DSE_HUMAN
ID DSE_HUMAN Reviewed; 958 AA.
AC Q9UL01; Q5R3K6;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Dermatan-sulfate epimerase;
DE Short=DS epimerase;
DE EC=5.1.3.19 {ECO:0000269|PubMed:16505484, ECO:0000269|PubMed:19004833, ECO:0000269|PubMed:7092807, ECO:0000269|Ref.7};
DE AltName: Full=Chondroitin-glucuronate 5-epimerase;
DE AltName: Full=Squamous cell carcinoma antigen recognized by T-cells 2;
DE Short=SART-2;
DE Flags: Precursor;
GN Name=DSE; Synonyms=SART2;
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], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10679095; DOI=10.4049/jimmunol.164.5.2565;
RA Nakao M., Shichijo S., Imaizumi T., Inoue Y., Matsunaga K., Yamada A.,
RA Kikuchi M., Tsuda N., Ohta K., Takamori S., Yamana H., Fujita H., Itoh K.;
RT "Identification of a gene coding for a new squamous cell carcinoma antigen
RT recognized by the CTL.";
RL J. Immunol. 164:2565-2574(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP PATHWAY, AND SUBCELLULAR LOCATION.
RX PubMed=7092807; DOI=10.1042/bj2010489;
RA Malmstroem A., Aberg L.;
RT "Biosynthesis of dermatan sulphate. Assay and properties of the uronosyl C-
RT 5 epimerase.";
RL Biochem. J. 201:489-493(1982).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=16505484; DOI=10.1074/jbc.m513373200;
RA Maccarana M., Olander B., Malmstroem J., Tiedemann K., Aebersold R.,
RA Lindahl U., Li J.-P., Malmstroem A.;
RT "Biosynthesis of dermatan sulfate: chondroitin-glucuronate C5-epimerase is
RT identical to SART2.";
RL J. Biol. Chem. 281:11560-11568(2006).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, ACTIVE SITE, GLYCOSYLATION AT
RP ASN-183; ASN-336; ASN-642 AND ASN-648, AND MUTAGENESIS OF HIS-203; HIS-205;
RP TYR-256; TYR-261; LYS-331 AND HIS-450.
RX PubMed=19004833; DOI=10.1074/jbc.m805479200;
RA Pacheco B., Maccarana M., Goodlett D.R., Malmstroem A., Malmstroem L.;
RT "Identification of the active site of DS-epimerase 1 and requirement of N-
RT glycosylation for enzyme function.";
RL J. Biol. Chem. 284:1741-1747(2009).
RN [7] {ECO:0007744|PDB:6HZN}
RP X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS) OF 23-775 IN COMPLEX WITH MANGANESE
RP IONS, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, ACTIVE SITE, GLYCOSYLATION AT
RP ASN-183; ASN-336; ASN-411; ASN-642 AND ASN-648, AND MUTAGENESIS OF TRP-98;
RP ASP-147; PRO-383; HIS-452; GLU-470 AND TYR-473.
RX DOI=10.1039/D0SC05971D;
RA Hasan M., Khakzad H., Happonen L., Sundin A., Unge J., Mueller U.,
RA Malmstrom J., Westergren-Thorsson G., Malmstrom L., Ellervik U.,
RA Malmstrom A., Tykesson E.;
RT "The structure of human dermatan sulfate epimerase 1 emphasizes the
RT importance of C5-epimerization of glucuronic acid in higher organisms.";
RL Chem. Sci. 11:0-0(2020).
RN [8]
RP VARIANT EDSMC2 LEU-268, AND CHARACTERIZATION OF VARIANT EDSMC2 LEU-268.
RX PubMed=23704329; DOI=10.1093/hmg/ddt227;
RA Mueller T., Mizumoto S., Suresh I., Komatsu Y., Vodopiutz J., Dundar M.,
RA Straub V., Lingenhel A., Melmer A., Lechner S., Zschocke J., Sugahara K.,
RA Janecke A.R.;
RT "Loss of dermatan sulfate epimerase (DSE) function results in
RT musculocontractural Ehlers-Danlos syndrome.";
RL Hum. Mol. Genet. 22:3761-3772(2013).
