HS3S2_MOUSE
ID HS3S2_MOUSE Reviewed; 367 AA.
AC Q673U1; Q8BLP1; Q8C055;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Heparan sulfate glucosamine 3-O-sulfotransferase 2;
DE EC=2.8.2.29 {ECO:0000250|UniProtKB:Q9Y278};
DE AltName: Full=Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 2;
DE Short=Heparan sulfate 3-O-sulfotransferase 2;
GN Name=Hs3st2; Synonyms=3ost2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 214-367 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain cortex, and Olfactory bulb;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 40-324 (ISOFORM 1).
RC STRAIN=BALB/cJ;
RA Lawrence R., Yabe T., Hajmohammadi S., Rhodes J., McNeely M., Liu J.,
RA Lamperti E.D., Toselli P.A., Spear P.G., Rosenberg R.D., Shworak N.W.;
RT "Neuronal 3-O-sulfotransferases exhibit trigeminal ganglion expression,
RT confer entry of HSV-1, and may explain disease patterns.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate
CC (PAPS) to catalyze the transfer of a sulfo group to an N-unsubstituted
CC glucosamine linked to a 2-O-sulfo iduronic acid unit on heparan sulfate
CC (By similarity). Catalyzes the O-sulfation of glucosamine in GlcA2S-
CC GlcNS (By similarity). Unlike HS3ST1/3-OST-1, does not convert non-
CC anticoagulant heparan sulfate to anticoagulant heparan sulfate (By
CC similarity). {ECO:0000250|UniProtKB:Q9Y278}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + alpha-D-glucosaminyl-[heparan
CC sulfate](n) = 3-sulfo-alpha-D-glucosaminyl-[heparan sulfate](n) +
CC adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:15461, Rhea:RHEA-
CC COMP:9830, Rhea:RHEA-COMP:9831, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:58388, ChEBI:CHEBI:70975; EC=2.8.2.29;
CC Evidence={ECO:0000250|UniProtKB:Q9Y278};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q673U1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q673U1-2; Sequence=VSP_013179, VSP_013180, VSP_013181,
CC VSP_013182;
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR EMBL; AK032292; BAC27796.1; -; mRNA.
DR EMBL; AK043969; BAC31718.1; -; mRNA.
DR EMBL; AC098715; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC125331; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY533705; AAT01565.1; -; mRNA.
DR CCDS; CCDS40115.1; -. [Q673U1-1]
DR RefSeq; NP_001074796.1; NM_001081327.1. [Q673U1-1]
DR AlphaFoldDB; Q673U1; -.
DR SMR; Q673U1; -.
DR STRING; 10090.ENSMUSP00000081678; -.
DR GlyGen; Q673U1; 4 sites.
DR iPTMnet; Q673U1; -.
DR PhosphoSitePlus; Q673U1; -.
DR PaxDb; Q673U1; -.
DR PRIDE; Q673U1; -.
DR ProteomicsDB; 267062; -. [Q673U1-1]
DR Antibodypedia; 2393; 94 antibodies from 17 providers.
DR DNASU; 195646; -.
DR Ensembl; ENSMUST00000084628; ENSMUSP00000081678; ENSMUSG00000046321. [Q673U1-1]
DR Ensembl; ENSMUST00000206880; ENSMUSP00000146027; ENSMUSG00000046321. [Q673U1-2]
DR GeneID; 195646; -.
DR KEGG; mmu:195646; -.
DR UCSC; uc009jnq.1; mouse. [Q673U1-2]
DR UCSC; uc009jnr.1; mouse. [Q673U1-1]
DR CTD; 9956; -.
DR MGI; MGI:1333802; Hs3st2.
DR VEuPathDB; HostDB:ENSMUSG00000046321; -.
DR eggNOG; KOG3704; Eukaryota.
DR GeneTree; ENSGT00940000160498; -.
DR HOGENOM; CLU_017703_0_1_1; -.
DR InParanoid; Q673U1; -.
DR OMA; NIIFYRG; -.
DR OrthoDB; 712400at2759; -.
DR PhylomeDB; Q673U1; -.
DR TreeFam; TF350755; -.
DR Reactome; R-MMU-2022928; HS-GAG biosynthesis.
DR BioGRID-ORCS; 195646; 1 hit in 71 CRISPR screens.
DR PRO; PR:Q673U1; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q673U1; protein.
DR Bgee; ENSMUSG00000046321; Expressed in lumbar dorsal root ganglion and 93 other tissues.
DR Genevisible; Q673U1; MM.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008467; F:[heparan sulfate]-glucosamine 3-sulfotransferase 1 activity; ISS:UniProtKB.
DR GO; GO:0033871; F:[heparan sulfate]-glucosamine 3-sulfotransferase 2 activity; IEA:UniProtKB-EC.
DR GO; GO:0007623; P:circadian rhythm; ISO:MGI.
DR GO; GO:0006024; P:glycosaminoglycan biosynthetic process; ISS:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR037359; NST/OST.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000863; Sulfotransferase_dom.
DR PANTHER; PTHR10605; PTHR10605; 1.
DR Pfam; PF00685; Sulfotransfer_1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Golgi apparatus;
KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..367
FT /note="Heparan sulfate glucosamine 3-O-sulfotransferase 2"
FT /id="PRO_0000085215"
FT TOPO_DOM 1..19
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 20..39
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 40..367
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 66..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..90
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 124..128
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:Q9Y663"
FT BINDING 146..152
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y663"
FT BINDING 177..180
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y663"
FT BINDING 205
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:Q9Y663"
FT BINDING 213
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:Q9Y663"
FT BINDING 245..246
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y663"
FT BINDING 330..334
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:Q9Y663"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 313..325
FT /evidence="ECO:0000250|UniProtKB:Q9Y663"
FT VAR_SEQ 1..33
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013179"
FT VAR_SEQ 34..36
FT /note="CYS -> MCG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013180"
FT VAR_SEQ 162..209
FT /note="RSLMPRTLETQITLEKTPSYFVTQEAPRRIFNMSRDTKLIVVVRNPVT ->
FT SVGVFLGLCKTSRNRICPRGNALSKTERGKHRMKSITLSSSWKSVTHL (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013181"
FT VAR_SEQ 210..367
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013182"
SQ SEQUENCE 367 AA; 41378 MW; 774E8E32C1C4588D CRC64;
MAYRVLGRAG PPQPRRARRL LFAFTLSLSC TYLCYSFLCC CDGLGQSRLL GAPRCLRGPS
ASGQKLLAKS RPCDPPGPTP SEPSAPSAPA AAAPAPRLSG SNHSGSPKPG TKRLPQALIV
GVKKGGTRAV LEFIRVHPDV RALGTEPHFF DRNYGRGLDW YRSLMPRTLE TQITLEKTPS
YFVTQEAPRR IFNMSRDTKL IVVVRNPVTR AISDYTQTLS KKPDIPTFEG LSFRNRSLGL
VDVSWNAIRI GMYALHLESW LRYFPLAQIH FVSGERLITD PAGEMGRIQD FLGIKRFITD
KHFYFNKTKG FPCLKKPEST LLPRCLGKSK GRTHVQIDPE VIDQLREFYR PYNIKFYETV
GQDFRWE
