Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9Y663 (HS3SA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Heparan sulfate glucosamine 3-O-sulfotransferase 3A1

EC=2.8.2.30
Alternative name(s):
Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 3A1
Short name=3-OST-3A
Short name=Heparan sulfate 3-O-sulfotransferase 3A1
Short name=h3-OST-3A
Gene names
Name:HS3ST3A1
Synonyms:3OST3A1, HS3ST3A
ORF Names:UNQ2551/PRO6180
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length406 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) to catalyze the transfer of a sulfo group to an N-unsubstituted glucosamine linked to a 2-O-sulfo iduronic acid unit on heparan sulfate. Catalyzes the O-sulfation of glucosamine in IdoUA2S-GlcNS and also in IdoUA2S-GlcNH2. The substrate-specific O-sulfation generates an enzyme-modified heparan sulfate which acts as a binding receptor to Herpes simplex virus-1 (HSV-1) and permits its entry. Unlike 3-OST-1, does not convert non-anticoagulant heparan sulfate to anticoagulant heparan sulfate. Ref.6

Catalytic activity

3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate.

Subcellular location

Golgi apparatus membrane; Single-pass type II membrane protein Probable.

Tissue specificity

Ubiquitous. Most abundant in heart and placenta, followed by liver and kidney. Ref.1

Sequence similarities

Belongs to the sulfotransferase 1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 406406Heparan sulfate glucosamine 3-O-sulfotransferase 3A1
PRO_0000085217

Regions

Topological domain1 – 2424Cytoplasmic Potential
Transmembrane25 – 4319Helical; Signal-anchor for type II membrane protein; Potential
Topological domain44 – 406363Lumenal Potential
Nucleotide binding162 – 1665PAPS
Nucleotide binding368 – 3725PAPS
Region184 – 1907Substrate binding
Region215 – 2184Substrate binding
Region255 – 2595Substrate binding
Region283 – 2842Substrate binding
Region367 – 3704Substrate binding

Sites

Binding site1661Substrate
Binding site2431PAPS
Binding site2511PAPS

Amino acid modifications

Glycosylation2731N-linked (GlcNAc...) Potential
Glycosylation3441N-linked (GlcNAc...) Potential
Disulfide bond351 ↔ 363 Ref.9

Experimental info

Mutagenesis1611K → A: 99.6% loss of enzymatic activity. Ref.9
Mutagenesis1621K → A: 99.6% loss of enzymatic activity; no HSV1 entry activity. Ref.6 Ref.9
Mutagenesis1661R → E: 99.8% loss of enzymatic activity. Ref.9
Mutagenesis1701E → Q: 17% loss of enzymatic activity. Ref.9
Mutagenesis1731R → S: 44.1% loss of enzymatic activity. Ref.9
Mutagenesis1821G → A: No effect on enzymatic activity. Ref.9
Mutagenesis1841E → Q: 99.9% loss of enzymatic activity. Ref.9
Mutagenesis1861H → F: Abolishes enzymatic activity. Ref.9
Mutagenesis1891D → N: 99.1% loss of enzymatic activity. Ref.9
Mutagenesis1901R → E: 32% loss of enzymatic activity. Ref.9
Mutagenesis1941K → A: 99.5% loss of enzymatic activity. Ref.9
Mutagenesis2151K → A: 99.9% loss of enzymatic activity. Ref.9
Mutagenesis2181S → A: 23.3% loss of enzymatic activity. Ref.9
Mutagenesis2241E → Q: 47.6% loss of enzymatic activity. Ref.9
Mutagenesis2551Q → A: 99.6% loss of enzymatic activity. Ref.9
Mutagenesis2591K → A: 48.3% loss of enzymatic activity. Ref.9
Mutagenesis2881I → A: 65% loss of enzymatic activity. Ref.9
Mutagenesis2931K → A: 33.6% loss of enzymatic activity. Ref.9
Mutagenesis3621H → A: No effect on enzymatic activity. Ref.9
Mutagenesis3651G → A: 43% loss of enzymatic activity. Ref.9
Mutagenesis3661K → A: 99.8% loss of enzymatic activity. Ref.9
Mutagenesis3681K → A: 99.9% loss of enzymatic activity. Ref.9
Mutagenesis3701R → E: 99.2% loss of enzymatic activity. Ref.9

Secondary structure

............................................ 406
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9Y663 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 57B6A0ABC897577A

FASTA40644,900
        10         20         30         40         50         60 
MAPPGPASAL STSAEPLSRS IFRKFLLMLC SLLTSLYVFY CLAERCQTLS GPVVGLSGGG 

        70         80         90        100        110        120 
EEAGAPGGGV LAGGPRELAV WPAAAQRKRL LQLPQWRRRR PPAPRDDGEE AAWEEESPGL 

       130        140        150        160        170        180 
SGGPGGSGAG STVAEAPPGT LALLLDEGSK QLPQAIIIGV KKGGTRALLE FLRVHPDVRA 

       190        200        210        220        230        240 
VGAEPHFFDR SYDKGLAWYR DLMPRTLDGQ ITMEKTPSYF VTREAPARIS AMSKDTKLIV 

       250        260        270        280        290        300 
VVRDPVTRAI SDYTQTLSKR PDIPTFESLT FKNRTAGLID TSWSAIQIGI YAKHLEHWLR 

       310        320        330        340        350        360 
HFPIRQMLFV SGERLISDPA GELGRVQDFL GLKRIITDKH FYFNKTKGFP CLKKAEGSSR 

       370        380        390        400 
PHCLGKTKGR THPEIDREVV RRLREFYRPF NLKFYQMTGH DFGWDG 

« Hide

References

« Hide 'large scale' references
[1]"Multiple isoforms of heparan sulfate D-glucosaminyl 3-O-sulfotransferase. Isolation, characterization, and expression of human cDNAs and identification of distinct genomic loci."
Shworak N.W., Liu J., Petros L.M., Zhang L., Kobayashi M., Copeland N.G., Jenkins N.A., Rosenberg R.D.
J. Biol. Chem. 274:5170-5184(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Tissue: Liver.
[2]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Spleen.
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[6]"A novel role for 3-O-sulfated heparan sulfate in herpes simplex virus 1 entry."
Shukla D., Liu J., Blaiklock P., Shworak N.W., Bai X., Esko J.D., Cohen G.H., Eisenberg R.J., Rosenberg R.D., Spear P.G.
Cell 99:13-22(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN HSV-1 ENTRY, MUTAGENESIS OF LYS-162.
[7]"Expression of heparan sulfate D-glucosaminyl 3-O-sulfotransferase isoforms reveals novel substrate specificities."
Liu J., Shworak N.W., Sinay P., Schwartz J.J., Zhang L., Fritze L.M.S., Rosenberg R.D.
J. Biol. Chem. 274:5185-5192(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[8]"Heparan sulfate D-glucosaminyl 3-O-sulfotransferase-3A sulfates N-unsubstituted glucosamine residues."
Liu J., Shriver Z., Blaiklock P., Yoshida K., Sasisekharan R., Rosenberg R.D.
J. Biol. Chem. 274:38155-38162(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[9]"Structural analysis of the sulfotransferase (3-o-sulfotransferase isoform 3) involved in the biosynthesis of an entry receptor for herpes simplex virus 1."
Moon A.F., Edavettal S.C., Krahn J.M., Munoz E.M., Negishi M., Linhardt R.J., Liu J., Pedersen L.C.
J. Biol. Chem. 279:45185-45193(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 139-406 IN A TERNARY COMPLEX WITH PAPS AND A TETRASACCHARIDE, DISULFIDE BOND, BINDING SITES, MUTAGENESIS OF LYS-161; LYS-162; ARG-166; GLU-170; ARG-173; GLY-182; GLU-184; HIS-186; ASP-189; ARG-190; LYS-194; LYS-215; SER-218; GLU-224; GLN-255; LYS-259; ILE-288; LYS-293; HIS-362; GLY-365; LYS-366; LYS-368 AND ARG-370.
+Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF105376 mRNA. Translation: AAD30208.1.
AY358838 mRNA. Translation: AAQ89197.1.
AK292047 mRNA. Translation: BAF84736.1.
CH471108 Genomic DNA. Translation: EAW89959.1.
BC044647 mRNA. Translation: AAH44647.1.
CCDSCCDS11165.1.
RefSeqNP_006033.1. NM_006042.1.
UniGeneHs.462270.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1T8TX-ray1.85A/B139-406[»]
1T8UX-ray1.95A/B139-406[»]
ProteinModelPortalQ9Y663.
SMRQ9Y663. Positions 139-406.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115280. 1 interaction.
STRING9606.ENSP00000284110.

PTM databases

PhosphoSiteQ9Y663.

Polymorphism databases

DMDM61214551.

Proteomic databases

PaxDbQ9Y663.
PRIDEQ9Y663.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000284110; ENSP00000284110; ENSG00000153976.
GeneID9955.
KEGGhsa:9955.
UCSCuc002gob.1. human.

Organism-specific databases

CTD9955.
GeneCardsGC17M013339.
HGNCHGNC:5196. HS3ST3A1.
MIM604057. gene.
neXtProtNX_Q9Y663.
PharmGKBPA29469.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG73846.
HOGENOMHOG000036663.
HOVERGENHBG053377.
InParanoidQ9Y663.
KOK07809.
OMASGERLIM.
OrthoDBEOG7PS1GM.
PhylomeDBQ9Y663.
TreeFamTF350755.

Enzyme and pathway databases

BioCycMetaCyc:HS07937-MONOMER.
ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.

Gene expression databases

ArrayExpressQ9Y663.
BgeeQ9Y663.
CleanExHS_HS3ST3A1.
GenevestigatorQ9Y663.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR000863. Sulfotransferase_dom.
[Graphical view]
PfamPF00685. Sulfotransfer_1. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ9Y663.
GeneWikiHS3ST3A1.
GenomeRNAi9955.
NextBio37564.
PROQ9Y663.
SOURCESearch...

Entry information

Entry nameHS3SA_HUMAN
AccessionPrimary (citable) accession number: Q9Y663
Secondary accession number(s): A8K7N2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM