MOGS_HUMAN
ID MOGS_HUMAN Reviewed; 837 AA.
AC Q13724; A8K938; F5H6D0; Q17RN9; Q8TCT5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 5.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Mannosyl-oligosaccharide glucosidase;
DE EC=3.2.1.106;
DE AltName: Full=Processing A-glucosidase I;
GN Name=MOGS; Synonyms=GCS1;
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] (ISOFORM 1), AND VARIANTS GLN-236; ASN-239 AND
RP SER-293.
RC TISSUE=Hippocampus;
RX PubMed=7635146; DOI=10.1111/j.1432-1033.1995.tb20706.x;
RA Kalz-Fueller B., Bieberich E., Bause E.;
RT "Cloning and expression of glucosidase I from human hippocampus.";
RL Eur. J. Biochem. 231:344-351(1995).
RN [2]
RP ERRATUM OF PUBMED:7635146.
RA Kalz-Fueller B., Bieberich E., Bause E.;
RL Eur. J. Biochem. 249:912-912(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Voelker C.;
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [8]
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 [9]
RP IDENTIFICATION BY 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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [11]
RP VARIANTS CDGIIB THR-486 AND LEU-652.
RX PubMed=10788335; DOI=10.1086/302948;
RA De Praeter C.M., Gerwig G.J., Bause E., Nuytinck L.K., Vliegenthart J.F.G.,
RA Breuer W., Kamerling J.P., Espeel M.F., Martin J.-J., De Paepe A.M.,
RA Chan N.W.C., Dacremont G.A., Van Coster R.N.;
RT "A novel disorder caused by defective biosynthesis of N-linked
RT oligosaccharides due to glucosidase I deficiency.";
RL Am. J. Hum. Genet. 66:1744-1756(2000).
RN [12]
RP CHARACTERIZATION OF VARIANTS CDGIIB THR-486 AND LEU-652.
RX PubMed=12145188; DOI=10.1093/glycob/cwf050;
RA Voelker C., De Praeter C.M., Hardt B., Breuer W., Kalz-Fueller B.,
RA Van Coster R.N., Bause E.;
RT "Processing of N-linked carbohydrate chains in a patient with glucosidase I
RT deficiency (CDG type IIb).";
RL Glycobiology 12:473-483(2002).
CC -!- FUNCTION: Cleaves the distal alpha 1,2-linked glucose residue from the
CC Glc(3)Man(9)GlcNAc(2) oligosaccharide precursor in a highly specific
CC manner.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(4)-(alpha-D-Glc-(1->2)-alpha-D-Glc-(1->3)-alpha-D-Glc-
CC (1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-
CC [alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-
CC Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-
CC (1->4)-alpha-D-GlcNAc)-L-asparaginyl-[protein] = beta-D-glucose +
CC N(4)-(alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-
CC D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-
CC (1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-
CC beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc)-L-asparaginyl-
CC [protein]; Xref=Rhea:RHEA:55988, Rhea:RHEA-COMP:12806, Rhea:RHEA-
CC COMP:14355, ChEBI:CHEBI:15377, ChEBI:CHEBI:15903, ChEBI:CHEBI:59082,
CC ChEBI:CHEBI:132537; EC=3.2.1.106;
CC -!- PATHWAY: Glycan metabolism; N-glycan degradation.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type
CC II membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q13724-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13724-2; Sequence=VSP_046921;
CC -!- DISEASE: Type IIb congenital disorder of glycosylation (CDGIIb)
CC [MIM:606056]: Characterized by marked generalized hypotonia and
CC hypomotility of the neonate, dysmorphic features, including a prominent
CC occiput, short palpebral fissures, retrognathia, high arched palate,
CC generalized edema, and hypoplastic genitalia. Symptoms of the infant
CC included hepatomegaly, hypoventilation, feeding problems and seizures.
CC The clinical course was progressive and the infant did not survive more
CC than a few months. {ECO:0000269|PubMed:10788335}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 63 family. {ECO:0000305}.
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DR EMBL; X87237; CAA60683.1; -; mRNA.
DR EMBL; AJ422288; CAD19636.1; -; Genomic_DNA.
DR EMBL; AK292553; BAF85242.1; -; mRNA.
DR EMBL; AC005041; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471053; EAW99653.1; -; Genomic_DNA.
DR EMBL; BC117252; AAI17253.1; -; mRNA.
DR EMBL; BC117250; AAI17251.1; -; mRNA.
DR CCDS; CCDS42700.1; -. [Q13724-1]
DR CCDS; CCDS54370.1; -. [Q13724-2]
DR PIR; S66258; S66258.
DR RefSeq; NP_001139630.1; NM_001146158.1. [Q13724-2]
DR RefSeq; NP_006293.2; NM_006302.2. [Q13724-1]
DR AlphaFoldDB; Q13724; -.