CC -!- FUNCTION: Converts D-glucuronic acid to L-iduronic acid (IdoUA)
CC residues. Plays an important role in the biosynthesis of the
CC glycosaminoglycan/mucopolysaccharide dermatan sulfate.
CC {ECO:0000269|PubMed:16505484, ECO:0000269|PubMed:19004833,
CC ECO:0000269|PubMed:7092807, ECO:0000269|Ref.7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chondroitin 4'-sulfate = dermatan 4'-sulfate;
CC Xref=Rhea:RHEA:21084, Rhea:RHEA-COMP:9829, Rhea:RHEA-COMP:9965,
CC ChEBI:CHEBI:58422, ChEBI:CHEBI:58465; EC=5.1.3.19;
CC Evidence={ECO:0000269|PubMed:16505484, ECO:0000269|PubMed:19004833,
CC ECO:0000269|PubMed:7092807, ECO:0000269|Ref.7};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:7092807};
CC Note=Also has weak activity in the presence of Mg(2+) or Ca(2+) ions.
CC {ECO:0000269|PubMed:7092807};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.12 mM for chondroitin {ECO:0000269|PubMed:7092807};
CC pH dependence:
CC Optimum pH is 5.5. {ECO:0000269|PubMed:7092807};
CC -!- PATHWAY: Glycan metabolism; chondroitin sulfate biosynthesis.
CC {ECO:0000305|PubMed:16505484, ECO:0000305|PubMed:19004833,
CC ECO:0000305|PubMed:7092807, ECO:0000305|Ref.7}.
CC -!- PATHWAY: Glycan metabolism; heparan sulfate biosynthesis.
CC {ECO:0000305|PubMed:16505484, ECO:0000305|PubMed:19004833,
CC ECO:0000305|PubMed:7092807, ECO:0000305|Ref.7}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:10679095, ECO:0000305|PubMed:7092807}; Multi-pass
CC membrane protein {ECO:0000305}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:10679095}; Multi-pass membrane protein
CC {ECO:0000305}. Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:10679095}; Multi-pass membrane protein
CC {ECO:0000305}. Microsome membrane {ECO:0000269|PubMed:7092807}; Multi-
CC pass membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with higher expression in
CC kidney and ovary and lower expression in brain, colon and thymus. Also
CC expressed in renal cell carcinomas, brain tumors, and in a part of
CC melanomas and adenocarcinomas from organs other than the breast.
CC Expressed in squamous cell carcinomas (SCC), glioma, and some
CC adenocarcinoma cell lines, but not in breast cancer cell lines or any
CC normal tissues (at protein level). {ECO:0000269|PubMed:10679095}.
CC -!- PTM: N-glycosylated (PubMed:19004833, Ref.7). Glycosylation is
CC important for enzymatic activity (PubMed:19004833).
CC {ECO:0000269|PubMed:19004833, ECO:0000269|Ref.7}.
CC -!- DISEASE: Ehlers-Danlos syndrome, musculocontractural type 2 (EDSMC2)
CC [MIM:615539]: A form of Ehlers-Danlos syndrome characterized by
CC progressive multisystem manifestations, including joint dislocations
CC and deformities, skin hyperextensibility, skin bruisability and
CC fragility with recurrent large subcutaneous hematomas, cardiac
CC valvular, respiratory, gastrointestinal, and ophthalmologic
CC complications. Motor developmental delay is associated with muscle
CC hypoplasia, muscle weakness, and an abnormal muscle fiber pattern in
CC histology in adulthood. {ECO:0000269|PubMed:23704329}. Note=The disease
CC is caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the dermatan-sulfate isomerase family.
CC {ECO:0000305}.
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DR EMBL; AF098066; AAF00087.1; -; mRNA.
DR EMBL; Z84488; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC039245; AAH39245.1; -; mRNA.
DR CCDS; CCDS5107.1; -.
