H6S3B_DANRE
ID H6S3B_DANRE Reviewed; 419 AA.
AC A0MGZ7;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Heparan-sulfate 6-O-sulfotransferase 3-B {ECO:0000312|ZFIN:ZDB-GENE-070103-3};
DE Short=HS 6-OST-3-B {ECO:0000305};
DE EC=2.8.2.- {ECO:0000269|PubMed:28103688};
GN Name=hs6st3b {ECO:0000312|ZFIN:ZDB-GENE-070103-3};
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:ABH11458.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
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).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 75-395 IN COMPLEX WITH PAPS AND
RP HEPARAN SULFATE OLIGOSACCHARIDE SUBSTRATES, FUNCTION, CATALYTIC ACTIVITY,
RP ACTIVE SITE, AND MUTAGENESIS OF HIS-101; LYS-104; LYS-131; LYS-132;
RP ARG-148; TRP-153; HIS-158; HIS-203 AND TRP-210.
RX PubMed=28103688; DOI=10.1021/acschembio.6b00841;
RA Xu Y., Moon A.F., Xu S., Krahn J.M., Liu J., Pedersen L.C.;
RT "Structure based substrate specificity analysis of heparan sulfate 6-O-
RT sulfotransferases.";
RL ACS Chem. Biol. 12:73-82(2017).
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:28103688}.
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:0000269|PubMed:28103688};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type II
CC membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: In early somitogenesis, expressed in presumptive
CC forebrain and midbrain, tail bud and Kupffer's vesicle. During mid-
CC somitogenesis, ubiquitous expression which is strongest in the somites
CC and eye. During late somitogenesis, predominantly expressed in eye,
CC hindbrain and ventral somites. At 24 hours post-fertilization (hpf),
CC restricted to lens and neural retina, brain, otic vesicle and somites.
CC At 36 hpf, brain expression is restricted to telencephalon. At 48 hpf,
CC restricted to telencephalon and pectoral fin.
CC {ECO:0000269|PubMed:17075883}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:17075883}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 6 family. {ECO:0000255}.
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; DQ812996; ABH11458.1; -; mRNA.
DR RefSeq; NP_001073663.1; NM_001080194.1.
DR PDB; 5T03; X-ray; 2.10 A; A/B=75-395.
DR PDB; 5T05; X-ray; 1.95 A; A/B=75-395.
DR PDB; 5T0A; X-ray; 1.95 A; A/B=75-395.
DR PDBsum; 5T03; -.
DR PDBsum; 5T05; -.
DR PDBsum; 5T0A; -.
DR AlphaFoldDB; A0MGZ7; -.
DR SMR; A0MGZ7; -.
DR STRING; 7955.ENSDARP00000065928; -.
DR PaxDb; A0MGZ7; -.
DR GeneID; 569353; -.
DR KEGG; dre:569353; -.
DR CTD; 569353; -.
DR ZFIN; ZDB-GENE-070103-3; hs6st3b.
DR eggNOG; KOG3955; Eukaryota.
DR InParanoid; A0MGZ7; -.
DR OrthoDB; 1167623at2759; -.
DR Reactome; R-DRE-2022928; HS-GAG biosynthesis.
DR PRO; PR:A0MGZ7; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0050656; F:3'-phosphoadenosine 5'-phosphosulfate binding; IDA:ZFIN.
DR GO; GO:0017095; F:heparan sulfate 6-O-sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0070492; F:oligosaccharide binding; IDA:ZFIN.
DR GO; GO:0008146; F:sulfotransferase activity; IDA: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 1: Evidence at protein level;
KW 3D-structure; Glycoprotein; Membrane; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..419
FT /note="Heparan-sulfate 6-O-sulfotransferase 3-B"
FT /id="PRO_0000283820"
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..419
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 158
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:28103688"
FT BINDING 101..109
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000269|PubMed:28103688"
FT BINDING 131..132
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:28103688"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:28103688"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:28103688"
FT BINDING 158
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:28103688"
FT BINDING 191
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000269|PubMed:28103688"
FT BINDING 199
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000269|PubMed:28103688"
FT BINDING 203
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:28103688"
FT BINDING 210
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:28103688"
FT BINDING 323..325
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000269|PubMed:28103688"
FT BINDING 329..330
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000269|PubMed:28103688"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 326
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 393
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 101
FT /note="H->A: Significantly impairs catalytic activity."
