Full text data of HS3ST2
HS3ST2
(3OST2)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Heparan sulfate glucosamine 3-O-sulfotransferase 2; 2.8.2.29 (Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 2; 3-OST-2; Heparan sulfate 3-O-sulfotransferase 2; h3-OST-2)
Heparan sulfate glucosamine 3-O-sulfotransferase 2; 2.8.2.29 (Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 2; 3-OST-2; Heparan sulfate 3-O-sulfotransferase 2; h3-OST-2)
hRBCD
IPI00001856
IPI00001856 Annexin A11 protein Annexin A11 protein membrane n/a 1 n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 1 n/a likely membrane bound and cytoskeleton n/a expected molecular weight found in band between 98-188 kDa together with ubiquitin
IPI00001856 Annexin A11 protein Annexin A11 protein membrane n/a 1 n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 1 n/a likely membrane bound and cytoskeleton n/a expected molecular weight found in band between 98-188 kDa together with ubiquitin
UniProt
Q9Y278
ID HS3S2_HUMAN Reviewed; 367 AA.
AC Q9Y278; Q52LZ1;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1999, sequence version 1.
DT 22-JAN-2014, entry version 104.
DE RecName: Full=Heparan sulfate glucosamine 3-O-sulfotransferase 2;
DE EC=2.8.2.29;
DE AltName: Full=Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 2;
DE Short=3-OST-2;
DE Short=Heparan sulfate 3-O-sulfotransferase 2;
DE Short=h3-OST-2;
GN Name=HS3ST2; Synonyms=3OST2; ORFNames=UNQ2442/PRO5004;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9988767; DOI=10.1074/jbc.274.8.5170;
RA Shworak N.W., Liu J., Petros L.M., Zhang L., Kobayashi M.,
RA Copeland N.G., Jenkins N.A., Rosenberg R.D.;
RT "Multiple isoforms of heparan sulfate D-glucosaminyl 3-O-
RT sulfotransferase. Isolation, characterization, and expression of human
RT cDNAs and identification of distinct genomic loci.";
RL J. Biol. Chem. 274:5170-5184(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale
RT effort to identify novel human secreted and transmembrane proteins: a
RT bioinformatics assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP CHARACTERIZATION.
RX PubMed=9988768; DOI=10.1074/jbc.274.8.5185;
RA Liu J., Shworak N.W., Sinay P., Schwartz J.J., Zhang L.,
RA Fritze L.M.S., Rosenberg R.D.;
RT "Expression of heparan sulfate D-glucosaminyl 3-O-sulfotransferase
RT isoforms reveals novel substrate specificities.";
RL J. Biol. Chem. 274:5185-5192(1999).
CC -!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl
CC sulfate (PAPS) to catalyze the transfer of a sulfo group to an N-
CC unsubstituted glucosamine linked to a 2-O-sulfo iduronic acid unit
CC on heparan sulfate. Catalyzes the O-sulfation of glucosamine in
CC GlcA2S-GlcNS. Unlike 3-OST-1, does not convert non-anticoagulant
CC heparan sulfate to anticoagulant heparan sulfate.
CC -!- CATALYTIC ACTIVITY: 3'-phosphoadenylyl sulfate + [heparan
CC sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan
CC sulfate]-glucosamine 3-sulfate.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type
CC II membrane protein (Probable).
CC -!- TISSUE SPECIFICITY: Highly expressed in the brain and weakly
CC expressed in the heart, placenta, lung and skeletal muscle.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family.
CC -!- WEB RESOURCE: Name=GGDB; Note=GlycoGene database;
CC URL="http://riodb.ibase.aist.go.jp/rcmg/ggdb/";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF105374; AAD30206.1; -; mRNA.
DR EMBL; AF105375; AAD30207.1; -; mRNA.
DR EMBL; AY359095; AAQ89453.1; -; mRNA.
DR EMBL; BC093734; AAH93734.1; -; mRNA.
DR EMBL; BC093736; AAH93736.1; -; mRNA.