DR RefSeq; NP_001074445.1; NM_001080976.2.
DR RefSeq; NP_001309866.1; NM_001322937.1.
DR RefSeq; NP_001309867.1; NM_001322938.1.
DR RefSeq; NP_001309868.1; NM_001322939.1.
DR RefSeq; NP_001309869.1; NM_001322940.1.
DR RefSeq; NP_001309870.1; NM_001322941.1.
DR RefSeq; NP_001309872.1; NM_001322943.1.
DR RefSeq; NP_001309873.1; NM_001322944.1.
DR RefSeq; NP_037484.1; NM_013352.3.
DR RefSeq; XP_016866285.1; XM_017010796.1.
DR PDB; 6HZN; X-ray; 2.41 A; A=23-775.
DR PDBsum; 6HZN; -.
DR AlphaFoldDB; Q9UL01; -.
DR SMR; Q9UL01; -.
DR BioGRID; 118977; 33.
DR IntAct; Q9UL01; 11.
DR MINT; Q9UL01; -.
DR STRING; 9606.ENSP00000332151; -.
DR GlyGen; Q9UL01; 5 sites.
DR iPTMnet; Q9UL01; -.
DR PhosphoSitePlus; Q9UL01; -.
DR BioMuta; DSE; -.
DR DMDM; 74762778; -.
DR EPD; Q9UL01; -.
DR jPOST; Q9UL01; -.
DR MassIVE; Q9UL01; -.
DR MaxQB; Q9UL01; -.
DR PaxDb; Q9UL01; -.
DR PeptideAtlas; Q9UL01; -.
DR PRIDE; Q9UL01; -.
DR ProteomicsDB; 84921; -.
DR Antibodypedia; 3106; 88 antibodies from 20 providers.
DR DNASU; 29940; -.
DR Ensembl; ENST00000331677.7; ENSP00000332151.2; ENSG00000111817.19.
DR Ensembl; ENST00000452085.7; ENSP00000404049.2; ENSG00000111817.19.
DR Ensembl; ENST00000644252.3; ENSP00000494147.2; ENSG00000111817.19.
DR GeneID; 29940; -.
DR KEGG; hsa:29940; -.
DR MANE-Select; ENST00000644252.3; ENSP00000494147.2; NM_013352.4; NP_037484.1.
DR UCSC; uc003pws.5; human.
DR CTD; 29940; -.
DR DisGeNET; 29940; -.
DR GeneCards; DSE; -.
DR HGNC; HGNC:21144; DSE.
DR HPA; ENSG00000111817; Low tissue specificity.
DR MalaCards; DSE; -.
DR MIM; 605942; gene.
DR MIM; 615539; phenotype.
DR neXtProt; NX_Q9UL01; -.
DR OpenTargets; ENSG00000111817; -.
DR Orphanet; 2953; Musculocontractural Ehlers-Danlos syndrome.
DR PharmGKB; PA162384080; -.
DR VEuPathDB; HostDB:ENSG00000111817; -.
DR eggNOG; ENOG502QPWZ; Eukaryota.
DR GeneTree; ENSGT00390000006522; -.
DR HOGENOM; CLU_308813_0_0_1; -.
DR InParanoid; Q9UL01; -.
DR OMA; EKMFAMS; -.
DR OrthoDB; 588663at2759; -.
DR PhylomeDB; Q9UL01; -.
DR TreeFam; TF334118; -.
DR BioCyc; MetaCyc:HS03472-MON; -.
DR BRENDA; 5.1.3.19; 2681.
DR PathwayCommons; Q9UL01; -.
DR Reactome; R-HSA-2022923; Dermatan sulfate biosynthesis.
DR SignaLink; Q9UL01; -.
DR UniPathway; UPA00755; -.
DR UniPathway; UPA00756; -.
DR BioGRID-ORCS; 29940; 10 hits in 1071 CRISPR screens.
DR ChiTaRS; DSE; human.
DR GeneWiki; DSE_(gene); -.
DR GenomeRNAi; 29940; -.
