR EMBL; AK171042; BAE42207.1; -; mRNA.
DR EMBL; BC021547; AAH21547.1; -; mRNA.
DR CCDS; CCDS17469.1; -.
DR RefSeq; NP_064387.1; NM_020003.1.
DR PDB; 6NYQ; X-ray; 1.85 A; C=1-404.
DR PDBsum; 6NYQ; -.
DR AlphaFoldDB; Q9JHJ3; -.
DR SMR; Q9JHJ3; -.
DR IntAct; Q9JHJ3; 3.
DR STRING; 10090.ENSMUSP00000135398; -.
DR GlyConnect; 2357; 1 N-Linked glycan (1 site).
DR GlyGen; Q9JHJ3; 9 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q9JHJ3; -.
DR PhosphoSitePlus; Q9JHJ3; -.
DR EPD; Q9JHJ3; -.
DR jPOST; Q9JHJ3; -.
DR MaxQB; Q9JHJ3; -.
DR PaxDb; Q9JHJ3; -.
DR PeptideAtlas; Q9JHJ3; -.
DR PRIDE; Q9JHJ3; -.
DR ProteomicsDB; 263367; -.
DR ABCD; Q9JHJ3; 7 sequenced antibodies.
DR Antibodypedia; 34210; 43 antibodies from 11 providers.
DR Ensembl; ENSMUST00000177005; ENSMUSP00000135398; ENSMUSG00000001418.
DR GeneID; 56700; -.
DR KEGG; mmu:56700; -.
DR UCSC; uc008pup.1; mouse.
DR CTD; 112770; -.
DR MGI; MGI:1913318; Glmp.
DR VEuPathDB; HostDB:ENSMUSG00000001418; -.
DR eggNOG; ENOG502QSBM; Eukaryota.
DR GeneTree; ENSGT00390000005131; -.
DR InParanoid; Q9JHJ3; -.
DR OMA; TLHYLWD; -.
DR OrthoDB; 562253at2759; -.
DR PhylomeDB; Q9JHJ3; -.
DR TreeFam; TF324431; -.
DR BioGRID-ORCS; 56700; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Glmp; mouse.
DR PRO; PR:Q9JHJ3; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9JHJ3; protein.
DR Bgee; ENSMUSG00000001418; Expressed in ileal epithelium and 260 other tissues.
DR ExpressionAtlas; Q9JHJ3; baseline and differential.
DR Genevisible; Q9JHJ3; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0061462; P:protein localization to lysosome; IMP:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IMP:UniProtKB.
DR InterPro; IPR029382; NCU-G1.
DR PANTHER; PTHR31981; PTHR31981; 1.
DR Pfam; PF15065; NCU-G1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycoprotein; Lysosome; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..404
FT /note="Glycosylated lysosomal membrane protein"
FT /evidence="ECO:0000305"
FT /id="PRO_0000284485"
FT TOPO_DOM 36..370
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 371..391
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 392..404
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOTIF 400..404
FT /note="Lysosomal targeting motif"
FT /evidence="ECO:0000269|PubMed:19489740,
FT ECO:0000269|PubMed:32959924"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:32959924"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:32959924"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973,
FT ECO:0000269|PubMed:32959924"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:32959924"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973,
FT ECO:0000269|PubMed:32959924"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:32959924"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:32959924"
FT MUTAGEN 85
FT /note="N->A: Reduced glycosylation."
FT /evidence="ECO:0000269|PubMed:32959924"
FT MUTAGEN 94
FT /note="N->A: Reduced glycosylation."
FT /evidence="ECO:0000269|PubMed:32959924"
FT MUTAGEN 133
FT /note="N->A: Reduced glycosylation."
FT /evidence="ECO:0000269|PubMed:32959924"
FT MUTAGEN 157
FT /note="N->A: Reduced glycosylation."
FT /evidence="ECO:0000269|PubMed:32959924"
FT MUTAGEN 166
FT /note="N->A: No effect on glycosylation."
FT /evidence="ECO:0000269|PubMed:32959924"
FT MUTAGEN 185
FT /note="N->A: Reduced glycosylation."
