HS2ST_CHICK
ID HS2ST_CHICK Reviewed; 356 AA.
AC Q76KB1;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Heparan sulfate 2-O-sulfotransferase 1;
DE Short=cHS2ST;
DE EC=2.8.2.-;
GN Name=HS2ST1; Synonyms=HS2ST;
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 TISSUE SPECIFICITY.
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 X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 69-356 IN COMPLEX WITH E COLI
RP MALE, FUNCTION, DISULFIDE BONDS, MUTAGENESIS OF ARG-80; TYR-94; HIS-106;
RP HIS-140; HIS-142; ARG-189 AND ARG-288, ACTIVE SITE, AND SUBUNIT.
RX PubMed=19022906; DOI=10.1073/pnas.0806975105;
RA Bethea H.N., Xu D., Liu J., Pedersen L.C.;
RT "Redirecting the substrate specificity of heparan sulfate 2-O-
RT sulfotransferase by structurally guided mutagenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:18724-18729(2008).
CC -!- FUNCTION: Catalyzes the transfer of sulfate to the C2-position of
CC selected hexuronic acid residues within the maturing heparan sulfate
CC (HS). 2-O-sulfation within HS, particularly of iduronate residues, is
CC essential for HS to participate in a variety of high-affinity ligand-
CC binding interactions and signaling processes.
CC {ECO:0000269|PubMed:19022906}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:19022906}.
CC -!- INTERACTION:
CC Q76KB1; Q76KB1: HS2ST1; NbExp=2; IntAct=EBI-9026219, EBI-9026219;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in heart, limb, head and trunk. At stages
CC 20 and 24, it is expressed in the most regions of the first and second
CC pharyngeal arche. In both wing and leg buds, it is detected at the
CC overlying ectoderm and mesenchyme throughout stages 21, 23 and 24.
CC {ECO:0000269|PubMed:14660620}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 3 family. {ECO:0000305}.
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DR EMBL; AB093516; BAD00706.1; -; mRNA.
DR RefSeq; NP_989812.1; NM_204481.1.
DR PDB; 3F5F; X-ray; 2.65 A; A=69-356.
DR PDB; 4NDZ; X-ray; 3.45 A; A/B/C/D/E/F=69-356.
DR PDBsum; 3F5F; -.
DR PDBsum; 4NDZ; -.
DR AlphaFoldDB; Q76KB1; -.
DR SMR; Q76KB1; -.
DR DIP; DIP-48642N; -.
DR STRING; 9031.ENSGALP00000042738; -.
DR PaxDb; Q76KB1; -.
DR Ensembl; ENSGALT00000044504; ENSGALP00000042738; ENSGALG00000028423.
DR GeneID; 395140; -.
DR KEGG; gga:395140; -.
DR CTD; 9653; -.
DR VEuPathDB; HostDB:geneid_395140; -.
DR eggNOG; KOG3922; Eukaryota.
DR GeneTree; ENSGT00530000063408; -.
DR InParanoid; Q76KB1; -.
DR OMA; KWHEMKP; -.
DR OrthoDB; 877221at2759; -.
DR PhylomeDB; Q76KB1; -.
DR TreeFam; TF315238; -.
DR EvolutionaryTrace; Q76KB1; -.
DR PRO; PR:Q76KB1; -.
DR Proteomes; UP000000539; Chromosome 8.
DR Bgee; ENSGALG00000028423; Expressed in liver and 14 other tissues.
DR ExpressionAtlas; Q76KB1; baseline and differential.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004394; F:heparan sulfate 2-O-sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008146; F:sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR GO; GO:0015015; P:heparan sulfate proteoglycan biosynthetic process, enzymatic modification; IBA:GO_Central.
DR GO; GO:0015014; P:heparan sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process; IBA:GO_Central.
DR GO; GO:0030202; P:heparin metabolic process; IEA:Ensembl.
DR GO; GO:0060676; P:ureteric bud formation; IEA:Ensembl.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR007734; Heparan_SO4_2-O-STrfase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005331; Sulfotransferase.
DR PANTHER; PTHR12129; PTHR12129; 1.