DR Pharos; Q9UL01; Tbio.
DR PRO; PR:Q9UL01; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9UL01; protein.
DR Bgee; ENSG00000111817; Expressed in parietal pleura and 196 other tissues.
DR ExpressionAtlas; Q9UL01; baseline and differential.
DR Genevisible; Q9UL01; HS.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HGNC-UCL.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HGNC-UCL.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0047757; F:chondroitin-glucuronate 5-epimerase activity; IDA:HGNC-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030206; P:chondroitin sulfate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0030204; P:chondroitin sulfate metabolic process; IBA:GO_Central.
DR GO; GO:0030208; P:dermatan sulfate biosynthetic process; IDA:UniProtKB.
DR GO; GO:0030205; P:dermatan sulfate metabolic process; IBA:GO_Central.
DR GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.50.10.100; -; 1.
DR InterPro; IPR008929; Chondroitin_lyas.
DR InterPro; IPR032518; HepII_N.
DR Pfam; PF16332; DUF4962; 1.
DR SUPFAM; SSF48230; SSF48230; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasmic vesicle; Disease variant; Ehlers-Danlos syndrome;
KW Endoplasmic reticulum; Glycoprotein; Golgi apparatus; Isomerase; Manganese;
KW Membrane; Metal-binding; Microsome; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..958
FT /note="Dermatan-sulfate epimerase"
FT /id="PRO_0000223311"
FT TOPO_DOM 23..902
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 903..923
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 924..933
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 934..954
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 955..958
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT ACT_SITE 205
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:19004833, ECO:0000269|Ref.7"
FT ACT_SITE 261
FT /evidence="ECO:0000269|PubMed:19004833, ECO:0000269|Ref.7"
FT ACT_SITE 473
FT /evidence="ECO:0000269|PubMed:19004833, ECO:0000269|Ref.7"
FT BINDING 452
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PDB:6HZN"
FT BINDING 470
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PDB:6HZN"
FT BINDING 481
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PDB:6HZN"
FT SITE 450
FT /note="Critical for catalysis"
FT /evidence="ECO:0000269|PubMed:19004833"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:19004833, ECO:0000269|Ref.7,
FT ECO:0007744|PDB:6HZN"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000269|PubMed:19004833, ECO:0000269|Ref.7,
FT ECO:0007744|PDB:6HZN"
FT CARBOHYD 411
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PDB:6HZN"
FT CARBOHYD 642
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:19004833, ECO:0000269|Ref.7,
FT ECO:0007744|PDB:6HZN"
FT CARBOHYD 648
FT /note="N-linked (GlcNAc...) (paucimannose) asparagine"
FT /evidence="ECO:0000269|PubMed:19004833, ECO:0000269|Ref.7,
FT ECO:0007744|PDB:6HZN"
FT VARIANT 25
FT /note="T -> I (in dbSNP:rs10485183)"
FT /id="VAR_034481"
FT VARIANT 34
FT /note="P -> L (in dbSNP:rs35548455)"
FT /id="VAR_053833"
FT VARIANT 268
FT /note="S -> L (in EDSMC2; shows a loss of epimerase
FT activity towards partially desulfated dermatan sulfate;
FT patient-derived fibroblasts show also a significant
FT reduction in activity; dbSNP:rs398122361)"
FT /evidence="ECO:0000269|PubMed:23704329"
FT /id="VAR_070911"
FT VARIANT 282
FT /note="I -> V (in dbSNP:rs34994230)"
FT /id="VAR_053834"
FT MUTAGEN 98
FT /note="W->A: Severely impairs catalytic activity."
FT /evidence="ECO:0000269|Ref.7"
FT MUTAGEN 147
FT /note="D->A: Impairs catalytic activity."
FT /evidence="ECO:0000269|Ref.7"
FT MUTAGEN 203
FT /note="H->A,N: Severely impairs catalytic activity."
FT /evidence="ECO:0000269|PubMed:19004833"
FT MUTAGEN 205
FT /note="H->A,N: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:19004833"
FT MUTAGEN 256
FT /note="Y->A: Moderately reduced catalytic activity."
