EXT1A_DANRE
ID EXT1A_DANRE Reviewed; 730 AA.
AC Q5IGR8;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Exostosin-1a;
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 1a;
DE AltName: Full=Multiple exostoses protein 1 homolog a;
GN Name=ext1a;
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 neuroectoderm. At the 3-somite stage,
CC expressed in the prospective forebrain, hindbrain and tailbud. From the
CC 5-somite stage, expressed in the somitic mesoderm. At the 16-somite
CC stage, also expressed in the dorsal neural tube, the eye and the
CC Kupffer's vesicle. At 48 hours-post-fertilization (hpf), expression
CC continues in the dorsal diencephalon and cerebellum and is observed in
CC the otic vesicle. {ECO:0000269|PubMed:15614771}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 47 family.
CC {ECO:0000305}.
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DR EMBL; AY734455; AAW29033.1; -; mRNA.
DR AlphaFoldDB; Q5IGR8; -.
DR SMR; Q5IGR8; -.
DR STRING; 7955.ENSDARP00000003397; -.
DR CAZy; GT47; Glycosyltransferase Family 47.
DR CAZy; GT64; Glycosyltransferase Family 64.
DR PaxDb; Q5IGR8; -.
DR Ensembl; ENSDART00000159902; ENSDARP00000135521; ENSDARG00000103155.
DR ZFIN; ZDB-GENE-050211-3; ext1a.
DR eggNOG; KOG1021; Eukaryota.
DR GeneTree; ENSGT00940000155321; -.
DR InParanoid; Q5IGR8; -.
DR PhylomeDB; Q5IGR8; -.
DR TreeFam; TF314231; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q5IGR8; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 16.
DR Bgee; ENSDARG00000103155; Expressed in mature ovarian follicle and 39 other tissues.
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..730
FT /note="Exostosin-1a"
FT /id="PRO_0000149659"
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..730
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 638
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 502
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 528..533
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 549..551
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 551
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 579
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 634..638
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 672..685
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT CARBOHYD 314
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 636..688
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
SQ SEQUENCE 730 AA; 84618 MW; 6BBBF8923E42E49C CRC64;
MQAKKRYLIL FSAGVCLILL FYLQGPASRR TPKRGDDPHP HWPHFSDPLR AFIPWDQTET
EDYNVRASPR HKRDDSTGAD KCRMDSCFDF ELCKRNGFKV YVYPQQKGEK ISESYQNILS
SIEGSRFYTS DPGQACLFVL NLDTLDRDQL SPQYVHNLKT KIQNLNLWNN GRNHLIFNLY
SGTWPDYTED LGFDIGQAML AKASISTESF RPNFDISIPL FSKDHPRTGG ERGFLKYNTI
PPFRKYMLVF KGKRYLTGIG SDTRNALYHI HNAEDVVLLT TCKHGKDWQK HKDARCDKDN
AEYDRYDYKE MLHNSTFCLV PRGRRLGSFR FLEALQAACV PVMLSNGWEL PFSEIIDWRT
AAVIGDERLL LQIPSTVRSI HQDRILSLRQ QTQFLWEAYF SSVEKIVLTT LEIIQDRVLQ
HSAHSTLMWN RLPGGLFTLP QYSSYLGDFP FFYALLGIKP HQKFTAVIHA VTPLVSQSQP
IFKLLVAVAK SQFCAQIMVL WNCDKPLPSK HRWPATSVPV IVIEGESKVM SSRFLPYENI
ITDAVLSLDE DTVLSTTEVD FAFTVWQSFP ERIVGYPARS HFWDSNKERW GYTSKWTNDY
SMVLTGAAFY HRYYNYLYTH YLPGSLKGLV DQLSNCEDIL MNFLVSAVTK MPPIKVTQKK
QYKETMMGQT SRASRWADPD HFAQRQTCMN KFASWFGTMP LVHSQMRLDP VLFRDQVSIL
RKKYRDIERL
