DSE_BOVIN
ID DSE_BOVIN Reviewed; 958 AA.
AC P0C2H4;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Dermatan-sulfate epimerase;
DE Short=DS epimerase;
DE EC=5.1.3.19 {ECO:0000305|PubMed:16505484};
DE AltName: Full=Chondroitin-glucuronate 5-epimerase;
DE Flags: Precursor;
GN Name=DSE;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19390049; DOI=10.1126/science.1169588;
RG The bovine genome sequencing and analysis consortium;
RT "The genome sequence of taurine cattle: a window to ruminant biology and
RT evolution.";
RL Science 324:522-528(2009).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Spleen;
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).
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}.
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:0000305|PubMed:16505484};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q9UL01};
CC Note=Also has weak activity in the presence of Mg(2+) or Ca(2+) ions.
CC {ECO:0000250|UniProtKB:Q9UL01};
CC -!- PATHWAY: Glycan metabolism; chondroitin sulfate biosynthesis.
CC {ECO:0000305|PubMed:16505484}.
CC -!- PATHWAY: Glycan metabolism; heparan sulfate biosynthesis.
CC {ECO:0000305|PubMed:16505484}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:16505484}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9UL01}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q9UL01}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9UL01}. Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:Q9UL01}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9UL01}. Microsome membrane
CC {ECO:0000269|PubMed:16505484}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9UL01}.
CC -!- PTM: N-glycosylated. Glycosylation is important for enzymatic activity.
CC {ECO:0000250|UniProtKB:Q9UL01}.
CC -!- SIMILARITY: Belongs to the dermatan-sulfate isomerase family.
CC {ECO:0000305}.
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DR AlphaFoldDB; P0C2H4; -.
DR SMR; P0C2H4; -.
DR STRING; 9913.ENSBTAP00000006855; -.
DR PaxDb; P0C2H4; -.
DR PRIDE; P0C2H4; -.
DR eggNOG; ENOG502QPWZ; Eukaryota.
DR HOGENOM; CLU_308813_0_0_1; -.
DR InParanoid; P0C2H4; -.
DR OrthoDB; 588663at2759; -.
DR UniPathway; UPA00755; -.
DR UniPathway; UPA00756; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:HGNC-UCL.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISS:HGNC-UCL.
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: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: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 Cytoplasmic vesicle; Endoplasmic reticulum; Glycoprotein; Golgi apparatus;
KW Isomerase; Manganese; Membrane; Metal-binding; Microsome;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..958
FT /note="Dermatan-sulfate epimerase"
FT /id="PRO_0000278287"
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:0000250|UniProtKB:Q9UL01"
FT ACT_SITE 261
FT /evidence="ECO:0000250|UniProtKB:Q9UL01"
FT ACT_SITE 473
FT /evidence="ECO:0000250|UniProtKB:Q9UL01"
FT BINDING 452
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q9UL01"
FT BINDING 470
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q9UL01"
FT BINDING 481
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q9UL01"
FT SITE 450
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250|UniProtKB:Q9UL01"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 411
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 642
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 648
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 958 AA; 109725 MW; 9669205F61BE4AD1 CRC64;
MRTHTRGAPS VFFICLFCFV SACVTDENPE VMIPFTNANY DSHPMLYFSR AEVAELQLRA
ASSHEHIAAR LTEAVNTMLS SPLEYLPPWD PKEYSARWNE IYGNNLGALA MFCVLYPENM
EARDMAKDYM ERMAAQPSWL VKDAPWDEVP LAHSLVGFAT AYDFLYNYLS KTQQEKFLEV
IANASGYMYE TSYRRGWGFQ YLHNHQPTNC MALLTGSLVL MNQGYLQEAY LWTKQVLTIM
EKSLVLLREV TDGSLYEGVA YGSYTTRSLF QYMFLVQRHF DINHFGHPWL KQHFAFMYRT
ILPGFQRTVA IADSNYNWFY GPESQLVFLD KFVMRNGSGN WLADQIRRNR VVEGPGTPSK
GQRWCTLHTE FLWYDASLKS VPPPDFGTPT LHYFEDWGVV TYGSALPAEI NRSFLSFKSG
KLGGRAIYDI VHRNKYKDWI KGWRNFNAGH EHPDQNSFTF APNGVPFITE ALYGPKYTFF
NNVLMFSPAA SKSCFSPWEG QVTEDCSSKW SKYKHDPAAS CQGRVVAAVE KNGVVFIRGE
GVGAYNPQLH LRNVQRNLIL LHPQLLLLVD QIHLGEDSPL ERAASFFHNV DFPFEETVVD
GVHGALIRQR DGLYKMYWMD DTGYSEKGTF ASVTYPRGYP YNGTNYVNVT THLRSPVTRA
AYLFIGPSID VQSFSIHGDA QQLDVFVATS EHAYATYLWT GETAGQSAFA QVIADRQKIL
FDRSSAIRSS VVPEVKDYAA LVEQNLQHFK PVFQLLEKQI LSRVRNTASF RKTAERLLRF
SDKRQTEEAI DRIFAISQQQ QQQQSKSKKN RRGGKRYKFV DAVPDIFAQI EVNERKVRQK
AQILAQKELP VDEDEEMKDL LDFADITYEK HKNGDVMNGR FGQARMVTTH SRAPALSASY
TRLFLILNIA IFFVMLAMQL TYFQRAQSLH GQRCLYAVLL IDSCILLWLY SSCSQSQC
