H6S1A_DANRE
ID H6S1A_DANRE Reviewed; 413 AA.
AC Q56UJ5; A0MGZ4; Q503W9;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Heparan-sulfate 6-O-sulfotransferase 1-A {ECO:0000250|UniProtKB:O60243};
DE Short=HS 6-OST-1A;
DE Short=HS6ST-1;
DE EC=2.8.2.- {ECO:0000250|UniProtKB:O60243};
GN Name=hs6st1a {ECO:0000250|UniProtKB:O60243}; Synonyms=hs6st1;
GN ORFNames=zgc:110038;
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], FUNCTION, DEVELOPMENTAL STAGE, AND TISSUE
RP SPECIFICITY.
RX PubMed=16009360; DOI=10.1016/j.ydbio.2005.05.032;
RA Chen E., Stringer S.E., Rusch M.A., Selleck S.B., Ekker S.C.;
RT "A unique role for 6-O sulfation modification in zebrafish vascular
RT development.";
RL Dev. Biol. 284:364-376(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Larva;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 9-413, DEVELOPMENTAL STAGE, AND TISSUE
RP SPECIFICITY.
RX PubMed=17075883; DOI=10.1002/dvdy.20990;
RA Cadwallader A.B., Yost H.J.;
RT "Combinatorial expression patterns of heparan sulfate sulfotransferases in
RT zebrafish: II. The 6-O-sulfotransferase family.";
RL Dev. Dyn. 235:3432-3437(2006).
CC -!- FUNCTION: 6-O-sulfation enzyme which catalyzes the transfer of sulfate
CC from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to position 6 of the
CC N-sulfoglucosamine residue (GlcNS) of heparan sulfate.
CC {ECO:0000269|PubMed:16009360}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + alpha-D-glucosaminyl-[heparan
CC sulfate](n) = 6-sulfo-alpha-D-glucosaminyl-[heparan sulfate](n) +
CC adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:56604, Rhea:RHEA-
CC COMP:9830, Rhea:RHEA-COMP:14621, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:58388,
CC ChEBI:CHEBI:140604; Evidence={ECO:0000250|UniProtKB:O60243};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: During somitogenesis, first expressed in polster
CC and presumptive forebrain. During mid-somitogenesis, expressed in eye,
CC hindbrain and anterior spinal cord. During late somitogenesis, strong
CC expression in eye and hindbrain, decreased levels in midbrain and
CC anterior spinal cord. At 24 hours post-fertilization (hpf), expressed
CC in neural retina and lens, brain and anterior spinal cord. At 36 hpf,
CC retinal expression is confined to the ciliary marginal zone and there
CC is strong expression in tectum, rhombomeres and otic vesicle. At 48
CC hpf, expressed in retinal ganglion cells and in tectum, rhombomeres and
CC pectoral fin. Not detected in the vasculature during embryogenesis.
CC {ECO:0000269|PubMed:16009360, ECO:0000269|PubMed:17075883}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Expression is lost before gastrulation and begins again during
CC somitogenesis. {ECO:0000269|PubMed:16009360,
CC ECO:0000269|PubMed:17075883}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 6 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH95149.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAT80869.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY575770; AAT80869.1; ALT_INIT; mRNA.
DR EMBL; BC095149; AAH95149.1; ALT_INIT; mRNA.
DR EMBL; DQ812993; ABH11455.1; -; mRNA.
DR RefSeq; NP_001018344.2; NM_001020508.2.
DR AlphaFoldDB; Q56UJ5; -.
DR SMR; Q56UJ5; -.
DR STRING; 7955.ENSDARP00000119653; -.
DR PaxDb; Q56UJ5; -.
DR PRIDE; Q56UJ5; -.
DR Ensembl; ENSDART00000189011; ENSDARP00000145279; ENSDARG00000054754.
DR GeneID; 553162; -.
DR KEGG; dre:553162; -.
DR CTD; 553162; -.
DR ZFIN; ZDB-GENE-050524-1; hs6st1a.
DR eggNOG; KOG3955; Eukaryota.
DR GeneTree; ENSGT00950000183071; -.
DR InParanoid; Q56UJ5; -.
DR OrthoDB; 1167623at2759; -.
DR PhylomeDB; Q56UJ5; -.
DR Reactome; R-DRE-2022928; HS-GAG biosynthesis.
DR PRO; PR:Q56UJ5; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 2.
DR Bgee; ENSDARG00000054754; Expressed in retina and 52 other tissues.
DR ExpressionAtlas; Q56UJ5; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0017095; F:heparan sulfate 6-O-sulfotransferase activity; IMP:ZFIN.
DR GO; GO:0015015; P:heparan sulfate proteoglycan biosynthetic process, enzymatic modification; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR010635; Heparan_SO4-6-sulfoTrfase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005331; Sulfotransferase.
DR PANTHER; PTHR12812; PTHR12812; 1.
DR Pfam; PF03567; Sulfotransfer_2; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Membrane; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..413
FT /note="Heparan-sulfate 6-O-sulfotransferase 1-A"
FT /id="PRO_0000190804"
FT TOPO_DOM 9..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..36
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..413
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 374..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..398
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 149
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 92..100
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 122..123
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 139
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 183
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 191
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 195
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 202
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 315..317
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 321..322
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 20
FT /note="V -> A (in Ref. 2; AAH95149)"
FT /evidence="ECO:0000305"
FT CONFLICT 79
FT /note="D -> H (in Ref. 3; ABH11455 and 2; AAH95149)"
FT /evidence="ECO:0000305"
FT CONFLICT 307
FT /note="R -> H (in Ref. 3; ABH11455 and 2; AAH95149)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="G -> D (in Ref. 2; AAH95149)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 413 AA; 48910 MW; B5A8195A0111BE32 CRC64;
MNLLTGRNMV ERSSKFLFIV VGSVLFMLIL YQYVAPGMMN FGSPHGYMLE DDADLFPTPD
PHYVKKFYFP IRDLERTVDF EIKGDDVIVF LHIQKTGGTT FGRHLVQNVR LEVPCDCRPG
QKKCTCYRPN RKETWLFSRF STGWSCGLHA DWTELTNCVP GVLNKKESRM KNQRKFYYIT
LLRDPVSRYL SEWRHVQRGA TWKTSLHMCD GRTPTPEELP PCYEGTDWSG CTLQQFMDCP
YNLANNRQVR MLADLSLVGC YNMSFIPEKK RAQVLLESAK KNLRDMAFFG LTEFQRKTQY
LFERTFRLKF IRPFMQYNST RAAGVDLDND TIQRIEELND LDMQLYDYAR DLFQQRYMYK
RQLERREQRL KNQPLFPFRR TSSSDSTFRD DAPESEGSRL PTEDYMNHII NRW
