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Protein

Dermatan-sulfate epimerase

Gene

Dse

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Converts D-glucuronic acid to L-iduronic acid (IdoUA) residues.

Catalytic activityi

Chondroitin D-glucuronate = dermatan L-iduronate.

Pathwayi: chondroitin sulfate biosynthesis

This protein is involved in the pathway chondroitin sulfate biosynthesis, which is part of Glycan metabolism.
View all proteins of this organism that are known to be involved in the pathway chondroitin sulfate biosynthesis and in Glycan metabolism.

Pathwayi: heparan sulfate biosynthesis

This protein is involved in the pathway heparan sulfate biosynthesis, which is part of Glycan metabolism.
View all proteins of this organism that are known to be involved in the pathway heparan sulfate biosynthesis and in Glycan metabolism.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Enzyme and pathway databases

BRENDAi5.1.3.19. 3474.
ReactomeiR-MMU-2022923. Dermatan sulfate biosynthesis.
UniPathwayiUPA00755.
UPA00756.

Names & Taxonomyi

Protein namesi
Recommended name:
Dermatan-sulfate epimerase (EC:5.1.3.19)
Short name:
DS epimerase
Alternative name(s):
Chondroitin-glucuronate 5-epimerase
Squamous cell carcinoma antigen recognized by T-cells 2
Short name:
SART-2
Gene namesi
Name:Dse
Synonyms:Sart2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:2443455. Dse.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei903 – 92321HelicalSequence analysisAdd
BLAST
Transmembranei934 – 95421HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence analysisAdd
BLAST
Chaini23 – 958936Dermatan-sulfate epimerasePRO_0000223312Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi642 – 6421N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ8BLI4.
PaxDbiQ8BLI4.
PeptideAtlasiQ8BLI4.
PRIDEiQ8BLI4.

PTM databases

iPTMnetiQ8BLI4.
PhosphoSiteiQ8BLI4.

Expressioni

Gene expression databases

BgeeiQ8BLI4.
CleanExiMM_DSE.
GenevisibleiQ8BLI4. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000040074.

Structurei

3D structure databases

ProteinModelPortaliQ8BLI4.
SMRiQ8BLI4. Positions 24-581.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the dermatan-sulfate isomerase family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IKEY. Eukaryota.
ENOG410ZW1M. LUCA.
GeneTreeiENSGT00390000006522.
HOGENOMiHOG000072706.
HOVERGENiHBG057715.
InParanoidiQ8BLI4.
KOiK01794.
OMAiWEGQVTE.
OrthoDBiEOG7RZ5P7.
PhylomeDBiQ8BLI4.
TreeFamiTF334118.

Family and domain databases

InterProiIPR008929. Chondroitin_lyas.
IPR032518. HepII_N.
[Graphical view]
PfamiPF16332. DUF4962. 1 hit.
[Graphical view]
SUPFAMiSSF48230. SSF48230. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8BLI4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRTHTRGAPS VFFICLLCCV SAFITDENPE VMIPFTNANY DSHPMLYFSR
60 70 80 90 100
KDVAELQLRA ASSHEHIAAR LTEAVHTMLT NPLEYLPPWD PKEYSARWNE
110 120 130 140 150
IYGNNLGALA MFCVLYPENT EARDMAKDYM ERMAAQPSWL VKDAPWDEVP
160 170 180 190 200
LAHSLVGFAT AYDFLYNYLS KTQQETFLEV IANASGYMYE TSYRRGWGFQ
210 220 230 240 250
YLHNHQPTNC MALLTGSLIL MNQGYLQEAY LWTKQVLSIM EKSLVLLREV
260 270 280 290 300
TDGSLYEGVA YGSYTTRSLF QYMFLVQRHF DINHFGHPWL KQHFAFMYRT
310 320 330 340 350
ILPGFQRTVA IADSNYNWFY GPESQLVFLD KFVMRNGSGN WLADQIRRNR
360 370 380 390 400
VVEGPGTPSK GQRWCTLHTE FLWYDASLKP VPPPDFGTPT LHYFEDWGVV
410 420 430 440 450
TYGSALPAEI NRSFLSFKSG KLGGRAIYDI VHRNKYKDWI KGWRNFNAGH
460 470 480 490 500
EHPDQNSFTF APNGVPFITE ALYGPKYTYF NNVLMFSPAV SKSCFSPWEG
510 520 530 540 550
QVTEDCSSKW SKYKHDLAAS CQGRVIAADE KDGVVFIRGE GVGAYNPMLN
560 570 580 590 600
LKHIQRNLIL LHPQLLLLVD QIHLGEESPL ETAASFFHNV DVPFEETVVD
610 620 630 640 650
GVHGALIRQR DGLYKMYWMD DTGYSEKANF ASVMYPRGYP YNGTNYVNVT
660 670 680 690 700
MHLRSPITRA AYLFIGPSVD VQSFSIHGDP QRLDVFIATS EHAYATYLWT
710 720 730 740 750
GENTGHSAFA QVIADHQKIL FDQSSAIKST AVPEVKDYAA IVEQNLQHFK
760 770 780 790 800
PVFQLLEKQI LSRVQNTASF RKTAERLLRF SDKRQTEEAI DRIFAISQQQ
810 820 830 840 850
RQQRGKSKKS RKAGKHYKFV DAVPDIFAQI EVNEKKIRQK AQVLAQREQP
860 870 880 890 900
IDEDEEMKDL LDFADVTYEK HKNEGSVKGG FGQVRMVTSH NRAPSLSASY
910 920 930 940 950
TRLFLILNIA IFFVMLAMQL TYFQRAQSLH GQRCLYAVLL IDSCVLLWLY

SSCSQSQC
Length:958
Mass (Da):109,755
Last modified:March 1, 2003 - v1
Checksum:i6C7D18A2F2BBBBE8
GO

Sequence cautioni

The sequence BAE31905.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti420 – 4201G → R in BAE31905 (PubMed:16141072).Curated
Sequence conflicti732 – 7321V → I in BAE31905 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK045065 mRNA. Translation: BAC32205.1.
AK153326 mRNA. Translation: BAE31905.1. Different initiation.
BC053095 mRNA. Translation: AAH53095.1.
CCDSiCCDS23776.1.
RefSeqiNP_766096.1. NM_172508.2.
XP_006512714.1. XM_006512651.2.
XP_011241458.1. XM_011243156.1.
UniGeneiMm.34557.

Genome annotation databases

EnsembliENSMUST00000048010; ENSMUSP00000040074; ENSMUSG00000039497.
GeneIDi212898.
KEGGimmu:212898.
UCSCiuc007eus.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK045065 mRNA. Translation: BAC32205.1.
AK153326 mRNA. Translation: BAE31905.1. Different initiation.
BC053095 mRNA. Translation: AAH53095.1.
CCDSiCCDS23776.1.
RefSeqiNP_766096.1. NM_172508.2.
XP_006512714.1. XM_006512651.2.
XP_011241458.1. XM_011243156.1.
UniGeneiMm.34557.

3D structure databases

ProteinModelPortaliQ8BLI4.
SMRiQ8BLI4. Positions 24-581.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000040074.

PTM databases

iPTMnetiQ8BLI4.
PhosphoSiteiQ8BLI4.

Proteomic databases

MaxQBiQ8BLI4.
PaxDbiQ8BLI4.
PeptideAtlasiQ8BLI4.
PRIDEiQ8BLI4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000048010; ENSMUSP00000040074; ENSMUSG00000039497.
GeneIDi212898.
KEGGimmu:212898.
UCSCiuc007eus.1. mouse.

Organism-specific databases

CTDi29940.
MGIiMGI:2443455. Dse.

Phylogenomic databases

eggNOGiENOG410IKEY. Eukaryota.
ENOG410ZW1M. LUCA.
GeneTreeiENSGT00390000006522.
HOGENOMiHOG000072706.
HOVERGENiHBG057715.
InParanoidiQ8BLI4.
KOiK01794.
OMAiWEGQVTE.
OrthoDBiEOG7RZ5P7.
PhylomeDBiQ8BLI4.
TreeFamiTF334118.

Enzyme and pathway databases

UniPathwayiUPA00755.
UPA00756.
BRENDAi5.1.3.19. 3474.
ReactomeiR-MMU-2022923. Dermatan sulfate biosynthesis.

Miscellaneous databases

ChiTaRSiDse. mouse.
PROiQ8BLI4.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BLI4.
CleanExiMM_DSE.
GenevisibleiQ8BLI4. MM.

Family and domain databases

InterProiIPR008929. Chondroitin_lyas.
IPR032518. HepII_N.
[Graphical view]
PfamiPF16332. DUF4962. 1 hit.
[Graphical view]
SUPFAMiSSF48230. SSF48230. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Bone marrow.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Brain.

Entry informationi

Entry nameiDSE_MOUSE
AccessioniPrimary (citable) accession number: Q8BLI4
Secondary accession number(s): Q3U620
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: March 1, 2003
Last modified: July 6, 2016
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.