DR SMR; Q13724; -.
DR BioGRID; 113599; 183.
DR ELM; Q13724; -.
DR IntAct; Q13724; 42.
DR MINT; Q13724; -.
DR STRING; 9606.ENSP00000233616; -.
DR ChEMBL; CHEMBL4684; -.
DR CAZy; GH63; Glycoside Hydrolase Family 63.
DR GlyConnect; 1489; 6 N-Linked glycans (1 site).
DR GlyGen; Q13724; 1 site, 7 N-linked glycans (1 site).
DR iPTMnet; Q13724; -.
DR PhosphoSitePlus; Q13724; -.
DR SwissPalm; Q13724; -.
DR BioMuta; MOGS; -.
DR DMDM; 116242490; -.
DR EPD; Q13724; -.
DR jPOST; Q13724; -.
DR MassIVE; Q13724; -.
DR MaxQB; Q13724; -.
DR PaxDb; Q13724; -.
DR PeptideAtlas; Q13724; -.
DR PRIDE; Q13724; -.
DR ProteomicsDB; 27150; -.
DR ProteomicsDB; 59667; -. [Q13724-1]
DR Antibodypedia; 2372; 186 antibodies from 25 providers.
DR DNASU; 7841; -.
DR Ensembl; ENST00000448666.7; ENSP00000410992.3; ENSG00000115275.15. [Q13724-1]
DR Ensembl; ENST00000452063.7; ENSP00000388201.2; ENSG00000115275.15. [Q13724-2]
DR GeneID; 7841; -.
DR KEGG; hsa:7841; -.
DR MANE-Select; ENST00000448666.7; ENSP00000410992.3; NM_006302.3; NP_006293.2.
DR UCSC; uc010ffi.4; human. [Q13724-1]
DR CTD; 7841; -.
DR DisGeNET; 7841; -.
DR GeneCards; MOGS; -.
DR GeneReviews; MOGS; -.
DR HGNC; HGNC:24862; MOGS.
DR HPA; ENSG00000115275; Low tissue specificity.
DR MalaCards; MOGS; -.
DR MIM; 601336; gene.
DR MIM; 606056; phenotype.
DR neXtProt; NX_Q13724; -.
DR OpenTargets; ENSG00000115275; -.
DR Orphanet; 79330; MOGS-CDG.
DR PharmGKB; PA164723075; -.
DR VEuPathDB; HostDB:ENSG00000115275; -.
DR eggNOG; KOG2161; Eukaryota.
DR GeneTree; ENSGT00390000017452; -.
DR HOGENOM; CLU_007380_1_0_1; -.
DR InParanoid; Q13724; -.
DR OMA; YWKAPLY; -.
DR OrthoDB; 278028at2759; -.
DR PhylomeDB; Q13724; -.
DR TreeFam; TF300749; -.
DR BioCyc; MetaCyc:HS03863-MON; -.
DR PathwayCommons; Q13724; -.
DR Reactome; R-HSA-4793954; Defective MOGS causes CDG-2b.
DR Reactome; R-HSA-532668; N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
DR Reactome; R-HSA-9683686; Maturation of spike protein.
DR Reactome; R-HSA-9694548; Maturation of spike protein.
DR SignaLink; Q13724; -.
DR UniPathway; UPA00280; -.
DR BioGRID-ORCS; 7841; 59 hits in 1087 CRISPR screens.
DR ChiTaRS; MOGS; human.
DR GeneWiki; GCS1; -.
DR GenomeRNAi; 7841; -.
DR Pharos; Q13724; Tbio.
DR PRO; PR:Q13724; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q13724; protein.
DR Bgee; ENSG00000115275; Expressed in body of pancreas and 121 other tissues.
DR ExpressionAtlas; Q13724; baseline and differential.
DR Genevisible; Q13724; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0004573; F:Glc3Man9GlcNAc2 oligosaccharide glucosidase activity; IBA:GO_Central.
DR GO; GO:0015926; F:glucosidase activity; TAS:ProtInc.
DR GO; GO:0009311; P:oligosaccharide metabolic process; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; TAS:Reactome.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR GO; GO:0019082; P:viral protein processing; TAS:Reactome.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.70.98.110; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR031335; Glyco_hydro_63_C.
DR InterPro; IPR031631; Glyco_hydro_63N.
DR InterPro; IPR038518; Glyco_hydro_63N_sf.
DR InterPro; IPR004888; Glycoside_hydrolase_63.
DR PANTHER; PTHR10412; PTHR10412; 1.
DR Pfam; PF03200; Glyco_hydro_63; 1.
DR Pfam; PF16923; Glyco_hydro_63N; 1.
DR SUPFAM; SSF48208; SSF48208; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disease variant; Endoplasmic reticulum; Glycoprotein;
KW Glycosidase; Hydrolase; Membrane; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..837
FT /note="Mannosyl-oligosaccharide glucosidase"
FT /id="PRO_0000057710"
FT TOPO_DOM 1..38
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 39..59
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 60..837
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 76..137
FT /note="Required for endoplasmic reticulum targeting"
FT /evidence="ECO:0000250"
FT MOTIF 3..9
FT /note="Endoplasmic reticulum targeting"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 657
FT /note="N-linked (GlcNAc...) asparagine"
FT VAR_SEQ 1..106
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_046921"
FT VARIANT 222
FT /note="G -> R (in dbSNP:rs3213671)"
FT /id="VAR_049233"
FT VARIANT 236
FT /note="E -> Q (in dbSNP:rs1063587)"
FT /evidence="ECO:0000269|PubMed:7635146"
FT /id="VAR_019361"
FT VARIANT 239
FT /note="D -> N (in dbSNP:rs1063588)"
FT /evidence="ECO:0000269|PubMed:7635146"
FT /id="VAR_019362"
FT VARIANT 293
FT /note="P -> S (in dbSNP:rs2268416)"
FT /evidence="ECO:0000269|PubMed:7635146"
FT /id="VAR_049234"
FT VARIANT 486
FT /note="R -> T (in CDGIIb; loss of activity;
FT dbSNP:rs121909291)"
FT /evidence="ECO:0000269|PubMed:10788335,
FT ECO:0000269|PubMed:12145188"
FT /id="VAR_018966"
FT VARIANT 495
FT /note="R -> P (in dbSNP:rs34075781)"
FT /id="VAR_049235"
FT VARIANT 652
FT /note="F -> L (in CDGIIb; loss of activity;
FT dbSNP:rs121909292)"
FT /evidence="ECO:0000269|PubMed:10788335,
FT ECO:0000269|PubMed:12145188"
FT /id="VAR_018967"
FT VARIANT 785
FT /note="G -> S (in dbSNP:rs35533773)"
FT /id="VAR_049236"
FT CONFLICT 330
FT /note="I -> F (in Ref. 1; CAA60683)"
FT /evidence="ECO:0000305"
FT CONFLICT 389
FT /note="V -> A (in Ref. 1; CAA60683)"
FT /evidence="ECO:0000305"
FT CONFLICT 605
FT /note="A -> G (in Ref. 1; CAA60683)"
FT /evidence="ECO:0000305"
FT CONFLICT 818
FT /note="Missing (in Ref. 1; CAA60683)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 837 AA; 91918 MW; 11C5B09301B50DEE CRC64;
MARGERRRRA VPAEGVRTAE RAARGGPGRR DGRGGGPRST AGGVALAVVV LSLALGMSGR
WVLAWYRARR AVTLHSAPPV LPADSSSPAV APDLFWGTYR PHVYFGMKTR SPKPLLTGLM
WAQQGTTPGT PKLRHTCEQG DGVGPYGWEF HDGLSFGRQH IQDGALRLTT EFVKRPGGQH
GGDWSWRVTV EPQDSGTSAL PLVSLFFYVV TDGKEVLLPE VGAKGQLKFI SGHTSELGDF
RFTLLPPTSP GDTAPKYGSY NVFWTSNPGL PLLTEMVKSR LNSWFQHRPP GAPPERYLGL
PGSLKWEDRG PSGQGQGQFL IQQVTLKIPI SIEFVFESGS AQAGGNQALP RLAGSLLTQA
LESHAEGFRE RFEKTFQLKE KGLSSGEQVL GQAALSGLLG GIGYFYGQGL VLPDIGVEGS
EQKVDPALFP PVPLFTAVPS RSFFPRGFLW DEGFHQLVVQ RWDPSLTREA LGHWLGLLNA
DGWIGREQIL GDEARARVPP EFLVQRAVHA NPPTLLLPVA HMLEVGDPDD LAFLRKALPR
LHAWFSWLHQ SQAGPLPLSY RWRGRDPALP TLLNPKTLPS GLDDYPRASH PSVTERHLDL
RCWVALGARV LTRLAEHLGE AEVAAELGPL AASLEAAESL DELHWAPELG VFADFGNHTK
AVQLKPRPPQ GLVRVVGRPQ PQLQYVDALG YVSLFPLLLR LLDPTSSRLG PLLDILADSR
HLWSPFGLRS LAASSSFYGQ RNSEHDPPYW RGAVWLNVNY LALGALHHYG HLEGPHQARA
AKLHGELRAN VVGNVWRQYQ ATGFLWEQYS DRDGRGMGCR PFHGWTSLVL LAMAEDY