FT /evidence="ECO:0000269|PubMed:32959924"
FT MUTAGEN 228
FT /note="N->A: Reduced glycosylation."
FT /evidence="ECO:0000269|PubMed:32959924"
FT MUTAGEN 331
FT /note="N->A: Reduced glycosylation."
FT /evidence="ECO:0000269|PubMed:32959924"
FT MUTAGEN 400
FT /note="Y->A: Abolishes lysosomal localization and results
FT in mislocalization to the cell surface. Localizes to
FT lysosomes when expressed with wild-type MFSD1."
FT /evidence="ECO:0000269|PubMed:19489740,
FT ECO:0000269|PubMed:32959924"
FT CONFLICT 21
FT /note="L -> I (in Ref. 2; BAC35859)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="P -> T (in Ref. 2; BAE29857)"
FT /evidence="ECO:0000305"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:6NYQ"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:6NYQ"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:6NYQ"
FT STRAND 66..72
FT /evidence="ECO:0007829|PDB:6NYQ"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:6NYQ"
FT STRAND 78..85
FT /evidence="ECO:0007829|PDB:6NYQ"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:6NYQ"
FT HELIX 95..98
FT /evidence="ECO:0007829|PDB:6NYQ"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:6NYQ"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:6NYQ"
FT STRAND 115..130
FT /evidence="ECO:0007829|PDB:6NYQ"
FT STRAND 139..144
FT /evidence="ECO:0007829|PDB:6NYQ"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:6NYQ"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:6NYQ"
FT TURN 158..161
FT /evidence="ECO:0007829|PDB:6NYQ"
FT TURN 164..167
FT /evidence="ECO:0007829|PDB:6NYQ"
FT STRAND 168..176
FT /evidence="ECO:0007829|PDB:6NYQ"
FT TURN 182..185
FT /evidence="ECO:0007829|PDB:6NYQ"
FT STRAND 187..194
FT /evidence="ECO:0007829|PDB:6NYQ"
FT STRAND 213..222
FT /evidence="ECO:0007829|PDB:6NYQ"
FT STRAND 230..239
FT /evidence="ECO:0007829|PDB:6NYQ"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:6NYQ"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:6NYQ"
FT STRAND 266..280
FT /evidence="ECO:0007829|PDB:6NYQ"
FT STRAND 282..287
FT /evidence="ECO:0007829|PDB:6NYQ"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:6NYQ"
FT STRAND 295..300
FT /evidence="ECO:0007829|PDB:6NYQ"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:6NYQ"
FT HELIX 308..310
FT /evidence="ECO:0007829|PDB:6NYQ"
FT HELIX 315..321
FT /evidence="ECO:0007829|PDB:6NYQ"
FT STRAND 327..334
FT /evidence="ECO:0007829|PDB:6NYQ"
FT STRAND 337..340
FT /evidence="ECO:0007829|PDB:6NYQ"
FT TURN 342..345
FT /evidence="ECO:0007829|PDB:6NYQ"
FT STRAND 346..358
FT /evidence="ECO:0007829|PDB:6NYQ"
SQ SEQUENCE 404 AA; 43804 MW; 65D490B53880B8B3 CRC64;
MFRCWGPHWG WVPCAPTPWL LLSLLVCSAP FGLQGEETRQ VSMEVISGWP NPQNLLHIRA
VGSNSTLHYV WSSLGPPAVV LVATNTTQSV LSVNWSLLLS PDPAGALMVL PKSSIQFSSA
LVFTRLLEFD STNASEGAQP PGKPYPPYSL AKFSWNNITN SLDLANLSAD FQGRPVDDPT
GAFANGSLTF KVQAFSRSGR PAQPPRLLHT ADVCQLEVAL VGASPRGNHS LFGLEVATLG
QGPDCPSVNE RNSIDDEYAP AVFQLNQLLW GSSPSGFMQW RPVAFSEEER ARESALPCQA
STLHSTLASS LPHSPIVQAF FGSQNNFCAF NLTFGAPTGP GYWDQYYLCW SMLLGMGFPP
VDIFSPLVLG IMAVALGAPG LMFLGGGLFL LLRHRRYSEY QSIN
