DSE_MOUSE
ID DSE_MOUSE Reviewed; 958 AA.
AC Q8BLI4; Q3U620;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Dermatan-sulfate epimerase;
DE Short=DS epimerase;
DE EC=5.1.3.19 {ECO:0000250|UniProtKB:Q9UL01};
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; 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).
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:0000250|UniProtKB:Q9UL01}.
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:0000250|UniProtKB:Q9UL01};
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:0000250|UniProtKB:Q9UL01}.
CC -!- PATHWAY: Glycan metabolism; heparan sulfate biosynthesis.
CC {ECO:0000250|UniProtKB:Q9UL01}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9UL01}; 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:0000250|UniProtKB:Q9UL01}; 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE31905.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK045065; BAC32205.1; -; mRNA.
DR EMBL; AK153326; BAE31905.1; ALT_INIT; mRNA.
DR EMBL; BC053095; AAH53095.1; -; mRNA.
DR CCDS; CCDS23776.1; -.
DR RefSeq; NP_766096.1; NM_172508.2.
DR RefSeq; XP_006512714.1; XM_006512651.3.
DR RefSeq; XP_011241458.1; XM_011243156.2.
DR AlphaFoldDB; Q8BLI4; -.
DR SMR; Q8BLI4; -.
DR BioGRID; 229367; 1.
DR STRING; 10090.ENSMUSP00000040074; -.
DR GlyGen; Q8BLI4; 5 sites.
DR iPTMnet; Q8BLI4; -.
DR PhosphoSitePlus; Q8BLI4; -.
DR EPD; Q8BLI4; -.
DR jPOST; Q8BLI4; -.
DR MaxQB; Q8BLI4; -.
DR PaxDb; Q8BLI4; -.
DR PeptideAtlas; Q8BLI4; -.
DR PRIDE; Q8BLI4; -.
DR ProteomicsDB; 277411; -.
DR DNASU; 212898; -.
DR Ensembl; ENSMUST00000048010; ENSMUSP00000040074; ENSMUSG00000039497.
DR GeneID; 212898; -.
DR KEGG; mmu:212898; -.
DR UCSC; uc007eus.1; mouse.
DR CTD; 29940; -.
DR MGI; MGI:2443455; Dse.
DR VEuPathDB; HostDB:ENSMUSG00000039497; -.
DR eggNOG; ENOG502QPWZ; Eukaryota.
DR GeneTree; ENSGT00390000006522; -.
DR HOGENOM; CLU_308813_0_0_1; -.
DR InParanoid; Q8BLI4; -.
DR OMA; EKMFAMS; -.
DR OrthoDB; 588663at2759; -.
DR PhylomeDB; Q8BLI4; -.
DR TreeFam; TF334118; -.
DR BRENDA; 5.1.3.19; 3474.
DR Reactome; R-MMU-2022923; Dermatan sulfate biosynthesis.
DR UniPathway; UPA00755; -.
DR UniPathway; UPA00756; -.
DR BioGRID-ORCS; 212898; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Dse; mouse.
DR PRO; PR:Q8BLI4; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8BLI4; protein.
DR Bgee; ENSMUSG00000039497; Expressed in manus and 206 other tissues.
DR ExpressionAtlas; Q8BLI4; baseline and differential.
DR Genevisible; Q8BLI4; MM.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
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; ISO:MGI.
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; ISO:MGI.
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 SUPFAM; SSF48230; SSF48230; 1.
PE 2: Evidence at transcript 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_0000223312"
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"
FT CONFLICT 420
FT /note="G -> R (in Ref. 1; BAE31905)"
FT /evidence="ECO:0000305"
FT CONFLICT 732
FT /note="V -> I (in Ref. 1; BAE31905)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 958 AA; 109755 MW; 6C7D18A2F2BBBBE8 CRC64;
MRTHTRGAPS VFFICLLCCV SAFITDENPE VMIPFTNANY DSHPMLYFSR KDVAELQLRA
ASSHEHIAAR LTEAVHTMLT NPLEYLPPWD PKEYSARWNE IYGNNLGALA MFCVLYPENT
EARDMAKDYM ERMAAQPSWL VKDAPWDEVP LAHSLVGFAT AYDFLYNYLS KTQQETFLEV
IANASGYMYE TSYRRGWGFQ YLHNHQPTNC MALLTGSLIL MNQGYLQEAY LWTKQVLSIM
EKSLVLLREV TDGSLYEGVA YGSYTTRSLF QYMFLVQRHF DINHFGHPWL KQHFAFMYRT
ILPGFQRTVA IADSNYNWFY GPESQLVFLD KFVMRNGSGN WLADQIRRNR VVEGPGTPSK
GQRWCTLHTE FLWYDASLKP VPPPDFGTPT LHYFEDWGVV TYGSALPAEI NRSFLSFKSG
KLGGRAIYDI VHRNKYKDWI KGWRNFNAGH EHPDQNSFTF APNGVPFITE ALYGPKYTYF
NNVLMFSPAV SKSCFSPWEG QVTEDCSSKW SKYKHDLAAS CQGRVIAADE KDGVVFIRGE
GVGAYNPMLN LKHIQRNLIL LHPQLLLLVD QIHLGEESPL ETAASFFHNV DVPFEETVVD
GVHGALIRQR DGLYKMYWMD DTGYSEKANF ASVMYPRGYP YNGTNYVNVT MHLRSPITRA
AYLFIGPSVD VQSFSIHGDP QRLDVFIATS EHAYATYLWT GENTGHSAFA QVIADHQKIL
FDQSSAIKST AVPEVKDYAA IVEQNLQHFK PVFQLLEKQI LSRVQNTASF RKTAERLLRF
SDKRQTEEAI DRIFAISQQQ RQQRGKSKKS RKAGKHYKFV DAVPDIFAQI EVNEKKIRQK
AQVLAQREQP IDEDEEMKDL LDFADVTYEK HKNEGSVKGG FGQVRMVTSH NRAPSLSASY
TRLFLILNIA IFFVMLAMQL TYFQRAQSLH GQRCLYAVLL IDSCVLLWLY SSCSQSQC
