H6S1B_DANRE
ID H6S1B_DANRE Reviewed; 407 AA.
AC A0MGZ5;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 3.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Heparan-sulfate 6-O-sulfotransferase 1-B {ECO:0000250|UniProtKB:O60243};
DE Short=HS 6-OST-1B;
DE EC=2.8.2.- {ECO:0000250|UniProtKB:Q91ZB4};
GN Name=hs6st1b {ECO:0000312|ZFIN:ZDB-GENE-070103-2};
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] {ECO:0000305, ECO:0000312|EMBL:ABH11456.1}
RP NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND TISSUE 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:0000250|UniProtKB:Q91ZB4}.
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:Q91ZB4};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type II
CC membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: During early somitogenesis, first expressed in
CC floor plate and somites. During mid-somitogenesis, expressed strongly
CC in somites and more weakly in eye and hindbrain. During late
CC somitogenesis, expressed in eye, hindbrain and posterior somites. At 24
CC hours post-fertilization (hpf), expressed in lens, forebrain,
CC hindbrain, otic vesicle, anterior spinal cord neurons and posterior
CC somites. At 36 hpf, expressed in the retinal ciliary marginal zone,
CC brain, pancreas and weakly in pectoral fin. At 48 hpf, expressed in the
CC retinal ciliary marginal zone, retinal ganglion cells, rhombomeres,
CC otic vesicle and weakly in pectoral fin. {ECO:0000269|PubMed:17075883}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Expression is lost before gastrulation and begins again during early
CC somitogenesis. {ECO:0000269|PubMed:17075883}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 6 family. {ECO:0000255}.
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DR EMBL; DQ812994; ABH11456.1; -; mRNA.
DR RefSeq; NP_001073672.1; NM_001080203.1.
DR AlphaFoldDB; A0MGZ5; -.
DR SMR; A0MGZ5; -.
DR STRING; 7955.ENSDARP00000096556; -.
DR PaxDb; A0MGZ5; -.
DR PRIDE; A0MGZ5; -.
DR Ensembl; ENSDART00000105778; ENSDARP00000096556; ENSDARG00000071501.
DR Ensembl; ENSDART00000180982; ENSDARP00000153923; ENSDARG00000116688.
DR GeneID; 791107; -.
DR KEGG; dre:791107; -.
DR CTD; 791107; -.
DR ZFIN; ZDB-GENE-070103-2; hs6st1b.
DR eggNOG; KOG3955; Eukaryota.
DR GeneTree; ENSGT00950000183071; -.
DR HOGENOM; CLU_027877_1_0_1; -.
DR InParanoid; A0MGZ5; -.
DR OMA; XAEGERA; -.
DR OrthoDB; 1167623at2759; -.
DR PhylomeDB; A0MGZ5; -.
DR TreeFam; TF312835; -.
DR PRO; PR:A0MGZ5; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 24.
DR Bgee; ENSDARG00000071501; Expressed in mature ovarian follicle and 22 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0017095; F:heparan sulfate 6-O-sulfotransferase activity; IBA:GO_Central.
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..407
FT /note="Heparan-sulfate 6-O-sulfotransferase 1-B"
FT /id="PRO_0000283819"
FT TOPO_DOM 8..14
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 15..35
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..407
FT /note="Lumenal"
FT /evidence="ECO:0000255"
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"
SQ SEQUENCE 407 AA; 47878 MW; DB1134529F617EB2 CRC64;
MNDTERNMVE RTSKFLLIVV GSVFFMLILY QYVAPGVINF GSPHGYLLGE EDMTIFPTPD
PHYVKKYYFP IKDLERKIDF EIKGEDVIVF LHIQKTGGTT FGRHLVQNVR LELPCDCRPG
QKKCTCYRPN RKETWLFSRF STGWSCGLHA DWTELTNCVP GVLNKRESKS KKMRKFYYIT
LLRDPVSRYL SEWRHVQRGA TWKTSLHMCD GRTPTPEELP PCYEGTDWSG CTLQQFMDCP
YNLANNRQVR MLADLSLVGC YNLSTVPEKR RSQLLLESAK KNLRDMAFYG LTEFQRKTQY
LFERTFHLKF IRPFMQYNST RAAGVDLDND TIQRIEELND LDMKLYDYAK DLFQQRYQYK
HMLDRREQRL LRGHASFHSP FREDGAGGEG TARLPTEDYM NHIINGW
