H6ST1_CHICK
ID H6ST1_CHICK Reviewed; 408 AA.
AC Q76KB2;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 4.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Heparan-sulfate 6-O-sulfotransferase 1 {ECO:0000250|UniProtKB:O60243};
DE Short=HS6ST-1;
DE Short=cHS6ST-1;
DE EC=2.8.2.- {ECO:0000250|UniProtKB:O60243};
GN Name=HS6ST1 {ECO:0000250|UniProtKB:O60243};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX PubMed=14660620; DOI=10.1074/jbc.m307304200;
RA Nogami K., Suzuki H., Habuchi H., Ishiguro N., Iwata H., Kimata K.;
RT "Distinctive expression patterns of heparan sulfate O-sulfotransferases and
RT regional differences in heparan sulfate structure in chick limb buds.";
RL J. Biol. Chem. 279:8219-8229(2004).
RN [2]
RP FUNCTION IN LIMB BUD DEVELOPMENT.
RX PubMed=20039926; DOI=10.1111/j.1440-169x.2009.01148.x;
RA Kobayashi T., Habuchi H., Nogami K., Ashikari-Hada S., Tamura K., Ide H.,
RA Kimata K.;
RT "Functional analysis of chick heparan sulfate 6-O-sulfotransferases in limb
RT bud development.";
RL Dev. Growth Differ. 52:146-156(2010).
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 (By similarity).
CC May also play a role in limb development.
CC {ECO:0000250|UniProtKB:O60243, ECO:0000269|PubMed:20039926}.
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 -!- DEVELOPMENTAL STAGE: Expressed in the developing wing bud. At stage 31,
CC widely expressed with a lower level in the heart.
CC {ECO:0000269|PubMed:14660620}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 6 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD00705.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB093515; BAD00705.1; ALT_INIT; mRNA.
DR RefSeq; NP_989813.1; NM_204482.1.
DR AlphaFoldDB; Q76KB2; -.
DR SMR; Q76KB2; -.
DR STRING; 9031.ENSGALP00000003371; -.
DR PaxDb; Q76KB2; -.
DR PRIDE; Q76KB2; -.
DR Ensembl; ENSGALT00000003376; ENSGALP00000003371; ENSGALG00000002155.
DR GeneID; 395141; -.
DR KEGG; gga:395141; -.
DR CTD; 9394; -.
DR VEuPathDB; HostDB:geneid_395141; -.
DR eggNOG; KOG3955; Eukaryota.
DR GeneTree; ENSGT00950000183071; -.
DR HOGENOM; CLU_027877_3_0_1; -.
DR InParanoid; Q76KB2; -.
DR OMA; KNHMQQN; -.
DR OrthoDB; 1167623at2759; -.
DR PhylomeDB; Q76KB2; -.
DR PRO; PR:Q76KB2; -.
DR Proteomes; UP000000539; Chromosome 9.
DR Bgee; ENSGALG00000002155; Expressed in liver and 14 other tissues.
DR ExpressionAtlas; Q76KB2; 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; IBA:GO_Central.
DR GO; GO:0015015; P:heparan sulfate proteoglycan biosynthetic process, enzymatic modification; IBA:GO_Central.
DR GO; GO:0060173; P:limb development; IDA:UniProtKB.
DR GO; GO:0048666; P:neuron development; ISS:UniProtKB.
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 Coiled coil; Glycoprotein; Membrane; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..408
FT /note="Heparan-sulfate 6-O-sulfotransferase 1"
FT /id="PRO_0000190803"
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..408
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 376..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 348..382
FT /evidence="ECO:0000255"
FT ACT_SITE 147
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 90..98
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 120..121
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 137
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 142
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 182
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 190
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 201
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 314..316
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 320..321
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 408 AA; 48092 MW; F1D91F0844ACAF29 CRC64;
MKRAGRTMVE RTSKFLLIVA ASVCFMLILY QYVGPGLSLG APSGRPYAEE PDLFPTPDPH
YVKKYYFPVR ELERELAFDM KGEDVIVFLH IQKTGGTTFG RHLVQNVRLE VPCDCRPGQK
KCTCYRPNRR ETWLFSRFST GWSCGLHADW TELTNCVPGV LGRRESAPNR TPRKFYYITL
LRDPVSRYLS EWRHVQRGAT WKTSLHMCDG RTPTPEELPS CYEGTDWSGC TLQEFMDCPY
NLANNRQVRM LADLSLVGCY NMSFIPENKR AQILLESAKK NLKDMAFFGL TEFQRKTQYL
FERTFNLKFI RPFMQYNSTR AGGVEVDNDT IRRIEELNDL DMQLYDYAKD LFQQRYQYKR
QLERMEQRIK NREERLLHRS NEALPKEETE EQGRLPTEDY MSHIIEKW
