ID   H6ST1_CRIGR             Reviewed;         401 AA.
AC   Q91ZB4; O70158;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 3.
DT   09-FEB-2010, entry version 33.
DE   RecName: Full=Heparan-sulfate 6-O-sulfotransferase 1;
DE            Short=HS6ST-1;
DE            EC=2.8.2.-;
GN   Name=HS6ST1; Synonyms=6OST1;
OS   Cricetulus griseus (Chinese hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   TISSUE=Ovary;
RX   PubMed=11551899; DOI=10.1074/jbc.M101441200;
RA   Zhang L., Beeler D.L., Lawrence R., Lech M., Liu J., Davis J.C.,
RA   Shriver Z., Sasisekharan R., Rosenberg R.D.;
RT   "6-O-sulfotransferase-1 represents a critical enzyme in the
RT   anticoagulant heparan sulfate biosynthetic pathway.";
RL   J. Biol. Chem. 276:42311-42321(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 28-263, AND PROTEIN SEQUENCE OF 28-40;
RP   58-65; 95-99; 124-128; 158-163 AND 230-236.
RC   TISSUE=Ovary;
RX   MEDLINE=98204920; PubMed=9535912; DOI=10.1074/jbc.273.15.9208;
RA   Habuchi H., Kobayashi M., Kimata K.;
RT   "Molecular characterization and expression of heparan-sulfate 6-
RT   sulfotransferase.";
RL   J. Biol. Chem. 273:9208-9213(1998).
RN   [3]
RP   FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   GLYCOSYLATION.
RC   TISSUE=Ovary;
RX   MEDLINE=95181391; PubMed=7876170; DOI=10.1074/jbc.270.8.4172;
RA   Habuchi H., Habuchi O., Kimata K.;
RT   "Purification and characterization of heparan sulfate 6-
RT   sulfotransferase from the culture medium of Chinese hamster ovary
RT   cells.";
RL   J. Biol. Chem. 270:4172-4179(1995).
CC   -!- FUNCTION: 6-O-sulfation enzyme which catalyzes the transfer of
CC       sulfate from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to
CC       position 6 of the N-sulfoglucosamine residue (GlcNS) of heparan
CC       sulfate. Also transfers sulfate to CDSNS-heparin and performs the
CC       crucial step modification in the biosynthesis of anticoagulant
CC       heparan sulfate (HSact).
CC   -!- CATALYTIC ACTIVITY: 3'-phosphoadenylyl sulfate + [heparan
CC       sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan
CC       sulfate]-glucosamine 6-sulfate.
CC   -!- ENZYME REGULATION: Inhibited by dithiothreitol and stimulated by
CC       protamine.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.44 uM for PAPS;
CC       pH dependence:
CC         Optimum pH is 6.3;
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane
CC       protein (Potential).
CC   -!- PTM: N-glycosylated.
CC   -!- SIMILARITY: Belongs to the sulfotransferase 6 family.
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DR   EMBL; AY043180; AAL05593.1; -; mRNA.
DR   EMBL; AB006180; BAA25761.1; -; mRNA.
DR   HOVERGEN; Q91ZB4; -.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:InterPro.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008146; F:sulfotransferase activity; IEA:InterPro.
DR   GO; GO:0016051; P:carbohydrate biosynthetic process; IEA:InterPro.
DR   InterPro; IPR010635; Heparan_SO4-6-sulfoTrfase.
DR   InterPro; IPR005331; Sulfotransferase.
DR   PANTHER; PTHR12812; HS6ST; 1.
DR   Pfam; PF03567; Sulfotransfer_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Membrane; Signal-anchor;
KW   Transferase; Transmembrane.
FT   CHAIN         1    401       Heparan-sulfate 6-O-sulfotransferase 1.
FT                                /FTId=PRO_0000190800.
FT   TOPO_DOM      1      4       Cytoplasmic (Potential).
FT   TRANSMEM      5     27       Signal-anchor for type II membrane
FT                                protein (Potential).
FT   TOPO_DOM     28    401       Lumenal (Potential).
FT   REGION       86     92       5'-phosphosulfate-binding (Potential).
FT   REGION      175    183       3'-phosphate binding (Potential).
FT   CARBOHYD    254    254       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    310    310       N-linked (GlcNAc...) (Potential).
FT   CONFLICT    172    174       TLL -> ILV (in Ref. 2; BAA25761).
FT   CONFLICT    261    263       SKR -> RAA (in Ref. 2; BAA25761).
SQ   SEQUENCE   401 AA;  47080 MW;  31FDB48A6FC4FB25 CRC64;
     MVERASKFVL VVAGSACFML ILYQYAGPGL SLGAPGGRAP PDDLDLFPTP DPHYEKKYYF
     PVRELERSLR FDMKGDDVIV FLHIQKTGGT TFGRHLVQNV RLEVPCDCRP GQKKCTCYRP
     NRRETWLFSR FSTGWSCGLH ADWTELTNCV PGVLDRRDPA GLRSPRKFYY ITLLRDPVSR
     YLSEWRHVQR GATWKTSLHM CDGRTPTPEE LPPCYEGTDW SGCTLQEFMD CPYNLANNRQ
     VRMLADLSLV GCYNLSFIPE SKRAQLLLES AKKNLRGMAF FGLTEFQRKT QYLFERTFNL
     KFIRPFMQYN STRAGGVEVD EDTIRHIEEL NDLDMQLYDY AKDLFQQRYQ YKRQLERREQ
     RLRNREERLL HRSKEALPRE DTEEPGRVPT EDYMSHIIEK W
//