ID   HS2ST_CRILO             Reviewed;         356 AA.
AC   O08889;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=Heparan sulfate 2-O-sulfotransferase 1;
DE            Short=2-O-sulfotransferase;
DE            Short=2OST;
DE            EC=2.8.2.-;
GN   Name=HS2ST1; Synonyms=HS2ST;
OS   Cricetulus longicaudatus (Long-tailed dwarf hamster) (Chinese hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10030;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 73-80; 95-107; 120-128;
RP   181-189 AND 277-280, AND ENZYME ACTIVITY.
RC   TISSUE=Ovary;
RX   PubMed=9153262; DOI=10.1074/jbc.272.21.13980;
RA   Kobayashi M., Habuchi H., Yoneda M., Habuchi O., Kimata K.;
RT   "Molecular cloning and expression of Chinese hamster ovary cell heparan-
RT   sulfate 2-sulfotransferase.";
RL   J. Biol. Chem. 272:13980-13985(1997).
RN   [2]
RP   ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND GLYCOSYLATION.
RX   PubMed=8631801; DOI=10.1074/jbc.271.13.7645;
RA   Kobayashi M., Habuchi H., Habuchi O., Saito M., Kimata K.;
RT   "Purification and characterization of heparan sulfate 2-sulfotransferase
RT   from cultured Chinese hamster ovary cells.";
RL   J. Biol. Chem. 271:7645-7653(1996).
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. Mediates 2-O-sulfation of
CC       both L-iduronyl and D-glucuronyl residues (By similarity).
CC       {ECO:0000250}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.2 uM for PAPS {ECO:0000269|PubMed:8631801};
CC       pH dependence:
CC         Optimum pH is 5.5. {ECO:0000269|PubMed:8631801};
CC   -!- SUBUNIT: Homotrimer. Interacts with the C5-epimerase GLCE (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC       pass type II membrane protein {ECO:0000250}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:8631801}.
CC   -!- SIMILARITY: Belongs to the sulfotransferase 3 family. {ECO:0000305}.
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DR   EMBL; D88811; BAA20422.1; -; mRNA.
DR   AlphaFoldDB; O08889; -.
DR   SMR; O08889; -.
DR   ChEMBL; CHEMBL4212; -.
DR   SABIO-RK; O08889; -.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:WormBase.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Golgi apparatus;
KW   Membrane; Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..356
FT                   /note="Heparan sulfate 2-O-sulfotransferase 1"
FT                   /id="PRO_0000207673"
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;  41831 MW;  DFE479ED070C5EFE CRC64;
     MGLLRIMMPP KLQLLAVVAF AVAMLFLENQ IQKLEESRAK LERAIARHEV REIEQRHTMD
     GPRQDAAVDE EEDIVIIYNR VPKTASTSFT NIAYDLCAKN RYHVLHINTT KNNPVMSLQD
     QVRFVKNITT WNEMKPGFYH GHISYLDFAK FGVKKKPIYI NVIRDPIERL VSYYYFLRFG
     DDYRPGLRRR KQGDKKTFDE CVAEGGSDCA PEKLWLQIPF FCGHSSECWN VGSRWAMDQA
     KYNLINEYFL VGVTEELEDF IMLLEAALPR FFRGATDLYR TGKKSHLRKT TEKKLPTKQT
     IAKLQQSDIW KMENEFYEFA LEQFQFIRAH AVREKDGDLY ILAQNFFYEK IYPKSN