FT /evidence="ECO:0000269|PubMed:19004833"
FT MUTAGEN 261
FT /note="Y->A,F: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:19004833"
FT MUTAGEN 331
FT /note="K->A: No significant effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:19004833"
FT MUTAGEN 383
FT /note="P->A: Very low levels of protein expression and no
FT detectable catalytic activity."
FT /evidence="ECO:0000269|Ref.7"
FT MUTAGEN 450
FT /note="H->A,N: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:19004833"
FT MUTAGEN 452
FT /note="H->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|Ref.7"
FT MUTAGEN 470
FT /note="E->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|Ref.7"
FT MUTAGEN 473
FT /note="Y->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|Ref.7"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:6HZN"
FT HELIX 53..61
FT /evidence="ECO:0007829|PDB:6HZN"
FT HELIX 65..80
FT /evidence="ECO:0007829|PDB:6HZN"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:6HZN"
FT HELIX 91..94
FT /evidence="ECO:0007829|PDB:6HZN"
FT HELIX 101..115
FT /evidence="ECO:0007829|PDB:6HZN"
FT HELIX 120..134
FT /evidence="ECO:0007829|PDB:6HZN"
FT HELIX 149..165
FT /evidence="ECO:0007829|PDB:6HZN"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:6HZN"
FT HELIX 171..191
FT /evidence="ECO:0007829|PDB:6HZN"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:6HZN"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:6HZN"
FT HELIX 205..222
FT /evidence="ECO:0007829|PDB:6HZN"
FT HELIX 226..247
FT /evidence="ECO:0007829|PDB:6HZN"
FT HELIX 258..280
FT /evidence="ECO:0007829|PDB:6HZN"
FT HELIX 288..298
FT /evidence="ECO:0007829|PDB:6HZN"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:6HZN"
FT HELIX 323..332
FT /evidence="ECO:0007829|PDB:6HZN"
FT HELIX 338..349
FT /evidence="ECO:0007829|PDB:6HZN"
FT STRAND 352..354
FT /evidence="ECO:0007829|PDB:6HZN"
FT TURN 360..366
FT /evidence="ECO:0007829|PDB:6HZN"
FT HELIX 367..373
FT /evidence="ECO:0007829|PDB:6HZN"
FT TURN 384..387
FT /evidence="ECO:0007829|PDB:6HZN"
FT STRAND 391..394
FT /evidence="ECO:0007829|PDB:6HZN"
FT TURN 395..398
FT /evidence="ECO:0007829|PDB:6HZN"
FT STRAND 399..403
FT /evidence="ECO:0007829|PDB:6HZN"
FT STRAND 414..418
FT /evidence="ECO:0007829|PDB:6HZN"
FT HELIX 424..432
FT /evidence="ECO:0007829|PDB:6HZN"
FT TURN 437..439
FT /evidence="ECO:0007829|PDB:6HZN"
FT HELIX 442..445
FT /evidence="ECO:0007829|PDB:6HZN"
FT STRAND 457..461
FT /evidence="ECO:0007829|PDB:6HZN"
FT HELIX 462..464
FT /evidence="ECO:0007829|PDB:6HZN"
FT HELIX 478..480