DR Pfam; PF03567; Sulfotransfer_2; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Golgi apparatus; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..356
FT /note="Heparan sulfate 2-O-sulfotransferase 1"
FT /id="PRO_0000207677"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..28
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..356
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 140
FT /evidence="ECO:0000305|PubMed:19022906"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 201..209
FT /evidence="ECO:0000269|PubMed:19022906"
FT DISULFID 222..228
FT /evidence="ECO:0000269|PubMed:19022906"
FT MUTAGEN 80
FT /note="R->A: Less than 10% activity toward polysaccharide
FT substrates."
FT /evidence="ECO:0000269|PubMed:19022906"
FT MUTAGEN 94
FT /note="Y->A: Preferentially transfers sulfates to IdoA
FT units."
FT /evidence="ECO:0000269|PubMed:19022906"
FT MUTAGEN 106
FT /note="H->A: Preferentially transfers sulfates to IdoA
FT units."
FT /evidence="ECO:0000269|PubMed:19022906"
FT MUTAGEN 140
FT /note="H->A: Complete loss of activity; when associated
FT with Ala-142."
FT /evidence="ECO:0000269|PubMed:19022906"
FT MUTAGEN 142
FT /note="H->A: Complete loss of activity; when associated
FT with Ala-140."
FT /evidence="ECO:0000269|PubMed:19022906"
FT MUTAGEN 189
FT /note="R->A: Only transfers sulfates to GlcA moieties
FT within the polysaccharide."
FT /evidence="ECO:0000269|PubMed:19022906"
FT MUTAGEN 288
FT /note="R->A: Less than 10% activity toward polysaccharide
FT substrates."
FT /evidence="ECO:0000269|PubMed:19022906"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:3F5F"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:3F5F"
FT HELIX 86..100
FT /evidence="ECO:0007829|PDB:3F5F"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:3F5F"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:3F5F"
FT HELIX 118..130
FT /evidence="ECO:0007829|PDB:3F5F"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:3F5F"
FT STRAND 136..142
FT /evidence="ECO:0007829|PDB:3F5F"
FT HELIX 148..151
FT /evidence="ECO:0007829|PDB:3F5F"
FT STRAND 158..163
FT /evidence="ECO:0007829|PDB:3F5F"
FT HELIX 166..179
FT /evidence="ECO:0007829|PDB:3F5F"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:3F5F"
FT HELIX 198..203
FT /evidence="ECO:0007829|PDB:3F5F"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:3F5F"
FT HELIX 217..222
FT /evidence="ECO:0007829|PDB:3F5F"
FT HELIX 226..229
FT /evidence="ECO:0007829|PDB:3F5F"
FT HELIX 234..246
FT /evidence="ECO:0007829|PDB:3F5F"
FT STRAND 248..253
FT /evidence="ECO:0007829|PDB:3F5F"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:3F5F"
FT HELIX 257..267
FT /evidence="ECO:0007829|PDB:3F5F"
FT HELIX 269..272
FT /evidence="ECO:0007829|PDB:3F5F"
FT HELIX 275..280
FT /evidence="ECO:0007829|PDB:3F5F"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:4NDZ"
FT HELIX 298..304
FT /evidence="ECO:0007829|PDB:3F5F"
FT HELIX 308..329
FT /evidence="ECO:0007829|PDB:3F5F"
FT STRAND 332..335
FT /evidence="ECO:0007829|PDB:3F5F"
FT STRAND 338..341
FT /evidence="ECO:0007829|PDB:3F5F"
FT STRAND 348..352
FT /evidence="ECO:0007829|PDB:3F5F"
SQ SEQUENCE 356 AA; 41702 MW; D19F4F276DDDBFA1 CRC64;
MGLLRIMLPP KLQLLAVLVF GVAVLFLENQ IQKLEESRGK LERAIARHEV REIEQRHTAD
GPRQEVALDE EDDVVIIYNR VPKTASTSFT NIAYDLCAKN RYHVLHINTT KNNPVMSLQD
QVRFVKNVTS WKEMKPGFYH GHVSYLDFAK FGVKKKPIYI NVIRDPIERL VSYYYFLRFG
DDYRPGLRRR KQGDKKTFDE CVAAGGSDCA PEKLWLQIPF FCGHSSECWN VGSRWALEQA
KYNLINEYFL VGVTEELEDF IMLLEAALPR FFRGATELYR TGKKSHLRKT TEKKLPTKET
IAKLQQSEIW KMENEFYEFA LEQFQFVRAH AVREKDGELY ILAQNFFYEK IYPKSN