DR RefSeq; NP_006034.1; NM_006043.1.
DR UniGene; Hs.115830; -.
DR UniGene; Hs.733610; -.
DR ProteinModelPortal; Q9Y278; -.
DR SMR; Q9Y278; 110-367.
DR STRING; 9606.ENSP00000261374; -.
DR PhosphoSite; Q9Y278; -.
DR DMDM; 61214416; -.
DR PaxDb; Q9Y278; -.
DR PRIDE; Q9Y278; -.
DR Ensembl; ENST00000261374; ENSP00000261374; ENSG00000122254.
DR GeneID; 9956; -.
DR KEGG; hsa:9956; -.
DR UCSC; uc002dli.3; human.
DR CTD; 9956; -.
DR GeneCards; GC16P022732; -.
DR HGNC; HGNC:5195; HS3ST2.
DR HPA; HPA017736; -.
DR MIM; 604056; gene.
DR neXtProt; NX_Q9Y278; -.
DR PharmGKB; PA29468; -.
DR eggNOG; NOG326911; -.
DR HOGENOM; HOG000036663; -.
DR HOVERGEN; HBG053377; -.
DR InParanoid; Q9Y278; -.
DR KO; K07808; -.
DR OMA; CYSLLCC; -.
DR OrthoDB; EOG7PS1GM; -.
DR PhylomeDB; Q9Y278; -.
DR BioCyc; MetaCyc:HS04557-MONOMER; -.
DR BRENDA; 2.8.2.29; 2681.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_116125; Disease.
DR GeneWiki; HS3ST2; -.
DR GenomeRNAi; 9956; -.
DR NextBio; 37568; -.
DR PRO; PR:Q9Y278; -.
DR ArrayExpress; Q9Y278; -.
DR Bgee; Q9Y278; -.
DR CleanEx; HS_HS3ST2; -.
DR Genevestigator; Q9Y278; -.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral to membrane; TAS:ProtInc.
DR GO; GO:0033871; F:[heparan sulfate]-glucosamine 3-sulfotransferase 2 activity; IEA:UniProtKB-EC.
DR GO; GO:0008146; F:sulfotransferase activity; TAS:ProtInc.
DR GO; GO:0005975; P:carbohydrate metabolic process; TAS:Reactome.
DR GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
DR GO; GO:0006024; P:glycosaminoglycan biosynthetic process; TAS:Reactome.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000863; Sulfotransferase_dom.
DR Pfam; PF00685; Sulfotransfer_1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Disulfide bond; Glycoprotein; Golgi apparatus;
KW Membrane; Polymorphism; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1 367 Heparan sulfate glucosamine 3-O-
FT sulfotransferase 2.
FT /FTId=PRO_0000085214.
FT TOPO_DOM 1 19 Cytoplasmic (Potential).
FT TRANSMEM 20 39 Helical; Signal-anchor for type II
FT membrane protein; (Potential).
FT TOPO_DOM 40 367 Lumenal (Potential).
FT NP_BIND 124 128 PAPS (By similarity).
FT NP_BIND 330 334 PAPS (By similarity).
FT REGION 146 152 Substrate binding (By similarity).
FT REGION 177 180 Substrate binding (By similarity).
FT REGION 245 246 Substrate binding (By similarity).
FT BINDING 205 205 PAPS (By similarity).
FT BINDING 213 213 PAPS (By similarity).
FT CARBOHYD 102 102 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 193 193 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 235 235 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 306 306 N-linked (GlcNAc...) (Potential).
FT DISULFID 313 325 By similarity.
FT VARIANT 339 339 P -> A (in dbSNP:rs17725080).
FT /FTId=VAR_052530.
