GLCE_HUMAN
ID GLCE_HUMAN Reviewed; 617 AA.
AC O94923; Q6GUQ2;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 3.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=D-glucuronyl C5-epimerase;
DE EC=5.1.3.17 {ECO:0000269|PubMed:20118238, ECO:0000269|PubMed:22528493, ECO:0000269|PubMed:30872481};
DE AltName: Full=Heparan sulfate C5-epimerase;
DE Short=Hsepi;
DE AltName: Full=Heparin/heparan sulfate:glucuronic acid C5-epimerase;
DE AltName: Full=Heparosan-N-sulfate-glucuronate 5-epimerase;
GN Name=GLCE; Synonyms=KIAA0836 {ECO:0000312|EMBL:BAA74859.1};
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 {ECO:0000312|EMBL:BAA74859.1};
RN [1] {ECO:0000312|EMBL:AAT48654.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Ghiselli G.;
RT "Homo sapiens D-glucuronyl C5-epimerase (GLCE).";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-617, AND VARIANT ILE-597.
RC TISSUE=Brain;
RX PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:355-364(1998).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-225.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [5]
RP CATALYTIC ACTIVITY, FUNCTION, AND MUTAGENESIS OF TYR-146; TYR-162; TYR-168;
RP TYR-210 AND TYR-222.
RX PubMed=20118238; DOI=10.1074/jbc.m109.081059;
RA Li K., Bethea H.N., Liu J.;
RT "Using engineered 2-O-sulfotransferase to determine the activity of heparan
RT sulfate C5-epimerase and its mutants.";
RL J. Biol. Chem. 285:11106-11113(2010).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=22528493; DOI=10.1074/jbc.m112.359885;
RA Sheng J., Xu Y., Dulaney S.B., Huang X., Liu J.;
RT "Uncovering a biphasic catalytic mode of C5-epimerase in heparan sulfate
RT biosynthesis.";
RL J. Biol. Chem. 287:20996-21002(2012).
RN [7] {ECO:0007744|PDB:6HZZ, ECO:0007744|PDB:6I01, ECO:0007744|PDB:6I02}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 98-617 OF WILD-TYPE AND MUTANT
RP PHE-578 IN COMPLEXES WITH CALCIUM AND SUBSTRATE ANALOGS, FUNCTION,
RP CATALYTIC ACTIVITY, SUBUNIT, PATHWAY, GLYCOSYLATION AT ASN-225; ASN-303 AND
RP ASN-393, AND MUTAGENESIS OF GLU-499; TYR-500 AND TYR-578.
RX PubMed=30872481; DOI=10.1073/pnas.1818333116;
RA Debarnot C., Monneau Y.R., Roig-Zamboni V., Delauzun V., Le Narvor C.,
RA Richard E., Henault J., Goulet A., Fadel F., Vives R.R., Priem B.,
RA Bonnaffe D., Lortat-Jacob H., Bourne Y.;
RT "Substrate binding mode and catalytic mechanism of human heparan sulfate d-
RT glucuronyl C5 epimerase.";
RL Proc. Natl. Acad. Sci. U.S.A. 116:6760-6765(2019).
CC -!- FUNCTION: Converts D-glucuronic acid residues adjacent to N-sulfate
CC sugar residues to L-iduronic acid residues, both in maturing heparan
CC sulfate (HS) and heparin chains. This is important for further
CC modifications that determine the specificity of interactions between
CC these glycosaminoglycans and proteins. {ECO:0000269|PubMed:20118238,
CC ECO:0000269|PubMed:22528493, ECO:0000269|PubMed:30872481}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[heparosan-N-sulfate](n) = [heparan-N-sulfate](n);
CC Xref=Rhea:RHEA:20197, Rhea:RHEA-COMP:9556, Rhea:RHEA-COMP:9557,
CC ChEBI:CHEBI:58041, ChEBI:CHEBI:58287; EC=5.1.3.17;
CC Evidence={ECO:0000269|PubMed:20118238, ECO:0000269|PubMed:22528493,
CC ECO:0000269|PubMed:30872481};
CC -!- PATHWAY: Glycan metabolism; heparan sulfate biosynthesis.
CC {ECO:0000305|PubMed:22528493, ECO:0000305|PubMed:30872481}.
CC -!- PATHWAY: Glycan metabolism; heparin biosynthesis. {ECO:0000305}.
CC -!- SUBUNIT: Homodimer (PubMed:30872481). Interacts with HS2ST1.
CC {ECO:0000250|UniProtKB:Q9EPS3, ECO:0000269|PubMed:30872481}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q9EPS3}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q9EPS3}.
