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Q8IZT8 (HS3S5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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 5

EC=2.8.2.23
Alternative name(s):
Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 5
Short name=3-OST-5
Short name=Heparan sulfate 3-O-sulfotransferase 5
Short name=h3-OST-5
Gene names
Name:HS3ST5
Synonyms:3OST5, HS3OST5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length346 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 position 3 of glucosamine residues in heparan. Catalyzes the rate limiting step in the biosynthesis of heparan sulfate (HSact). This modification is a crucial step in the biosynthesis of anticoagulant heparan sulfate as it completes the structure of the antithrombin pentasaccharide binding site. Also generates GlcUA-GlcNS or IdoUA-GlcNS and 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. Ref.1

Catalytic activity

3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate. Ref.8

Subcellular location

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

Tissue specificity

Highly expressed in skeletal muscle and fetal brain, and also found in adult brain, spinal cord, cerebellum and colon. Ref.1 Ref.5

Sequence similarities

Belongs to the sulfotransferase 1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 346346Heparan sulfate glucosamine 3-O-sulfotransferase 5
PRO_0000085222

Regions

Topological domain1 – 1212Cytoplasmic Potential
Transmembrane13 – 3220Helical; Signal-anchor for type II membrane protein; Potential
Topological domain33 – 346314Lumenal Potential
Nucleotide binding100 – 1045PAPS By similarity
Nucleotide binding309 – 3135PAPS By similarity
Region122 – 1287Substrate binding By similarity
Region155 – 1584Substrate binding By similarity
Region226 – 2272Substrate binding By similarity

Sites

Binding site1831PAPS By similarity
Binding site1911PAPS By similarity
Binding site2931PAPS By similarity

Amino acid modifications

Glycosylation2871N-linked (GlcNAc...) Potential
Disulfide bond294 ↔ 304 By similarity

Natural variations

Natural variant2471I → N.
Corresponds to variant rs17793043 [ dbSNP | Ensembl ].
VAR_052531

Experimental info

Mutagenesis991R → A: Reduces enzyme activity by over 99%. Ref.8
Mutagenesis1041R → A: Reduces enzyme activity by 93%,. Ref.8
Mutagenesis1551K → A: Reduces enzyme activity by over 99%. Ref.8
Mutagenesis1951Q → A: Reduces enzyme activity by over 99%. Ref.8
Mutagenesis3091K → A: Loss of enzyme activity. Ref.8
Mutagenesis3111R → A: Reduces enzyme activity by 98%. Ref.8

Secondary structure

............................................ 346
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8IZT8 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: C763F70793FDB156

FASTA34640,408
        10         20         30         40         50         60 
MLFKQQAWLR QKLLVLGSLA VGSLLYLVAR VGSLDRLQPI CPIEGRLGGA RTQAEFPLRA 

        70         80         90        100        110        120 
LQFKRGLLHE FRKGNASKEQ VRLHDLVQQL PKAIIIGVRK GGTRALLEML NLHPAVVKAS 

       130        140        150        160        170        180 
QEIHFFDNDE NYGKGIEWYR KKMPFSYPQQ ITIEKSPAYF ITEEVPERIY KMNSSIKLLI 

       190        200        210        220        230        240 
IVREPTTRAI SDYTQVLEGK ERKNKTYYKF EKLAIDPNTC EVNTKYKAVR TSIYTKHLER 

       250        260        270        280        290        300 
WLKYFPIEQF HVVDGDRLIT EPLPELQLVE KFLNLPPRIS QYNLYFNATR GFYCLRFNII 

       310        320        330        340 
FNKCLAGSKG RIHPEVDPSV ITKLRKFFHP FNQKFYQITG RTLNWP 

« Hide

References

« Hide 'large scale' references
[1]"Heparan sulfate 3-O-sulfotransferase isoform 5 generates both an antithrombin-binding site and an entry receptor for herpes simplex virus, type 1."
Xia G., Chen J., Tiwari V., Ju W., Li J.-P., Malmstroem A., Shukla D., Liu J.
J. Biol. Chem. 277:37912-37919(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, CHARACTERIZATION, FUNCTION IN HSV-1 ENTRY.
Tissue: Placenta.
[2]"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: Caudate nucleus and Corpus callosum.
[3]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].
[4]"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.
[5]"Characterization of a heparan sulfate 3-O-sulfotransferase-5, an enzyme synthesizing a tetrasulfated disaccharide."
Mochizuki H., Yoshida K., Gotoh M., Sugioka S., Kikuchi N., Kwon Y.-D., Tawada A., Maeyama K., Inaba N., Hiruma T., Kimata K., Narimatsu H.
J. Biol. Chem. 278:26780-26787(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, TISSUE SPECIFICITY.
[6]"The biosynthesis of anticoagulant heparan sulfate by the heparan sulfate 3-O-sulfotransferase isoform 5."
Duncan M.B., Chen J., Krise J.P., Liu J.
Biochim. Biophys. Acta 1671:34-43(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[7]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"Engineering sulfotransferases to modify heparan sulfate."
Xu D., Moon A.F., Song D., Pedersen L.C., Liu J.
Nat. Chem. Biol. 4:200-202(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 88-346 IN COMPLEX WITH ADENOSINE-3'-5'-DIPHOSPHATE, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-99; ARG-104; LYS-155; GLN-195; LYS-309 AND ARG-311.
+Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF503292 mRNA. Translation: AAN37737.1.
AK091074 mRNA. No translation available.
AK289907 mRNA. Translation: BAF82596.1.
CH471051 Genomic DNA. Translation: EAW48251.1.
BC093911 mRNA. Translation: AAH93911.1.
BC093913 mRNA. Translation: AAH93913.1.
RefSeqNP_705840.2. NM_153612.3.
UniGeneHs.645477.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3BD9X-ray2.30A88-346[»]
ProteinModelPortalQ8IZT8.
SMRQ8IZT8. Positions 87-346.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000387653.

PTM databases

PhosphoSiteQ8IZT8.

Polymorphism databases

DMDM61214369.

Proteomic databases

PaxDbQ8IZT8.
PeptideAtlasQ8IZT8.
PRIDEQ8IZT8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000312719; ENSP00000427888; ENSG00000249853.
ENST00000411826; ENSP00000440332; ENSG00000249853.
GeneID222537.
KEGGhsa:222537.
UCSCuc003pwg.4. human.

Organism-specific databases

CTD222537.
GeneCardsGC06M114376.
HGNCHGNC:19419. HS3ST5.
HPAHPA021823.
MIM609407. gene.
neXtProtNX_Q8IZT8.
PharmGKBPA164741639.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG282030.
HOGENOMHOG000036663.
HOVERGENHBG053377.
InParanoidQ8IZT8.
KOK08104.
OMAGRTFNWP.
OrthoDBEOG7PS1GM.
PhylomeDBQ8IZT8.
TreeFamTF350755.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.

Gene expression databases

BgeeQ8IZT8.
CleanExHS_HS3ST5.
GenevestigatorQ8IZT8.

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

EvolutionaryTraceQ8IZT8.
GenomeRNAi222537.
NextBio91615.
PROQ8IZT8.
SOURCESearch...

Entry information

Entry nameHS3S5_HUMAN
AccessionPrimary (citable) accession number: Q8IZT8
Secondary accession number(s): A8K1J2, Q52LI2, Q8N285
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 1, 2003
Last modified: April 16, 2014
This is version 101 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM