H6ST2_CHICK
ID H6ST2_CHICK Reviewed; 403 AA.
AC Q76LW2; Q5ZJE1;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Heparan-sulfate 6-O-sulfotransferase 2;
DE Short=HS6ST-2;
DE Short=cHS6ST-2;
DE EC=2.8.2.-;
GN Name=HS6ST2; ORFNames=RCJMB04_19a20;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
RN [3]
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. {ECO:0000250,
CC 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;
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 higher level in limb and head.
CC {ECO:0000269|PubMed:14660620}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 6 family. {ECO:0000305}.
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DR EMBL; AB071190; BAD02830.1; -; mRNA.
DR EMBL; AJ720493; CAG32152.1; -; mRNA.
DR RefSeq; NP_989821.1; NM_204490.1.
DR AlphaFoldDB; Q76LW2; -.
DR SMR; Q76LW2; -.
DR STRING; 9031.ENSGALP00000009781; -.
DR PaxDb; Q76LW2; -.
DR Ensembl; ENSGALT00000067058; ENSGALP00000048682; ENSGALG00000034250.
DR GeneID; 395150; -.
DR KEGG; gga:395150; -.
DR CTD; 90161; -.
DR VEuPathDB; HostDB:geneid_395150; -.
DR eggNOG; KOG3955; Eukaryota.
DR GeneTree; ENSGT00950000183071; -.
DR InParanoid; Q76LW2; -.
DR OMA; WWDLDEN; -.
DR OrthoDB; 1167623at2759; -.
DR PhylomeDB; Q76LW2; -.
DR PRO; PR:Q76LW2; -.
DR Proteomes; UP000000539; Chromosome 4.
DR Bgee; ENSGALG00000034250; Expressed in cerebellum and 13 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 GO; GO:0060173; P:limb development; IDA: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 Glycoprotein; Membrane; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..403
FT /note="Heparan-sulfate 6-O-sulfotransferase 2"
FT /id="PRO_0000190807"
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..403
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 381..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 145
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 88..96
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 118..119
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 140
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 145
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 180
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 188
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 199
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 312..314
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 318..319
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 389
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 38
FT /note="R -> H (in Ref. 2; CAG32152)"
FT /evidence="ECO:0000305"
FT CONFLICT 215..223
FT /note="Missing (in Ref. 2; CAG32152)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 403 AA; 47175 MW; 03BEE030927BF3BF CRC64;
MEDRSHKVLL ALVMLFLFAV IVLQYVCPGT ECQLLRLRAL SPAAAADPYR AEDETPARFV
PRFNFSAGDL LRRVDFNIKG DDLIVFLHIQ KTGGTTFGRH LVRNIQLEQP CECRAGQKKC
TCHRPGKRET WLFSRFSTGW SCGLHADWTE LTNCVPSVVD SKKEVRLRPS RNFYYITILR
DPVSRYLSEW RHVQRGATWK ASLHVCDGRS PTTEELPSCY TGDDWSGCSL QEFMDCPYNL
ANNRQVRMLS DLSLVGCYNL SVMPEEQRNK VLLDSAKENL KRMAFFGLTE FQRKTQYLFE
KTFNMNFISP FTQYNSTRAS SVEIDEQTQQ RIEALNFLDM ELYDYAKDLF LQRYQYMRQK
EHQEARRKRQ EQRKILRAKQ AHLREQGENS SSTDYLGNVE RWR