FT /evidence="ECO:0007829|PDB:6HZN"
FT STRAND 484..488
FT /evidence="ECO:0007829|PDB:6HZN"
FT HELIX 515..518
FT /evidence="ECO:0007829|PDB:6HZN"
FT STRAND 524..531
FT /evidence="ECO:0007829|PDB:6HZN"
FT STRAND 534..540
FT /evidence="ECO:0007829|PDB:6HZN"
FT HELIX 542..544
FT /evidence="ECO:0007829|PDB:6HZN"
FT HELIX 547..549
FT /evidence="ECO:0007829|PDB:6HZN"
FT STRAND 551..562
FT /evidence="ECO:0007829|PDB:6HZN"
FT STRAND 565..574
FT /evidence="ECO:0007829|PDB:6HZN"
FT STRAND 582..592
FT /evidence="ECO:0007829|PDB:6HZN"
FT STRAND 595..599
FT /evidence="ECO:0007829|PDB:6HZN"
FT STRAND 602..609
FT /evidence="ECO:0007829|PDB:6HZN"
FT STRAND 612..620
FT /evidence="ECO:0007829|PDB:6HZN"
FT STRAND 629..633
FT /evidence="ECO:0007829|PDB:6HZN"
FT STRAND 639..641
FT /evidence="ECO:0007829|PDB:6HZN"
FT STRAND 644..652
FT /evidence="ECO:0007829|PDB:6HZN"
FT STRAND 655..665
FT /evidence="ECO:0007829|PDB:6HZN"
FT STRAND 671..678
FT /evidence="ECO:0007829|PDB:6HZN"
FT STRAND 680..691
FT /evidence="ECO:0007829|PDB:6HZN"
FT STRAND 693..701
FT /evidence="ECO:0007829|PDB:6HZN"
FT STRAND 704..707
FT /evidence="ECO:0007829|PDB:6HZN"
FT STRAND 709..713
FT /evidence="ECO:0007829|PDB:6HZN"
FT STRAND 718..721
FT /evidence="ECO:0007829|PDB:6HZN"
FT HELIX 723..725
FT /evidence="ECO:0007829|PDB:6HZN"
FT HELIX 738..746
FT /evidence="ECO:0007829|PDB:6HZN"
FT HELIX 750..765
FT /evidence="ECO:0007829|PDB:6HZN"
SQ SEQUENCE 958 AA; 109773 MW; A3D05C6194B4D2F9 CRC64;
MRTHTRGAPS VFFIYLLCFV SAYITDENPE VMIPFTNANY DSHPMLYFSR AEVAELQLRA
ASSHEHIAAR LTEAVHTMLS SPLEYLPPWD PKDYSARWNE IFGNNLGALA MFCVLYPENI
EARDMAKDYM ERMAAQPSWL VKDAPWDEVP LAHSLVGFAT AYDFLYNYLS KTQQEKFLEV
IANASGYMYE TSYRRGWGFQ YLHNHQPTNC MALLTGSLVL MNQGYLQEAY LWTKQVLTIM
EKSLVLLREV TDGSLYEGVA YGSYTTRSLF QYMFLVQRHF NINHFGHPWL KQHFAFMYRT
ILPGFQRTVA IADSNYNWFY GPESQLVFLD KFVMRNGSGN WLADQIRRNR VVEGPGTPSK
GQRWCTLHTE FLWYDGSLKS VPPPDFGTPT LHYFEDWGVV TYGSALPAEI NRSFLSFKSG
KLGGRAIYDI VHRNKYKDWI KGWRNFNAGH EHPDQNSFTF APNGVPFITE ALYGPKYTFF
NNVLMFSPAV SKSCFSPWVG QVTEDCSSKW SKYKHDLAAS CQGRVVAAEE KNGVVFIRGE
GVGAYNPQLN LKNVQRNLIL LHPQLLLLVD QIHLGEESPL ETAASFFHNV DVPFEETVVD
GVHGAFIRQR DGLYKMYWMD DTGYSEKATF ASVTYPRGYP YNGTNYVNVT MHLRSPITRA
AYLFIGPSID VQSFTVHGDS QQLDVFIATS KHAYATYLWT GEATGQSAFA QVIADRHKIL
FDRNSAIKSS IVPEVKDYAA IVEQNLQHFK PVFQLLEKQI LSRVRNTASF RKTAERLLRF
SDKRQTEEAI DRIFAISQQQ QQQSKSKKNR RAGKRYKFVD AVPDIFAQIE VNEKKIRQKA
QILAQKELPI DEDEEMKDLL DFADVTYEKH KNGGLIKGRF GQARMVTTTH SRAPSLSASY
TRLFLILNIA IFFVMLAMQL TYFQRAQSLH GQRCLYAVLL IDSCILLWLY SSCSQSQC
