EXT1C_DANRE
ID EXT1C_DANRE Reviewed; 737 AA.
AC Q5IGR6;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Exostosin-1c;
DE EC=2.4.1.224;
DE EC=2.4.1.225;
DE AltName: Full=Glucuronosyl-N-acetylglucosaminyl-proteoglycan/N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase 1c;
DE AltName: Full=Multiple exostoses protein 1 homolog c;
GN Name=ext1c;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX PubMed=15614771; DOI=10.1002/dvdy.20248;
RA Siekmann A.F., Brand M.;
RT "Distinct tissue-specificity of three zebrafish ext1 genes encoding
RT proteoglycan modifying enzymes and their relationship to somitic Sonic
RT hedgehog signaling.";
RL Dev. Dyn. 232:498-505(2005).
CC -!- FUNCTION: Glycosyltransferase required for the biosynthesis of heparan-
CC sulfate. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-{[(1->4)-beta-D-GlcA-(1->4)-alpha-D-GlcNAc](n)-(1->4)-
CC beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl}-L-
CC seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-{alpha-D-
CC GlcNAc-[(1->4)-beta-D-GlcA-(1->4)-alpha-D-GlcNAc](n)-(1->4)-beta-D-
CC GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl}-L-seryl-
CC [protein] + H(+) + UDP; Xref=Rhea:RHEA:16213, Rhea:RHEA-COMP:12621,
CC Rhea:RHEA-COMP:12623, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:132415, ChEBI:CHEBI:132416;
CC EC=2.4.1.224;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-{alpha-D-GlcNAc-[(1->4)-beta-D-GlcA-(1->4)-alpha-D-
CC GlcNAc](n)-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-
CC (1->4)-beta-D-Xyl}-L-seryl-[protein] + UDP-alpha-D-glucuronate = 3-
CC O-{[(1->4)-beta-D-GlcA-(1->4)-alpha-D-GlcNAc](n+1)-(1->4)-beta-D-
CC GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl}-L-seryl-
CC [protein] + H(+) + UDP; Xref=Rhea:RHEA:20908, Rhea:RHEA-COMP:12623,
CC Rhea:RHEA-COMP:14295, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:132415, ChEBI:CHEBI:132416;
CC EC=2.4.1.225;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q9ES89};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass type II membrane protein {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expressed zygotically. First detected at the
CC beginning of somatogenesis. At the 16-somite stage, restricted to
CC posterior adaxial cells and, in the anterior, to cells adjacent to the
CC neural tube and to ventromedial reigons of the somites. At 24 hours-
CC post-fertilization (hpf), expressed in the ventral rhombomeres,
CC telencephalon and olfactory bulbs. At 48 hpf, expressed in the brain,
CC retina and fin buds. {ECO:0000269|PubMed:15614771}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 47 family.
CC {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; AY734457; AAW29035.1; -; mRNA.
DR AlphaFoldDB; Q5IGR6; -.
DR SMR; Q5IGR6; -.
DR STRING; 7955.ENSDARP00000051693; -.
DR CAZy; GT47; Glycosyltransferase Family 47.
DR CAZy; GT64; Glycosyltransferase Family 64.
DR PaxDb; Q5IGR6; -.
DR ZFIN; ZDB-GENE-050211-5; ext1c.
DR eggNOG; KOG1021; Eukaryota.
DR InParanoid; Q5IGR6; -.
DR PhylomeDB; Q5IGR6; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q5IGR6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0008375; F:acetylglucosaminyltransferase activity; IBA:GO_Central.
DR GO; GO:0050508; F:glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity; ISS:UniProtKB.
DR GO; GO:0015020; F:glucuronosyltransferase activity; IBA:GO_Central.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050509; F:N-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR004263; Exostosin.
DR InterPro; IPR027670; Exostosin-1.
DR InterPro; IPR040911; Exostosin_GT47.
DR InterPro; IPR015338; GT64.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR11062; PTHR11062; 1.
DR PANTHER; PTHR11062:SF97; PTHR11062:SF97; 1.
DR Pfam; PF03016; Exostosin; 1.
DR Pfam; PF09258; Glyco_transf_64; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Glycosyltransferase;
KW Manganese; Membrane; Metal-binding; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..737
FT /note="Exostosin-1c"
FT /id="PRO_0000149661"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..27
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..737
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 645
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 510
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 536..540
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 556..558
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 558
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 586
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 641..645
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 679..692
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 643..695
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
SQ SEQUENCE 737 AA; 85389 MW; 349EB644FB7AADB4 CRC64;
MQARKKYVLL GLCTCCWILL YYWAGLQERL LGLITHRRGE VPRPWPDWLD RALLPNFAEQ
LDLQNGGGPG DSPRQRKQAW SSIYKDSRCR MDTCFDFGRC QTQSGFRVYI YPPEKGERVS
EGYRKILTSV SESRYYTSDP REACLFVLGI DTLDRDQLSQ QFVPNVDERI RGYPLWNDGR
NHVIFNLYSG TWPNYTEDLG FNVGQAILAK ASLNTEHFRP GFDISIPLFS KEHPQKGGKR
GWLVRNSVPP RRKYLLMFKG KRYLTGIGSD TRNALHHIHN GKDIVSLTTC RHGKDWEKHK
DARCDHDNQE YERFDYQELL HNSTFCLVPR GRRLGSFRFL ESLQAACIPV LLSNGWELPF
SDVIQWNQAV VEGDERLLLQ VPSTVRAVGI DRVLALRQQT QTLWDAYFSS VDKIVLTTLE
IIKDRVYSHI SRNKLMWNAL PGGLLVLPEF STHLAHYPFY YLHLGISPGL EFTAVIHATS
PLVSQSQPIM KLLQVVSKSK YCSQIIILWN SEKSPPQRSK WPPMPVPLTV TDGRRKTSSR
FLPHAAIETE AVLSLDEDTV LLTSEINFAF HVWRSFPDRI VGYPPRSHFW DPVKKAWGYT
SKWTNEYSII LTGAAFYHRY YHHLFSHYLP SSLRALVDHS CNCEDILMNF LVSSVAHLPP
VKVAQRKQYK EMPSLQGTKM APWANPEHFT QRQECVNTFS SWFGYMPLEH SQFRLDPVLF
KDHVSVLRKR YKDLERV