SQ SEQUENCE 367 AA; 41501 MW; F63EACDD4721607C CRC64;
MAYRVLGRAG PPQPRRARRL LFAFTLSLSC TYLCYSFLCC CDDLGRSRLL GAPRCLRGPS
AGGQKLLQKS RPCDPSGPTP SEPSAPSAPA AAVPAPRLSG SNHSGSPKLG TKRLPQALIV
GVKKGGTRAV LEFIRVHPDV RALGTEPHFF DRNYGRGLDW YRSLMPRTLE SQITLEKTPS
YFVTQEAPRR IFNMSRDTKL IVVVRNPVTR AISDYTQTLS KKPDIPTFEG LSFRNRTLGL
VDVSWNAIRI GMYVLHLESW LQYFPLAQIH FVSGERLITD PAGEMGRVQD FLGIKRFITD
KHFYFNKTKG FPCLKKTESS LLPRCLGKSK GRTHVQIDPE VIDQLREFYR PYNIKFYETV
GQDFRWE
//
ID HS3S2_HUMAN Reviewed; 367 AA.
AC Q9Y278; Q52LZ1;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1999, sequence version 1.
DT 22-JAN-2014, entry version 104.
DE RecName: Full=Heparan sulfate glucosamine 3-O-sulfotransferase 2;
DE EC=2.8.2.29;
DE AltName: Full=Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 2;
DE Short=3-OST-2;
DE Short=Heparan sulfate 3-O-sulfotransferase 2;
DE Short=h3-OST-2;
GN Name=HS3ST2; Synonyms=3OST2; ORFNames=UNQ2442/PRO5004;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9988767; DOI=10.1074/jbc.274.8.5170;
RA Shworak N.W., Liu J., Petros L.M., Zhang L., Kobayashi M.,
RA Copeland N.G., Jenkins N.A., Rosenberg R.D.;
RT "Multiple isoforms of heparan sulfate D-glucosaminyl 3-O-
RT sulfotransferase. Isolation, characterization, and expression of human
RT cDNAs and identification of distinct genomic loci.";
RL J. Biol. Chem. 274:5170-5184(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale
RT effort to identify novel human secreted and transmembrane proteins: a
RT bioinformatics assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP CHARACTERIZATION.
RX PubMed=9988768; DOI=10.1074/jbc.274.8.5185;
RA Liu J., Shworak N.W., Sinay P., Schwartz J.J., Zhang L.,
RA Fritze L.M.S., Rosenberg R.D.;
RT "Expression of heparan sulfate D-glucosaminyl 3-O-sulfotransferase
RT isoforms reveals novel substrate specificities.";
RL J. Biol. Chem. 274:5185-5192(1999).
CC -!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl
CC sulfate (PAPS) to catalyze the transfer of a sulfo group to an N-
CC unsubstituted glucosamine linked to a 2-O-sulfo iduronic acid unit
CC on heparan sulfate. Catalyzes the O-sulfation of glucosamine in
CC GlcA2S-GlcNS. Unlike 3-OST-1, does not convert non-anticoagulant
CC heparan sulfate to anticoagulant heparan sulfate.
CC -!- CATALYTIC ACTIVITY: 3'-phosphoadenylyl sulfate + [heparan
CC sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan
CC sulfate]-glucosamine 3-sulfate.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type
CC II membrane protein (Probable).
CC -!- TISSUE SPECIFICITY: Highly expressed in the brain and weakly
CC expressed in the heart, placenta, lung and skeletal muscle.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family.
CC -!- WEB RESOURCE: Name=GGDB; Note=GlycoGene database;
CC URL="http://riodb.ibase.aist.go.jp/rcmg/ggdb/";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF105374; AAD30206.1; -; mRNA.
DR EMBL; AF105375; AAD30207.1; -; mRNA.
DR EMBL; AY359095; AAQ89453.1; -; mRNA.
DR EMBL; BC093734; AAH93734.1; -; mRNA.
DR EMBL; BC093736; AAH93736.1; -; mRNA.
DR RefSeq; NP_006034.1; NM_006043.1.
DR UniGene; Hs.115830; -.
DR UniGene; Hs.733610; -.
DR ProteinModelPortal; Q9Y278; -.
DR SMR; Q9Y278; 110-367.
