HS3S1_MOUSE
ID HS3S1_MOUSE Reviewed; 311 AA.
AC O35310;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Heparan sulfate glucosamine 3-O-sulfotransferase 1;
DE EC=2.8.2.23 {ECO:0000269|PubMed:15060080};
DE AltName: Full=Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 1;
DE Short=Heparan sulfate 3-O-sulfotransferase 1;
DE Flags: Precursor;
GN Name=Hs3st1; Synonyms=3ost, 3ost1;
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 [MRNA], PARTIAL PROTEIN SEQUENCE, AND FUNCTION.
RC STRAIN=C3H/An;
RX PubMed=9346953; DOI=10.1074/jbc.272.44.28008;
RA Shworak N.W., Liu J., Fritze L.M.S., Schwartz J.J., Zhang L., Logeart D.,
RA Rosenberg R.D.;
RT "Molecular cloning and expression of mouse and human cDNAs encoding heparan
RT sulfate D-glucosaminyl 3-O-sulfotransferase.";
RL J. Biol. Chem. 272:28008-28019(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=129; TISSUE=Mammary tumor;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP CHARACTERIZATION.
RX PubMed=11006120; DOI=10.1006/bbrc.2000.3453;
RA Hernaiz M., Liu J., Rosenberg R.D., Linhardt R.J.;
RT "Enzymatic modification of heparan sulfate on a biochip promotes its
RT interaction with antithrombin III.";
RL Biochem. Biophys. Res. Commun. 276:292-297(2000).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 74-311 IN COMPLEX WITH PAPS,
RP FUNCTION, CATALYTIC ACTIVITY, DISULFIDE BOND, BINDING SITES, AND
RP MUTAGENESIS OF ARG-67; LYS-68; ARG-72; GLU-76; GLU-88; ASN-89; GLU-90;
RP HIS-92; ASP-95; TRP-96; GLU-98; LYS-123; LYS-132; GLN-163; ARG-197;
RP HIS-271; SER-273; LYS-274 AND ARG-276.
RX PubMed=15060080; DOI=10.1074/jbc.m401089200;
RA Edavettal S.C., Lee K.A., Negishi M., Linhardt R.J., Liu J., Pedersen L.C.;
RT "Crystal structure and mutational analysis of heparan sulfate 3-O-
RT sulfotransferase isoform 1.";
RL J. Biol. Chem. 279:25789-25797(2004).
CC -!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate
CC (PAPS) to catalyze the transfer of a sulfo group to position 3 of
CC glucosamine residues in heparan (PubMed:9346953, PubMed:15060080).
CC Catalyzes the rate limiting step in the biosynthesis of heparan sulfate
CC (HSact) (PubMed:9346953, PubMed:15060080). This modification is a
CC crucial step in the biosynthesis of anticoagulant heparan sulfate as it
CC completes the structure of the antithrombin pentasaccharide binding
CC site (PubMed:9346953, PubMed:15060080). {ECO:0000269|PubMed:15060080,
CC ECO:0000269|PubMed:9346953}.
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=2.8.2.23;
CC Evidence={ECO:0000269|PubMed:15060080};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus lumen {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR EMBL; AF019385; AAB84387.1; -; mRNA.
DR EMBL; AK087753; BAC39991.1; -; mRNA.
DR EMBL; BC009133; AAH09133.1; -; mRNA.
DR CCDS; CCDS19257.1; -.
DR RefSeq; NP_034604.1; NM_010474.2.
DR RefSeq; XP_017176175.1; XM_017320686.1.
DR PDB; 1VKJ; X-ray; 2.50 A; A/B/C=48-311.
DR PDB; 3UAN; X-ray; 1.84 A; A/B=48-311.
DR PDBsum; 1VKJ; -.
DR PDBsum; 3UAN; -.
DR AlphaFoldDB; O35310; -.
DR SMR; O35310; -.
DR STRING; 10090.ENSMUSP00000051055; -.
DR GlyGen; O35310; 4 sites.
DR PhosphoSitePlus; O35310; -.
DR PaxDb; O35310; -.
DR PRIDE; O35310; -.
DR ProteomicsDB; 267061; -.
DR Antibodypedia; 1208; 128 antibodies from 26 providers.
DR DNASU; 15476; -.
DR Ensembl; ENSMUST00000053116; ENSMUSP00000051055; ENSMUSG00000051022.