FT /evidence="ECO:0000269|PubMed:28103688"
FT MUTAGEN 104
FT /note="K->A: Significantly impairs catalytic activity."
FT /evidence="ECO:0000269|PubMed:28103688"
FT MUTAGEN 131
FT /note="K->A: Slightly impairs catalytic activity."
FT /evidence="ECO:0000269|PubMed:28103688"
FT MUTAGEN 132
FT /note="K->A,E: Significantly impairs catalytic activity."
FT /evidence="ECO:0000269|PubMed:28103688"
FT MUTAGEN 148
FT /note="R->A: Moderately impairs catalytic activity."
FT /evidence="ECO:0000269|PubMed:28103688"
FT MUTAGEN 153
FT /note="W->A: Moderately impairs catalytic activity."
FT /evidence="ECO:0000269|PubMed:28103688"
FT MUTAGEN 158
FT /note="H->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:28103688"
FT MUTAGEN 203
FT /note="H->A: Significantly impairs catalytic activity."
FT /evidence="ECO:0000269|PubMed:28103688"
FT MUTAGEN 210
FT /note="W->A: Significantly impairs catalytic activity."
FT /evidence="ECO:0000269|PubMed:28103688"
FT HELIX 80..83
FT /evidence="ECO:0007829|PDB:5T0A"
FT TURN 91..94
FT /evidence="ECO:0007829|PDB:5T0A"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:5T0A"
FT HELIX 107..116
FT /evidence="ECO:0007829|PDB:5T0A"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:5T0A"
FT TURN 148..151
FT /evidence="ECO:0007829|PDB:5T0A"
FT HELIX 161..172
FT /evidence="ECO:0007829|PDB:5T0A"
FT STRAND 184..190
FT /evidence="ECO:0007829|PDB:5T0A"
FT HELIX 193..205
FT /evidence="ECO:0007829|PDB:5T0A"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:5T0A"
FT STRAND 230..234
FT /evidence="ECO:0007829|PDB:5T05"
FT HELIX 241..246
FT /evidence="ECO:0007829|PDB:5T0A"
FT TURN 251..254
FT /evidence="ECO:0007829|PDB:5T0A"
FT HELIX 255..260
FT /evidence="ECO:0007829|PDB:5T0A"
FT HELIX 263..266
FT /evidence="ECO:0007829|PDB:5T0A"
FT TURN 267..269
FT /evidence="ECO:0007829|PDB:5T0A"
FT HELIX 276..293
FT /evidence="ECO:0007829|PDB:5T0A"
FT STRAND 294..299
FT /evidence="ECO:0007829|PDB:5T0A"
FT HELIX 303..314
FT /evidence="ECO:0007829|PDB:5T0A"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:5T0A"
FT TURN 329..332
FT /evidence="ECO:0007829|PDB:5T0A"
FT HELIX 337..346
FT /evidence="ECO:0007829|PDB:5T0A"
FT HELIX 348..382
FT /evidence="ECO:0007829|PDB:5T0A"
FT HELIX 384..389
FT /evidence="ECO:0007829|PDB:5T0A"
SQ SEQUENCE 419 AA; 49346 MW; D83CDCF7356749B5 CRC64;
MNDKPNKWIF IPILAILFVM IGYQYVCPAG GQACHFRTGD KLVRIAPLAT PDPTTDDLYR
EQDPEEDNPP KCASKFNFTE RDLTRDVDFN IKGDDVIVFL HIQKTGGTTF GRHLVRNIRL
EQPCDCKAGQ KKCTCHRPGK QESWLFSRFS TGWSCGLHAD WTELTNCVPV IMDKRQPPKR
KRNFYYITML RDPVSRYLSE WKHVQRGATW KTSLHMCDGR SPTQDELPTC YNGDDWSGVT
LHDFMDCPSN LANNRQVRML ADLSLVGCYN LSTMNESERN PILLASAKSN LKNMAFYGLT
EFQRKTQYLF ERTFHLRFIS AFTQINSTRA ANVELRDDMR SRIEQLNMLD MQLYEFAKDL
FLQRYQFVRQ RERQEERLKR REERRWIRER RVNQSKEPIV ENQTRVTTTE DYASQVVRW