DR STRING; 9606.ENSP00000261374; -.
DR PhosphoSite; Q9Y278; -.
DR DMDM; 61214416; -.
DR PaxDb; Q9Y278; -.
DR PRIDE; Q9Y278; -.
DR Ensembl; ENST00000261374; ENSP00000261374; ENSG00000122254.
DR GeneID; 9956; -.
DR KEGG; hsa:9956; -.
DR UCSC; uc002dli.3; human.
DR CTD; 9956; -.
DR GeneCards; GC16P022732; -.
DR HGNC; HGNC:5195; HS3ST2.
DR HPA; HPA017736; -.
DR MIM; 604056; gene.
DR neXtProt; NX_Q9Y278; -.
DR PharmGKB; PA29468; -.
DR eggNOG; NOG326911; -.
DR HOGENOM; HOG000036663; -.
DR HOVERGEN; HBG053377; -.
DR InParanoid; Q9Y278; -.
DR KO; K07808; -.
DR OMA; CYSLLCC; -.
DR OrthoDB; EOG7PS1GM; -.
DR PhylomeDB; Q9Y278; -.
DR BioCyc; MetaCyc:HS04557-MONOMER; -.
DR BRENDA; 2.8.2.29; 2681.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_116125; Disease.
DR GeneWiki; HS3ST2; -.
DR GenomeRNAi; 9956; -.
DR NextBio; 37568; -.
DR PRO; PR:Q9Y278; -.
DR ArrayExpress; Q9Y278; -.
DR Bgee; Q9Y278; -.
DR CleanEx; HS_HS3ST2; -.
DR Genevestigator; Q9Y278; -.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral to membrane; TAS:ProtInc.
DR GO; GO:0033871; F:[heparan sulfate]-glucosamine 3-sulfotransferase 2 activity; IEA:UniProtKB-EC.
DR GO; GO:0008146; F:sulfotransferase activity; TAS:ProtInc.
DR GO; GO:0005975; P:carbohydrate metabolic process; TAS:Reactome.
DR GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
DR GO; GO:0006024; P:glycosaminoglycan biosynthetic process; TAS:Reactome.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000863; Sulfotransferase_dom.
DR Pfam; PF00685; Sulfotransfer_1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Disulfide bond; Glycoprotein; Golgi apparatus;
KW Membrane; Polymorphism; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1 367 Heparan sulfate glucosamine 3-O-
FT sulfotransferase 2.
FT /FTId=PRO_0000085214.
FT TOPO_DOM 1 19 Cytoplasmic (Potential).
FT TRANSMEM 20 39 Helical; Signal-anchor for type II
FT membrane protein; (Potential).
FT TOPO_DOM 40 367 Lumenal (Potential).
FT NP_BIND 124 128 PAPS (By similarity).
FT NP_BIND 330 334 PAPS (By similarity).
FT REGION 146 152 Substrate binding (By similarity).
FT REGION 177 180 Substrate binding (By similarity).
FT REGION 245 246 Substrate binding (By similarity).
FT BINDING 205 205 PAPS (By similarity).
FT BINDING 213 213 PAPS (By similarity).
FT CARBOHYD 102 102 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 193 193 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 235 235 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 306 306 N-linked (GlcNAc...) (Potential).
FT DISULFID 313 325 By similarity.
FT VARIANT 339 339 P -> A (in dbSNP:rs17725080).
FT /FTId=VAR_052530.
