EXT1B_DANRE
ID EXT1B_DANRE Reviewed; 741 AA.
AC Q5IGR7;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Exostosin-1b;
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 1b;
DE AltName: Full=Multiple exostoses protein 1 homolog b;
GN Name=ext1b;
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 both maternally and zygotically. During
CC gastrulation, expressed in the embryonic midline and in the involuting
CC mesendoderm of the germ ring. During somatogenesis, expressed in the
CC somitic mesoderm. At the 16-somite stage, expression is highest in the
CC tailbud region, the eye and the dorsal somites. At 24 hours-post-
CC fertilization (hpf), expressed in the neural tube, tailbud, posterior
CC somites and forming fin bud. At 48 hpf, expressed in the fin buds and
CC brain. {ECO:0000269|PubMed:15614771}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 47 family.
CC {ECO:0000305}.
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DR EMBL; AY734456; AAW29034.1; -; mRNA.
DR AlphaFoldDB; Q5IGR7; -.
DR SMR; Q5IGR7; -.
DR STRING; 7955.ENSDARP00000108198; -.
DR CAZy; GT47; Glycosyltransferase Family 47.
DR CAZy; GT64; Glycosyltransferase Family 64.
DR PaxDb; Q5IGR7; -.
DR ZFIN; ZDB-GENE-050211-4; ext1b.
DR eggNOG; KOG1021; Eukaryota.
DR InParanoid; Q5IGR7; -.
DR PhylomeDB; Q5IGR7; -.
DR Reactome; R-DRE-2022928; HS-GAG biosynthesis.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q5IGR7; -.
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..741
FT /note="Exostosin-1b"
FT /id="PRO_0000149660"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..28
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..741
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 649
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 513
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 539..544
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 560..562
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 562
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 590
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 645..649
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 683..696
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 647..699
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
SQ SEQUENCE 741 AA; 85121 MW; C2793E62F5378393 CRC64;
MQAKKRYLIS LLTGAFLVLL IYLGGGGVPG PAAPGSRSRT HGYNRPDQPW PHFSDPLQHF
SPWDHSDTED YNVHISPRQK RDVNSSVYKG KRCRMQSCFD FSLCQRNGFK VYVYPQQKGE
KISESYQNIL STIEGSRFYT SDPGQACVFV LSLDTLDRDQ LSPQYVHNLK TKVQSLALWN
NGRNHLIFNL YSGTWPDYTE DLGFDIGQAM LAKASISTEN FRPNFDISIP LFSKEHPRTG
GDRGYLKYNT IPPFRKYMLV FKGKRYLTGI GSDTRNALYH VHNAEDVVLL TTCKHGKDWQ
KHKDARCDKD NAEYDKYDYR EMLHNSTFCL VPRGRRLGSF RFLEALQAAC VPVMLSNGWE
LPFSEVIDWN TAAVIGDERL LLQIPSTVRS IHQDKILALR QQTQFLWEAY FSSVEKIVLT
TLEIIQDRVL QQSSRSSVMW NSHPGGLFSL PQYSSYLGDL PFFYAKLGIK PSPKFTAVIH
AVTPLVSQSQ PILKLIVSVA RSQYCAQIIV LWNCDKPLPA KQRWPATAVP IIVIEGENKV
MSSRFQPYES LISDAVLSLD EDTVLSTTEV DFAFTVWQSF PERIVGYPAR SHFWDNNKER
WGYTSKWTND YSMVLTGAAI YHRYYHFLYT HFLPSSLKSM VDQLANCEDI LMNFLVSAVT
KLPPVKVTQK KQYKETMMGQ SSRASRWADP DHFAQRQTCM NKFASWFGGM PLVHSQMRLD
PVLFKDQVSI LRKKYREIER L
