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   27-MAR-2024, entry version 174.
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; 52.
DR   IntAct; O94923; 20.
DR   MINT; O94923; -.
DR   STRING; 9606.ENSP00000261858; -.
DR   GlyCosmos; O94923; 4 sites, 1 glycan.
DR   GlyGen; O94923; 6 sites, 2 O-linked glycans (3 sites).
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; 9606-ENSP00000261858; -.
DR   PeptideAtlas; O94923; -.
DR   ProteomicsDB; 50559; -.
DR   Pumba; O94923; -.
DR   Antibodypedia; 26368; 80 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   AGR; HGNC:17855; -.
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; 5392022at2759; -.
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 1123 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 166 other cell types or tissues.
DR   ExpressionAtlas; O94923; baseline and differential.
DR   GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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   GO; GO:0031345; P:negative regulation of cell projection organization; IEA:Ensembl.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR   GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; IEA:Ensembl.
DR   InterPro; IPR010598; C5-epim_C.
DR   InterPro; IPR039721; C5-epimerase.
DR   PANTHER; PTHR13174; D-GLUCURONYL C5-EPIMERASE; 1.
DR   PANTHER; PTHR13174:SF3; D-GLUCURONYL C5-EPIMERASE; 1.
DR   Pfam; PF06662; C5-epim_C; 1.
DR   Pfam; PF21174; Glce_b_sandwich; 1.
DR   Genevisible; O94923; HS.
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
//