SQ SEQUENCE 367 AA; 41501 MW; F63EACDD4721607C CRC64;
MAYRVLGRAG PPQPRRARRL LFAFTLSLSC TYLCYSFLCC CDDLGRSRLL GAPRCLRGPS
AGGQKLLQKS RPCDPSGPTP SEPSAPSAPA AAVPAPRLSG SNHSGSPKLG TKRLPQALIV
GVKKGGTRAV LEFIRVHPDV RALGTEPHFF DRNYGRGLDW YRSLMPRTLE SQITLEKTPS
YFVTQEAPRR IFNMSRDTKL IVVVRNPVTR AISDYTQTLS KKPDIPTFEG LSFRNRTLGL
VDVSWNAIRI GMYVLHLESW LQYFPLAQIH FVSGERLITD PAGEMGRVQD FLGIKRFITD
KHFYFNKTKG FPCLKKTESS LLPRCLGKSK GRTHVQIDPE VIDQLREFYR PYNIKFYETV
GQDFRWE
//
MIM
604056
*RECORD*
*FIELD* NO
604056
*FIELD* TI
*604056 HEPARAN SULFATE D-GLUCOSAMINYL 3-O-SULFOTRANSFERASE 2; HS3ST2
;;3OST2
*FIELD* TX
read moreHeparan sulfate proteoglycans are hybrid molecules composed of a protein
core attached to 1 or more linear heparan sulfate glycosaminoglycan
chains. The order and ring positions of sulfate groups along the length
of the chain create distinct oligosaccharide sequences and define the
specificity of any given heparan sulfate-protein interaction and the
corresponding biologic activity. Heparan sulfate biosynthetic enzymes
are key components in generating regions of defined monosaccharide
sequence. For example, the enzyme heparan sulfate D-glucosaminyl
3-O-sulfotransferase-1 (3OST1; 603244) controls the rate of production
of the critical active site 3-O-sulfate group on the antithrombin
binding site of anticoagulant heparan sulfate.
By searching an EST database for sequences related to the
sulfotransferase domain of 3OST1, Shworak et al. (1999) identified
partial cDNAs from the 3OST2, 3OST3A1 (604057), and 3OST4 (604059)
genes. They used the partial cDNAs as probes and recovered additional
clones corresponding to these genes and to 3OST3B1 (604058). The 3OST2
gene encodes a predicted 367-amino acid protein that, like 3OST3A1 and
3OST3B1, is a predicted type II integral membrane protein. These 3
enzymes contain a positively charged N-terminal domain, a transmembrane
domain, a region termed the SPLAG domain because it is rich in serine,
proline, leucine, alanine, and glycine, and a C-terminal putative
sulfotransferase domain. Although they share a similar regional
structure, the only significant sequence homology between these 3OST
proteins occurs in the sulfotransferase domains. Northern blot analysis
revealed that the 3OST2 and 3OST4 genes were expressed predominantly in
brain, while the 3OST3 gene exhibited more widespread expression. In a
companion paper, Liu et al. (1999) demonstrated that the 3OST1, 3OST2,
and 3OST3 isoforms each generate unique 3-O-sulfated structures. Shworak
et al. (1999) stated that the isoforms with different sulfotransferase
domains differentially place the rare 3-O-sulfate group in distinct
sequence contexts, presumably to regulate discrete biologic activities.
This capacity of the sulfotransferase domain to generate distinct
sequences may in turn be modulated by the unique N-terminal domains of
the proteins.
By inclusion within mapped clones, Shworak et al. (1999) mapped the
3OST2 gene to 16p12, near the 3OST4 gene at 16p11.2. Using interspecific
backcross analysis, they mapped the mouse 3Ost2 and 3Ost4 genes to the
distal region of chromosome 7, in a region sharing homology of synteny
with human chromosome 16p.
*FIELD* RF
1. Liu, J.; Shworak, N. W.; Sinay, P.; Schwartz, J. J.; Zhang, L.;
Fritze, L. M.; Rosenberg, R. D.: Expression of heparan sulfate D-glucosaminyl
3-O-sulfotransferase isoforms reveals novel substrate specificities. J.
Biol. Chem. 274: 5185-5192, 1999.
2. Shworak, N. W.; Liu, J.; Petros, L. M.; Zhang, L.; Kobayashi, M.;
Copeland, N. G.; Jenkins, N. A.; Rosenberg, R. D.: Multiple isoforms
of heparan sulfate D-glucosaminyl 3-O-sulfotransferase: isolation,
characterization, and expression of human cDNAs and identification
of distinct genomic loci. J. Biol. Chem. 274: 5170-5184, 1999.