CC -!- SIMILARITY: Belongs to the D-glucuronyl C5-epimerase family.
CC {ECO:0000305}.
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DR EMBL; AY635582; AAT48654.1; -; mRNA.
DR EMBL; AC026992; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AB020643; BAA74859.1; -; mRNA.
DR CCDS; CCDS32277.1; -.
DR RefSeq; NP_001311022.1; NM_001324093.1.
DR RefSeq; NP_001311023.1; NM_001324094.1.
DR RefSeq; NP_056369.1; NM_015554.2.
DR RefSeq; XP_005254355.1; XM_005254298.3.
DR PDB; 6HZZ; X-ray; 2.52 A; A/B=98-617.
DR PDB; 6I01; X-ray; 2.10 A; A/B=98-617.
DR PDB; 6I02; X-ray; 2.45 A; A/B=98-617.
DR PDBsum; 6HZZ; -.
DR PDBsum; 6I01; -.
DR PDBsum; 6I02; -.
DR AlphaFoldDB; O94923; -.
DR SMR; O94923; -.
DR BioGRID; 117501; 50.
DR IntAct; O94923; 20.
DR MINT; O94923; -.
DR STRING; 9606.ENSP00000261858; -.
DR GlyGen; O94923; 4 sites, 1 O-linked glycan (1 site).
DR iPTMnet; O94923; -.
DR PhosphoSitePlus; O94923; -.
DR SwissPalm; O94923; -.
DR BioMuta; GLCE; -.
DR EPD; O94923; -.
DR jPOST; O94923; -.
DR MassIVE; O94923; -.
DR MaxQB; O94923; -.
DR PaxDb; O94923; -.
DR PeptideAtlas; O94923; -.
DR PRIDE; O94923; -.
DR ProteomicsDB; 50559; -.
DR Antibodypedia; 26368; 67 antibodies from 13 providers.
DR DNASU; 26035; -.
DR Ensembl; ENST00000261858.7; ENSP00000261858.2; ENSG00000138604.10.
DR GeneID; 26035; -.
DR KEGG; hsa:26035; -.
DR MANE-Select; ENST00000261858.7; ENSP00000261858.2; NM_015554.3; NP_056369.1.
DR UCSC; uc002ary.2; human.
DR CTD; 26035; -.
DR DisGeNET; 26035; -.
DR GeneCards; GLCE; -.
DR HGNC; HGNC:17855; GLCE.
DR HPA; ENSG00000138604; Tissue enhanced (brain).
DR MIM; 612134; gene.
DR neXtProt; NX_O94923; -.
DR OpenTargets; ENSG00000138604; -.
DR PharmGKB; PA145148750; -.
DR VEuPathDB; HostDB:ENSG00000138604; -.
DR eggNOG; KOG3760; Eukaryota.
DR GeneTree; ENSGT00390000006043; -.
DR InParanoid; O94923; -.
DR OMA; RGVFMYF; -.
DR OrthoDB; 561819at2759; -.
DR PhylomeDB; O94923; -.
DR TreeFam; TF105869; -.
DR BRENDA; 5.1.3.17; 2681.
DR PathwayCommons; O94923; -.
DR Reactome; R-HSA-2022928; HS-GAG biosynthesis.
DR SignaLink; O94923; -.
DR UniPathway; UPA00756; -.
DR UniPathway; UPA00862; -.
DR BioGRID-ORCS; 26035; 16 hits in 1043 CRISPR screens.
DR ChiTaRS; GLCE; human.
DR GeneWiki; GLCE; -.
DR GenomeRNAi; 26035; -.
DR Pharos; O94923; Tbio.
DR PRO; PR:O94923; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; O94923; protein.
DR Bgee; ENSG00000138604; Expressed in cerebellar hemisphere and 165 other tissues.
DR ExpressionAtlas; O94923; baseline and differential.
DR Genevisible; O94923; HS.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0047464; F:heparosan-N-sulfate-glucuronate 5-epimerase activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0016857; F:racemase and epimerase activity, acting on carbohydrates and derivatives; ISS:UniProtKB.
DR GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; IDA:UniProtKB.
DR GO; GO:0030210; P:heparin biosynthetic process; ISS:UniProtKB.
DR InterPro; IPR010598; C5-epim_C.
DR InterPro; IPR039721; C5-epimerase.
DR PANTHER; PTHR13174; PTHR13174; 1.
DR Pfam; PF06662; C5-epim_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Glycoprotein; Golgi apparatus; Isomerase; Membrane;
KW Metal-binding; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..617
FT /note="D-glucuronyl C5-epimerase"
FT /id="PRO_0000192645"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..28
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..617
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT BINDING 180
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:30872481,
FT ECO:0007744|PDB:6I01"
FT BINDING 185..187
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:30872481,
FT ECO:0007744|PDB:6I01"
FT BINDING 202
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:30872481,
FT ECO:0007744|PDB:6I01"
FT BINDING 210
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:30872481,
FT ECO:0007744|PDB:6I01"
FT BINDING 213
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:30872481,
FT ECO:0007744|PDB:6I02"
FT BINDING 216
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:30872481,
FT ECO:0007744|PDB:6I01"
FT BINDING 238
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:30872481,
FT ECO:0007744|PDB:6HZZ, ECO:0007744|PDB:6I01,
FT ECO:0007744|PDB:6I02"
FT BINDING 240
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:30872481,
FT ECO:0007744|PDB:6HZZ, ECO:0007744|PDB:6I01,
FT ECO:0007744|PDB:6I02"
FT BINDING 268
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:30872481,
FT ECO:0007744|PDB:6HZZ, ECO:0007744|PDB:6I01,
FT ECO:0007744|PDB:6I02"
FT BINDING 269
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:30872481,
FT ECO:0007744|PDB:6HZZ, ECO:0007744|PDB:6I01,
FT ECO:0007744|PDB:6I02"
FT BINDING 392
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:30872481,
FT ECO:0007744|PDB:6HZZ, ECO:0007744|PDB:6I01,
FT ECO:0007744|PDB:6I02"
FT BINDING 429..432
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:F1QR43"
FT BINDING 499..500
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:30872481,
FT ECO:0007744|PDB:6I01"
FT BINDING 510
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:30872481,
FT ECO:0007744|PDB:6I01"
FT BINDING 514
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:30872481,
FT ECO:0007744|PDB:6I01"
FT BINDING 560
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:30872481,
FT ECO:0007744|PDB:6I01"
FT BINDING 563
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:30872481,
FT ECO:0007744|PDB:6I01"
FT BINDING 572..581
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:30872481,
FT ECO:0007744|PDB:6I01"
FT SITE 180
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250|UniProtKB:F1QR43"
FT SITE 187
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250|UniProtKB:F1QR43"
FT SITE 560
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250|UniProtKB:F1QR43"
FT SITE 578
FT /note="Critical for catalysis"
FT /evidence="ECO:0000269|PubMed:30872481"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:30872481, ECO:0007744|PDB:6HZZ,
FT ECO:0007744|PDB:6I01, ECO:0007744|PDB:6I02"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:30872481,
FT ECO:0007744|PDB:6HZZ, ECO:0007744|PDB:6I01,
FT ECO:0007744|PDB:6I02"
FT CARBOHYD 393
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:30872481,
FT ECO:0007744|PDB:6HZZ, ECO:0007744|PDB:6I01,
FT ECO:0007744|PDB:6I02"
FT VARIANT 65
FT /note="M -> V (in dbSNP:rs12440300)"
FT /id="VAR_055837"
FT VARIANT 597
FT /note="V -> I (in dbSNP:rs3865014)"
FT /evidence="ECO:0000269|PubMed:10048485"
FT /id="VAR_057958"
FT MUTAGEN 146
FT /note="Y->A: Reduces enzyme activity by about 60%."
FT /evidence="ECO:0000269|PubMed:20118238"
FT MUTAGEN 162
FT /note="Y->A: Reduces enzyme activity by about 75%."
FT /evidence="ECO:0000269|PubMed:20118238"
FT MUTAGEN 168
FT /note="Y->A: Almost abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:20118238"
FT MUTAGEN 210
FT /note="Y->A: Reduces enzyme activity by about 30%."
FT /evidence="ECO:0000269|PubMed:20118238"
FT MUTAGEN 222
FT /note="Y->A: Almost abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:20118238"
FT MUTAGEN 499
FT /note="E->Q: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:30872481"
FT MUTAGEN 500
FT /note="Y->F: Mildly decreased enzyme activity."
FT /evidence="ECO:0000269|PubMed:30872481"
FT MUTAGEN 578
FT /note="Y->F: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:30872481"
FT STRAND 105..111
FT /evidence="ECO:0007829|PDB:6I01"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:6I01"
FT STRAND 115..122
FT /evidence="ECO:0007829|PDB:6I01"
FT STRAND 125..129
FT /evidence="ECO:0007829|PDB:6I01"
FT HELIX 130..137
FT /evidence="ECO:0007829|PDB:6I01"
FT STRAND 140..146
FT /evidence="ECO:0007829|PDB:6I01"
FT STRAND 149..156
FT /evidence="ECO:0007829|PDB:6I01"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:6I01"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:6I02"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:6I01"
FT TURN 193..195
FT /evidence="ECO:0007829|PDB:6I01"
FT STRAND 197..200
FT /evidence="ECO:0007829|PDB:6I01"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:6HZZ"
FT HELIX 211..227
FT /evidence="ECO:0007829|PDB:6I01"
FT STRAND 233..237
FT /evidence="ECO:0007829|PDB:6I01"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:6I01"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:6I02"
FT STRAND 257..263
FT /evidence="ECO:0007829|PDB:6I01"
FT TURN 264..267
FT /evidence="ECO:0007829|PDB:6I01"
FT STRAND 268..275
FT /evidence="ECO:0007829|PDB:6I01"
FT STRAND 282..290
FT /evidence="ECO:0007829|PDB:6I01"
FT STRAND 293..314
FT /evidence="ECO:0007829|PDB:6I01"
FT STRAND 318..326
FT /evidence="ECO:0007829|PDB:6I01"
FT STRAND 330..333
FT /evidence="ECO:0007829|PDB:6I01"
FT STRAND 336..340
FT /evidence="ECO:0007829|PDB:6I01"
FT STRAND 348..353
FT /evidence="ECO:0007829|PDB:6I01"
FT HELIX 354..362
FT /evidence="ECO:0007829|PDB:6I01"
FT STRAND 366..369
FT /evidence="ECO:0007829|PDB:6I01"
FT STRAND 377..398
FT /evidence="ECO:0007829|PDB:6I01"
FT HELIX 401..415
FT /evidence="ECO:0007829|PDB:6I01"
FT STRAND 439..441
FT /evidence="ECO:0007829|PDB:6HZZ"
FT HELIX 444..461
FT /evidence="ECO:0007829|PDB:6I01"
FT HELIX 464..472
FT /evidence="ECO:0007829|PDB:6I01"
FT HELIX 473..478
FT /evidence="ECO:0007829|PDB:6I01"
FT HELIX 481..483
FT /evidence="ECO:0007829|PDB:6I01"
FT STRAND 487..490
FT /evidence="ECO:0007829|PDB:6I01"
FT TURN 491..493
FT /evidence="ECO:0007829|PDB:6I01"
FT STRAND 494..497
FT /evidence="ECO:0007829|PDB:6I01"
FT HELIX 509..530
FT /evidence="ECO:0007829|PDB:6I01"
FT HELIX 532..548
FT /evidence="ECO:0007829|PDB:6I01"
FT HELIX 549..552
FT /evidence="ECO:0007829|PDB:6I01"
FT STRAND 555..560
FT /evidence="ECO:0007829|PDB:6I01"
FT HELIX 563..567
FT /evidence="ECO:0007829|PDB:6I01"
FT HELIX 576..589
FT /evidence="ECO:0007829|PDB:6I01"
FT TURN 590..592
FT /evidence="ECO:0007829|PDB:6I01"
FT HELIX 596..608
FT /evidence="ECO:0007829|PDB:6I01"
FT TURN 609..611
FT /evidence="ECO:0007829|PDB:6I01"
SQ SEQUENCE 617 AA; 70101 MW; 2F909A15FEA6DA05 CRC64;
MRCLAARVNY KTLIIICALF TLVTVLLWNK CSSDKAIQFP RRSSSGFRVD GFEKRAAASE
SNNYMNHVAK QQSEEAFPQE QQKAPPVVGG FNSNVGSKVL GLKYEEIDCL INDEHTIKGR
REGNEVFLPF TWVEKYFDVY GKVVQYDGYD RFEFSHSYSK VYAQRAPYHP DGVFMSFEGY
NVEVRDRVKC ISGVEGVPLS TQWGPQGYFY PIQIAQYGLS HYSKNLTEKP PHIEVYETAE
DRDKNKPNDW TVPKGCFMAN VADKSRFTNV KQFIAPETSE GVSLQLGNTK DFIISFDLKF
LTNGSVSVVL ETTEKNQLFT IHYVSNAQLI AFKERDIYYG IGPRTSWSTV TRDLVTDLRK
GVGLSNTKAV KPTKIMPKKV VRLIAKGKGF LDNITISTTA HMAAFFAASD WLVRNQDEKG
GWPIMVTRKL GEGFKSLEPG WYSAMAQGQA ISTLVRAYLL TKDHIFLNSA LRATAPYKFL
SEQHGVKAVF MNKHDWYEEY PTTPSSFVLN GFMYSLIGLY DLKETAGEKL GKEARSLYER
GMESLKAMLP LYDTGSGTIY DLRHFMLGIA PNLARWDYHT THINQLQLLS TIDESPVFKE
FVKRWKSYLK GSRAKHN
