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Protein

Heparan sulfate glucosamine 3-O-sulfotransferase 3A1

Gene

HS3ST3A1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei166 – 1661Substrate
Binding sitei243 – 2431PAPS
Binding sitei251 – 2511PAPS

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi162 – 1665PAPS
Nucleotide bindingi368 – 3725PAPS

GO - Molecular functioni

  1. [heparan sulfate]-glucosamine 3-sulfotransferase 3 activity Source: UniProtKB-EC
  2. sulfotransferase activity Source: ProtInc

GO - Biological processi

  1. carbohydrate metabolic process Source: Reactome
  2. glycosaminoglycan biosynthetic process Source: Reactome
  3. glycosaminoglycan metabolic process Source: Reactome
  4. pathogenesis Source: Reactome
  5. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BioCyciMetaCyc:HS07937-MONOMER.
ReactomeiREACT_121248. HS-GAG biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:HS3ST3A1
Synonyms:3OST3A1, HS3ST3A
ORF Names:UNQ2551/PRO6180
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:5196. HS3ST3A1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2424CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei25 – 4319Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini44 – 406363LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. Golgi membrane Source: Reactome
  2. integral component of membrane Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi161 – 1611K → A: 99.6% loss of enzymatic activity. 1 Publication
Mutagenesisi162 – 1621K → A: 99.6% loss of enzymatic activity; no HSV1 entry activity. 2 Publications
Mutagenesisi166 – 1661R → E: 99.8% loss of enzymatic activity. 1 Publication
Mutagenesisi170 – 1701E → Q: 17% loss of enzymatic activity. 1 Publication
Mutagenesisi173 – 1731R → S: 44.1% loss of enzymatic activity. 1 Publication
Mutagenesisi182 – 1821G → A: No effect on enzymatic activity. 1 Publication
Mutagenesisi184 – 1841E → Q: 99.9% loss of enzymatic activity. 1 Publication
Mutagenesisi186 – 1861H → F: Abolishes enzymatic activity. 1 Publication
Mutagenesisi189 – 1891D → N: 99.1% loss of enzymatic activity. 1 Publication
Mutagenesisi190 – 1901R → E: 32% loss of enzymatic activity. 1 Publication
Mutagenesisi194 – 1941K → A: 99.5% loss of enzymatic activity. 1 Publication
Mutagenesisi215 – 2151K → A: 99.9% loss of enzymatic activity. 1 Publication
Mutagenesisi218 – 2181S → A: 23.3% loss of enzymatic activity. 1 Publication
Mutagenesisi224 – 2241E → Q: 47.6% loss of enzymatic activity. 1 Publication
Mutagenesisi255 – 2551Q → A: 99.6% loss of enzymatic activity. 1 Publication
Mutagenesisi259 – 2591K → A: 48.3% loss of enzymatic activity. 1 Publication
Mutagenesisi288 – 2881I → A: 65% loss of enzymatic activity. 1 Publication
Mutagenesisi293 – 2931K → A: 33.6% loss of enzymatic activity. 1 Publication
Mutagenesisi362 – 3621H → A: No effect on enzymatic activity. 1 Publication
Mutagenesisi365 – 3651G → A: 43% loss of enzymatic activity. 1 Publication
Mutagenesisi366 – 3661K → A: 99.8% loss of enzymatic activity. 1 Publication
Mutagenesisi368 – 3681K → A: 99.9% loss of enzymatic activity. 1 Publication
Mutagenesisi370 – 3701R → E: 99.2% loss of enzymatic activity. 1 Publication

Organism-specific databases

PharmGKBiPA29469.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 406406Heparan sulfate glucosamine 3-O-sulfotransferase 3A1PRO_0000085217Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi273 – 2731N-linked (GlcNAc...)Sequence Analysis
Glycosylationi344 – 3441N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi351 ↔ 3631 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9Y663.
PRIDEiQ9Y663.

PTM databases

PhosphoSiteiQ9Y663.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ9Y663.
CleanExiHS_HS3ST3A1.
ExpressionAtlasiQ9Y663. baseline and differential.
GenevestigatoriQ9Y663.

Interactioni

Protein-protein interaction databases

BioGridi115280. 1 interaction.
STRINGi9606.ENSP00000284110.

Structurei

Secondary structure

1
406
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi139 – 1479Combined sources
Beta strandi154 – 1596Combined sources
Helixi165 – 1728Combined sources
Beta strandi178 – 1803Combined sources
Turni187 – 1904Combined sources
Helixi192 – 1943Combined sources
Helixi195 – 2028Combined sources
Beta strandi211 – 2155Combined sources
Helixi217 – 2215Combined sources
Helixi225 – 2328Combined sources
Beta strandi237 – 2426Combined sources
Helixi245 – 25915Combined sources
Helixi266 – 2705Combined sources
Helixi284 – 2874Combined sources
Helixi291 – 2988Combined sources
Turni299 – 3013Combined sources
Helixi304 – 3063Combined sources
Beta strandi307 – 3115Combined sources
Helixi312 – 3176Combined sources
Helixi319 – 33012Combined sources
Helixi338 – 3403Combined sources
Beta strandi341 – 3444Combined sources
Turni345 – 3484Combined sources
Beta strandi349 – 3546Combined sources
Helixi377 – 39822Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1T8TX-ray1.85A/B139-406[»]
1T8UX-ray1.95A/B139-406[»]
ProteinModelPortaliQ9Y663.
SMRiQ9Y663. Positions 139-406.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y663.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni184 – 1907Substrate binding
Regioni215 – 2184Substrate binding
Regioni255 – 2595Substrate binding
Regioni283 – 2842Substrate binding
Regioni367 – 3704Substrate binding

Sequence similaritiesi

Belongs to the sulfotransferase 1 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG73846.
GeneTreeiENSGT00760000119023.
HOGENOMiHOG000036663.
HOVERGENiHBG053377.
InParanoidiQ9Y663.
KOiK07809.
OMAiSGERLIM.
OrthoDBiEOG7PS1GM.
PhylomeDBiQ9Y663.
TreeFamiTF350755.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR000863. Sulfotransferase_dom.
[Graphical view]
PfamiPF00685. Sulfotransfer_1. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9Y663-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPPGPASAL STSAEPLSRS IFRKFLLMLC SLLTSLYVFY CLAERCQTLS
60 70 80 90 100
GPVVGLSGGG EEAGAPGGGV LAGGPRELAV WPAAAQRKRL LQLPQWRRRR
110 120 130 140 150
PPAPRDDGEE AAWEEESPGL SGGPGGSGAG STVAEAPPGT LALLLDEGSK
160 170 180 190 200
QLPQAIIIGV KKGGTRALLE FLRVHPDVRA VGAEPHFFDR SYDKGLAWYR
210 220 230 240 250
DLMPRTLDGQ ITMEKTPSYF VTREAPARIS AMSKDTKLIV VVRDPVTRAI
260 270 280 290 300
SDYTQTLSKR PDIPTFESLT FKNRTAGLID TSWSAIQIGI YAKHLEHWLR
310 320 330 340 350
HFPIRQMLFV SGERLISDPA GELGRVQDFL GLKRIITDKH FYFNKTKGFP
360 370 380 390 400
CLKKAEGSSR PHCLGKTKGR THPEIDREVV RRLREFYRPF NLKFYQMTGH

DFGWDG
Length:406
Mass (Da):44,900
Last modified:October 31, 1999 - v1
Checksum:i57B6A0ABC897577A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS11165.1.
RefSeqiNP_006033.1. NM_006042.1.
UniGeneiHs.462270.
Hs.562745.

Genome annotation databases

EnsembliENST00000284110; ENSP00000284110; ENSG00000153976.
GeneIDi9955.
KEGGihsa:9955.
UCSCiuc002gob.1. human.

Polymorphism databases

DMDMi61214551.

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS11165.1.
RefSeqiNP_006033.1. NM_006042.1.
UniGeneiHs.462270.
Hs.562745.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1T8TX-ray1.85A/B139-406[»]
1T8UX-ray1.95A/B139-406[»]
ProteinModelPortaliQ9Y663.
SMRiQ9Y663. Positions 139-406.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115280. 1 interaction.
STRINGi9606.ENSP00000284110.

PTM databases

PhosphoSiteiQ9Y663.

Polymorphism databases

DMDMi61214551.

Proteomic databases

PaxDbiQ9Y663.
PRIDEiQ9Y663.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000284110; ENSP00000284110; ENSG00000153976.
GeneIDi9955.
KEGGihsa:9955.
UCSCiuc002gob.1. human.

Organism-specific databases

CTDi9955.
GeneCardsiGC17M013399.
HGNCiHGNC:5196. HS3ST3A1.
MIMi604057. gene.
neXtProtiNX_Q9Y663.
PharmGKBiPA29469.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG73846.
GeneTreeiENSGT00760000119023.
HOGENOMiHOG000036663.
HOVERGENiHBG053377.
InParanoidiQ9Y663.
KOiK07809.
OMAiSGERLIM.
OrthoDBiEOG7PS1GM.
PhylomeDBiQ9Y663.
TreeFamiTF350755.

Enzyme and pathway databases

BioCyciMetaCyc:HS07937-MONOMER.
ReactomeiREACT_121248. HS-GAG biosynthesis.

Miscellaneous databases

ChiTaRSiHS3ST3A1. human.
EvolutionaryTraceiQ9Y663.
GeneWikiiHS3ST3A1.
GenomeRNAii9955.
NextBioi37564.
PROiQ9Y663.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y663.
CleanExiHS_HS3ST3A1.
ExpressionAtlasiQ9Y663. baseline and differential.
GenevestigatoriQ9Y663.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR000863. Sulfotransferase_dom.
[Graphical view]
PfamiPF00685. Sulfotransfer_1. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Liver.
  2. 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.
    , 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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Spleen.
  4. 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(2003) [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(1998) [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(1998) [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(1998) [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(2003) [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.

Entry informationi

Entry nameiHS3SA_HUMAN
AccessioniPrimary (citable) accession number: Q9Y663
Secondary accession number(s): A8K7N2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 14, 2005
Last sequence update: October 31, 1999
Last modified: March 31, 2015
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.