*FIELD* CD
Rebekah S. Rasooly: 7/23/1999
*FIELD* ED
mgross: 07/23/1999
*RECORD*
*FIELD* NO
604056
*FIELD* TI
*604056 HEPARAN SULFATE D-GLUCOSAMINYL 3-O-SULFOTRANSFERASE 2; HS3ST2
;;3OST2
*FIELD* TX
read moreHeparan sulfate proteoglycans are hybrid molecules composed of a protein
core attached to 1 or more linear heparan sulfate glycosaminoglycan
chains. The order and ring positions of sulfate groups along the length
of the chain create distinct oligosaccharide sequences and define the
specificity of any given heparan sulfate-protein interaction and the
corresponding biologic activity. Heparan sulfate biosynthetic enzymes
are key components in generating regions of defined monosaccharide
sequence. For example, the enzyme heparan sulfate D-glucosaminyl
3-O-sulfotransferase-1 (3OST1; 603244) controls the rate of production
of the critical active site 3-O-sulfate group on the antithrombin
binding site of anticoagulant heparan sulfate.
By searching an EST database for sequences related to the
sulfotransferase domain of 3OST1, Shworak et al. (1999) identified
partial cDNAs from the 3OST2, 3OST3A1 (604057), and 3OST4 (604059)
genes. They used the partial cDNAs as probes and recovered additional
clones corresponding to these genes and to 3OST3B1 (604058). The 3OST2
gene encodes a predicted 367-amino acid protein that, like 3OST3A1 and
3OST3B1, is a predicted type II integral membrane protein. These 3
enzymes contain a positively charged N-terminal domain, a transmembrane
domain, a region termed the SPLAG domain because it is rich in serine,
proline, leucine, alanine, and glycine, and a C-terminal putative
sulfotransferase domain. Although they share a similar regional
structure, the only significant sequence homology between these 3OST
proteins occurs in the sulfotransferase domains. Northern blot analysis
revealed that the 3OST2 and 3OST4 genes were expressed predominantly in
brain, while the 3OST3 gene exhibited more widespread expression. In a
companion paper, Liu et al. (1999) demonstrated that the 3OST1, 3OST2,
and 3OST3 isoforms each generate unique 3-O-sulfated structures. Shworak
et al. (1999) stated that the isoforms with different sulfotransferase
domains differentially place the rare 3-O-sulfate group in distinct
sequence contexts, presumably to regulate discrete biologic activities.
This capacity of the sulfotransferase domain to generate distinct
sequences may in turn be modulated by the unique N-terminal domains of
the proteins.
By inclusion within mapped clones, Shworak et al. (1999) mapped the
3OST2 gene to 16p12, near the 3OST4 gene at 16p11.2. Using interspecific
backcross analysis, they mapped the mouse 3Ost2 and 3Ost4 genes to the
distal region of chromosome 7, in a region sharing homology of synteny
with human chromosome 16p.
*FIELD* RF
1. Liu, J.; Shworak, N. W.; Sinay, P.; Schwartz, J. J.; Zhang, L.;
Fritze, L. M.; Rosenberg, R. D.: Expression of heparan sulfate D-glucosaminyl
3-O-sulfotransferase isoforms reveals novel substrate specificities. J.
Biol. Chem. 274: 5185-5192, 1999.
2. Shworak, N. W.; Liu, J.; Petros, L. M.; Zhang, L.; Kobayashi, M.;
Copeland, N. G.; Jenkins, N. A.; Rosenberg, R. D.: Multiple isoforms
of heparan sulfate D-glucosaminyl 3-O-sulfotransferase: isolation,
characterization, and expression of human cDNAs and identification
of distinct genomic loci. J. Biol. Chem. 274: 5170-5184, 1999.
*FIELD* CD
Rebekah S. Rasooly: 7/23/1999
*FIELD* ED
mgross: 07/23/1999