[1]	NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION. TISSUE=Ovary; DOI=10.1074/jbc.M101441200; PubMed=11551899 [NCBI, ExPASy, EBI, Israel, Japan] Zhang L., Beeler D.L., Lawrence R., Lech M., Liu J., Davis J.C., Shriver Z., Sasisekharan R., Rosenberg R.D.; "6-O-sulfotransferase-1 represents a critical enzyme in the anticoagulant heparan sulfate biosynthetic pathway."; J. Biol. Chem. 276:42311-42321(2001).
[2]	NUCLEOTIDE SEQUENCE [MRNA] OF 28-263, AND PROTEIN SEQUENCE OF 28-40; 58-65; 95-99; 124-128; 158-163 AND 230-236. TISSUE=Ovary; DOI=10.1074/jbc.273.15.9208; PubMed=9535912 [NCBI, ExPASy, EBI, Israel, Japan] Habuchi H., Kobayashi M., Kimata K.; "Molecular characterization and expression of heparan-sulfate 6-sulfotransferase."; J. Biol. Chem. 273:9208-9213(1998).
[3]	FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND GLYCOSYLATION. TISSUE=Ovary; DOI=10.1074/jbc.270.8.4172; PubMed=7876170 [NCBI, ExPASy, EBI, Israel, Japan] Habuchi H., Habuchi O., Kimata K.; "Purification and characterization of heparan sulfate 6-sulfotransferase from the culture medium of Chinese hamster ovary cells."; J. Biol. Chem. 270:4172-4179(1995).

Comments

FUNCTION: 6-O-sulfation enzyme which catalyzes the transfer of sulfate from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to position 6 of the N-sulfoglucosamine residue (GlcNS) of heparan sulfate. Also transfers sulfate to CDSNS-heparin and performs the crucial step modification in the biosynthesis of anticoagulant heparan sulfate (HSact).
CATALYTIC ACTIVITY: 3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 6-sulfate.
ENZYME REGULATION: Inhibited by dithiothreitol and stimulated by protamine.
BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters: K_M=0.44 µM for PAPS;
pH dependence: Optimum pH is 6.3;
SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein (Potential).
PTM: N-glycosylated.
SIMILARITY: Belongs to the sulfotransferase 6 family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AY043180; AAL05593.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB006180; BAA25761.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

Q91ZB4.

Ontologies

GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0016740;	Molecular function: transferase activity (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR010635; HS6ST.
Graphical view of domain structure.

PANTHER

PTHR12812; HS6ST; 1.

Pfam

PF06765; HS6ST; 1.
Pfam graphical view of domain structure.

ProtoNet

Q91ZB4.

Phylogenomic databases

HOVERGEN

Q91ZB4; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Direct protein sequencing; Glycoprotein; Membrane; Signal-anchor; Transferase; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 401`	`401`	`Heparan-sulfate 6-O-sulfotransferase 1.`	`PRO_0000190800`
`TOPO_DOM`	`1 4`	`4`	`Cytoplasmic (Potential).`
`TRANSMEM`	`5 27`	`23`	`Signal-anchor for type II membrane protein (Potential).`
`TOPO_DOM`	`28 401`	`374`	`Lumenal (Potential).`
`REGION`	`86 92`	`7`	`5'-phosphosulfate-binding (Potential).`
`REGION`	`175 183`	`9`	`3'-phosphate binding (Potential).`
`CARBOHYD`	`254 254`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`310 310`		`N-linked (GlcNAc...) (Potential).`
`CONFLICT`	`172 174`		`TLL -> ILV (in Ref. 2; BAA25761).`
`CONFLICT`	`261 263`		`SKR -> RAA (in Ref. 2; BAA25761).`

Sequence information

Length: 401 AA [This is the length of the unprocessed precursor]

Molecular weight: 47080 Da [This is the MW of the unprocessed precursor]

CRC64: 31FDB48A6FC4FB25 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVERASKFVL VVAGSACFML ILYQYAGPGL SLGAPGGRAP PDDLDLFPTP DPHYEKKYYF 

        70         80         90        100        110        120 
PVRELERSLR FDMKGDDVIV FLHIQKTGGT TFGRHLVQNV RLEVPCDCRP GQKKCTCYRP 

       130        140        150        160        170        180 
NRRETWLFSR FSTGWSCGLH ADWTELTNCV PGVLDRRDPA GLRSPRKFYY ITLLRDPVSR 

       190        200        210        220        230        240 
YLSEWRHVQR GATWKTSLHM CDGRTPTPEE LPPCYEGTDW SGCTLQEFMD CPYNLANNRQ 

       250        260        270        280        290        300 
VRMLADLSLV GCYNLSFIPE SKRAQLLLES AKKNLRGMAF FGLTEFQRKT QYLFERTFNL 

       310        320        330        340        350        360 
KFIRPFMQYN STRAGGVEVD EDTIRHIEEL NDLDMQLYDY AKDLFQQRYQ YKRQLERREQ 

       370        380        390        400 
RLRNREERLL HRSKEALPRE DTEEPGRVPT EDYMSHIIEK W

Q91ZB4 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools