ID   HS2ST_XENLA             Reviewed;         356 AA.
AC   O93336;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Heparan sulfate 2-O-sulfotransferase 1;
DE            EC=2.8.2.-;
GN   Name=hs2st1; Synonyms=hs2st;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9637690; DOI=10.1101/gad.12.12.1894;
RA   Bullock S.L., Fletcher J.M., Beddington R.S.P., Wilson V.A.;
RT   "Renal agenesis in mice homozygous for a gene trap mutation in the gene
RT   encoding heparan sulfate 2-sulfotransferase.";
RL   Genes Dev. 12:1894-1906(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Oocyte;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC       pass type II membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the sulfotransferase 3 family. {ECO:0000305}.
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DR   EMBL; AF060179; AAC41301.1; -; mRNA.
DR   EMBL; BC078097; AAH78097.1; -; mRNA.
DR   RefSeq; NP_001083748.1; NM_001090279.1.
DR   AlphaFoldDB; O93336; -.
DR   SMR; O93336; -.
DR   DNASU; 399095; -.
DR   GeneID; 399095; -.
DR   KEGG; xla:399095; -.
DR   CTD; 399095; -.
DR   Xenbase; XB-GENE-5953205; hs2st1.L.
DR   OMA; KWHEMKP; -.
DR   OrthoDB; 877221at2759; -.
DR   Proteomes; UP000186698; Chromosome 4L.
DR   Bgee; 399095; Expressed in blastula and 19 other tissues.
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:0008146; F:sulfotransferase activity; IEA:InterPro.
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   2: Evidence at transcript level;
KW   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_0000207678"
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:0000250"
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:0000250"
FT   DISULFID        222..228
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   356 AA;  41749 MW;  FEBA74FCF4ACC8AA CRC64;
     MGLLRIMMPP KLQLLAVLTF GVLMLFLENQ IQNLEESREK LERAIARHEV REIEQRHSMD
     GSRQEIALDD DEDILIIYNR VPKTASTSFT NIAYDLCAKN KYHVLHINTT KNNPVMSLQD
     QVRFVKNVSS WREMKPGFYH GHVSFLDFTK FGVKKKPIYI NVIRDPIERL VSYYYFLRFG
     DDYRPGLRRR KQGDKKTFDE CVAAGGSDCA PEKLWLQIPF FCGHSSECWN VGSRWALDQA
     KYNLVNEYFL VGVTEELEDF IMLLEAALPR FFRGATELYR SGKKSHLRKT TEKKAPSKET
     TAKLQQSDIW KMENEFYEFA LEQFQFVRAH AVREKDGELY VLAPNFFYEK IYPKSN