GLCE_CAEEL
ID GLCE_CAEEL Reviewed; 616 AA.
AC P46555; Q6Q8P8;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=D-glucuronyl C5-epimerase;
DE EC=5.1.3.17 {ECO:0000250|UniProtKB:O94923};
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=hse-5; ORFNames=B0285.5;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND MUTAGENESIS OF GLY-610.
RX PubMed=15003172; DOI=10.1016/s0896-6273(04)00084-4;
RA Buelow H.E., Hobert O.;
RT "Differential sulfations and epimerization define heparan sulfate
RT specificity in nervous system development.";
RL Neuron 41:723-736(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26022293; DOI=10.1534/g3.115.018770;
RA Sundararajan L., Norris M.L., Lundquist E.A.;
RT "SDN-1/Syndecan acts in parallel to the transmembrane molecule MIG-13 to
RT promote anterior neuroblast migration.";
RL G3 (Bethesda) 5:1567-1574(2015).
CC -!- FUNCTION: Converts D-glucuronic acid residues adjacent to N-sulfate
CC sugar residues to L-iduronic acids (By similarity). Plays a role in the
CC early migration of AQR and PQR neurons, which descend from the Q
CC neuroblasts (PubMed:26022293). {ECO:0000250|UniProtKB:O94923,
CC ECO:0000269|PubMed:26022293}.
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:0000250|UniProtKB:O94923};
CC -!- PATHWAY: Glycan metabolism; heparan sulfate biosynthesis.
CC -!- PATHWAY: Glycan metabolism; heparin biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:F1QR43}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}. Secreted, extracellular space,
CC extracellular matrix, basement membrane.
CC -!- TISSUE SPECIFICITY: Expression in comma stage embryos is strong in the
CC hypodermis and intestine and weaker in the head region. In late
CC embryos, larval, and adult stages, expressed primarily in hypodermis
CC and intestine. {ECO:0000269|PubMed:15003172}.
CC -!- DISRUPTION PHENOTYPE: Irregular positioning of the AQR and PQR neurons
CC in larva at the L4 stage. {ECO:0000269|PubMed:26022293}.
CC -!- SIMILARITY: Belongs to the D-glucuronyl C5-epimerase family.
CC {ECO:0000305}.
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DR EMBL; AY552607; AAS89254.1; -; mRNA.
DR EMBL; Z34533; CAA84297.2; -; Genomic_DNA.
DR PIR; T18692; T18692.
DR RefSeq; NP_497876.2; NM_065475.5.
DR AlphaFoldDB; P46555; -.
DR SMR; P46555; -.
DR BioGRID; 40798; 1.
DR STRING; 6239.B0285.5; -.
DR EPD; P46555; -.
DR PaxDb; P46555; -.
DR PeptideAtlas; P46555; -.
DR EnsemblMetazoa; B0285.5.1; B0285.5.1; WBGene00002003.
DR EnsemblMetazoa; B0285.5.2; B0285.5.2; WBGene00002003.
DR EnsemblMetazoa; B0285.5.3; B0285.5.3; WBGene00002003.
DR GeneID; 175562; -.
DR KEGG; cel:CELE_B0285.5; -.
DR UCSC; B0285.5; c. elegans.
DR CTD; 175562; -.
DR WormBase; B0285.5; CE36681; WBGene00002003; hse-5.
DR eggNOG; KOG3760; Eukaryota.
DR GeneTree; ENSGT00390000006043; -.
DR HOGENOM; CLU_028636_0_0_1; -.
DR InParanoid; P46555; -.
DR OMA; RGVFMYF; -.
DR OrthoDB; 561819at2759; -.
DR PhylomeDB; P46555; -.
DR UniPathway; UPA00756; -.
DR UniPathway; UPA00862; -.
DR PRO; PR:P46555; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00002003; Expressed in embryo and 4 other tissues.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0047464; F:heparosan-N-sulfate-glucuronate 5-epimerase activity; IBA:GO_Central.
DR GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; IBA:GO_Central.
DR GO; GO:0015015; P:heparan sulfate proteoglycan biosynthetic process, enzymatic modification; IMP:WormBase.
DR GO; GO:0030210; P:heparin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:WormBase.
DR GO; GO:0030334; P:regulation of cell migration; IMP:WormBase.
DR InterPro; IPR010598; C5-epim_C.
DR InterPro; IPR039721; C5-epimerase.
DR PANTHER; PTHR13174; PTHR13174; 1.
DR Pfam; PF06662; C5-epim_C; 1.
PE 1: Evidence at protein level;
KW Basement membrane; Cell membrane; Extracellular matrix; Glycoprotein;
KW Isomerase; Membrane; Reference proteome; Secreted; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..616
FT /note="D-glucuronyl C5-epimerase"
FT /id="PRO_0000192647"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..29
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..616
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT BINDING 136
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:F1QR43"
FT BINDING 141..143
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:F1QR43"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:F1QR43"
FT BINDING 504
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:F1QR43"
FT BINDING 562
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:F1QR43"
FT BINDING 574..580
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:F1QR43"
FT SITE 136
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250|UniProtKB:F1QR43"
FT SITE 143
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250|UniProtKB:F1QR43"
FT SITE 559
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250|UniProtKB:F1QR43"
FT SITE 577
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250|UniProtKB:F1QR43"
FT CARBOHYD 188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 471
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 610
FT /note="G->E: In ot16; midline crossover defects of PVQL and
FT PVQR axons."
FT /evidence="ECO:0000269|PubMed:15003172"
SQ SEQUENCE 616 AA; 70055 MW; 301946860AB1CDE2 CRC64;
MKCLRWRSNR HRIYLLVACG ALFLLNRHLT QEESRIDEED EELTQVDVNE DDKKIECEPP
GSIESKCIAD NGKSMKCWKD EEDVYFPVSY LKKRFDMTGK LGKDGSTFEL YTSYAKMRSP
DSTYDPLGPF GHFSTYSVET RDRVRCVSAK TDVPMSTQWD PIPYYYPIQI SQYGLQHYSR
MKLDSISNKS EASPKDDVIL GVNSKEWKGA AGMHETTERL FFNDEQMGKV VNISAGAALA
NAGAYVYLDK SPDLHVISFD WKPYEANSSF TVLAKMKQDD LLVLINYVYS EGNGKCVWQE
EERISDDYIV QKPKKDGQVS YSYSYIGNSP IGEWSTVTRD LLVDVARALS SGDNRKKDDN
VVLHAGDLRL VSLGFRGELT VKQKITQRRE QHSHAFYAAA DWLVKNQNDR GGWSVPVERS
IAERKLVLPP GWHSAMAQGH GISVLTRAFK HFNDEKYLKS AAKALKLFKI NSSDGGVRGE
FFGNIWYEEY PTTPGSFVLN GFLYSLIGLY DLSQLELMID ENDETMRAKI QEAQELYSAG
VRSLKQLLPL YDTGSGTIYD LRHVALGTAP NLARWDYHAV HVYLLKWIAG IEKDEVLSKT
ADRWIGYAYG KRAKHN
