ID   HS2ST_PONAB             Reviewed;         356 AA.
AC   Q5R621; Q5R6Q4;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 64.
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   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-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. Mediates 2-O-sulfation of
CC       both L-iduronyl and D-glucuronyl residues (By similarity).
CC       {ECO:0000250}.
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:0000250}.
CC   -!- SIMILARITY: Belongs to the sulfotransferase 3 family. {ECO:0000305}.
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DR   EMBL; CR860431; CAH92556.1; -; mRNA.
DR   EMBL; CR860679; CAH92795.1; -; mRNA.
DR   RefSeq; NP_001126497.1; NM_001133025.1.
DR   AlphaFoldDB; Q5R621; -.
DR   SMR; Q5R621; -.
DR   STRING; 9601.ENSPPYP00000001370; -.
DR   PRIDE; Q5R621; -.
DR   Ensembl; ENSPPYT00000001415; ENSPPYP00000001370; ENSPPYG00000001183.
DR   GeneID; 100173485; -.
DR   KEGG; pon:100173485; -.
DR   CTD; 9653; -.
DR   eggNOG; KOG3922; Eukaryota.
DR   GeneTree; ENSGT00530000063408; -.
DR   InParanoid; Q5R621; -.
DR   OrthoDB; 877221at2759; -.
DR   Proteomes; UP000001595; Chromosome 1.
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; IEA:Ensembl.
DR   GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR   GO; GO:0015014; P:heparan sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process; IEA:Ensembl.
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   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_0000207676"
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"
FT   CONFLICT        228
FT                   /note="C -> R (in Ref. 1; CAH92556)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   356 AA;  41913 MW;  8F5BBA8DBAE972CE CRC64;
     MGLLRIMMPP KLQLLAVVAF AVAMLFLENQ IQKLEESRSK LERAIARHEV REIEQRHTMD
     GPRQDATLDE EEDMVIIYNR VPKTASTSFT NIAYDLCAKN KYHVLHINTT KNNPVMSLQD
     QMRFVKNITS WKEMKPGFYH GHVSYLDFAK FGVKKKPIYI NVIRDPIERL VSYYYFLRFG
     DDYRPGLRRR KQGDKKTFDE CVAEGGSDCA PEKLWLQIPF FCGHSSECWN VGSRWAMDQA
     KYNLINEYFL VGVTEELEDF IMLLEAALPR FFRGATELYR TGKKSHLRKT TEKKLPTKQT
     IAKLQQSDIW KMENEFYEFA LEQFQFIRAH AVREKDGDLY ILAQNFFYEK IYPKSN