DR Ensembl; ENSMUST00000117944; ENSMUSP00000113919; ENSMUSG00000051022.
DR GeneID; 15476; -.
DR KEGG; mmu:15476; -.
DR UCSC; uc008xgy.2; mouse.
DR CTD; 9957; -.
DR MGI; MGI:1201606; Hs3st1.
DR VEuPathDB; HostDB:ENSMUSG00000051022; -.
DR eggNOG; KOG3704; Eukaryota.
DR GeneTree; ENSGT00940000160449; -.
DR HOGENOM; CLU_017703_0_0_1; -.
DR InParanoid; O35310; -.
DR OMA; RCLHDSK; -.
DR OrthoDB; 712400at2759; -.
DR PhylomeDB; O35310; -.
DR TreeFam; TF350755; -.
DR BRENDA; 2.8.2.23; 3474.
DR Reactome; R-MMU-2022928; HS-GAG biosynthesis.
DR BioGRID-ORCS; 15476; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Hs3st1; mouse.
DR EvolutionaryTrace; O35310; -.
DR PRO; PR:O35310; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; O35310; protein.
DR Bgee; ENSMUSG00000051022; Expressed in ectoplacental cone and 218 other tissues.
DR ExpressionAtlas; O35310; baseline and differential.
DR Genevisible; O35310; MM.
DR GO; GO:0005796; C:Golgi lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0008467; F:[heparan sulfate]-glucosamine 3-sulfotransferase 1 activity; IDA:UniProtKB.
DR GO; GO:0006024; P:glycosaminoglycan biosynthetic process; IDA: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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Golgi apparatus; Reference proteome; Signal; Transferase.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:9346953"
FT CHAIN 21..311
FT /note="Heparan sulfate glucosamine 3-O-sulfotransferase 1"
FT /id="PRO_0000033452"
FT BINDING 68..72
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000269|PubMed:15060080"
FT BINDING 151
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000269|PubMed:15060080"
FT BINDING 159
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000269|PubMed:15060080"
FT BINDING 259
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000269|PubMed:15060080"
FT BINDING 274..278
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000269|PubMed:15060080"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 260..269
FT /evidence="ECO:0000269|PubMed:15060080"
FT MUTAGEN 67
FT /note="R->E,A: Abolishes the enzymatic activity."
FT /evidence="ECO:0000269|PubMed:15060080"
FT MUTAGEN 68
FT /note="K->A: Abolishes the enzymatic activity."
FT /evidence="ECO:0000269|PubMed:15060080"
FT MUTAGEN 72
FT /note="R->A,E: Abolishes the enzymatic activity."
FT /evidence="ECO:0000269|PubMed:15060080"
FT MUTAGEN 76
FT /note="E->A,Q: Strongly decreases the enzymatic activity."
FT /evidence="ECO:0000269|PubMed:15060080"
FT MUTAGEN 88
FT /note="E->A: Decreases the enzymatic activity."
FT /evidence="ECO:0000269|PubMed:15060080"
FT MUTAGEN 89
FT /note="N->A,D: Decreases the enzymatic activity."
FT /evidence="ECO:0000269|PubMed:15060080"
FT MUTAGEN 90
FT /note="E->Q,A: Abolishes the enzymatic activity."
FT /evidence="ECO:0000269|PubMed:15060080"
FT MUTAGEN 92
FT /note="H->F,A: Abolishes the enzymatic activity."
FT /evidence="ECO:0000269|PubMed:15060080"
FT MUTAGEN 95
FT /note="D->A,N: Abolishes the enzymatic activity."
FT /evidence="ECO:0000269|PubMed:15060080"
FT MUTAGEN 96
FT /note="W->A,F: Decreases the enzymatic activity."
FT /evidence="ECO:0000269|PubMed:15060080"
FT MUTAGEN 98
FT /note="E->A: Decreases the enzymatic activity."
FT /evidence="ECO:0000269|PubMed:15060080"
FT MUTAGEN 123
FT /note="K->A: Abolishes the enzymatic activity."
FT /evidence="ECO:0000269|PubMed:15060080"
FT MUTAGEN 132
FT /note="K->A: Decreases the enzymatic activity."
FT /evidence="ECO:0000269|PubMed:15060080"
FT MUTAGEN 163
FT /note="Q->A: Strongly decreases the enzymatic activity."
FT /evidence="ECO:0000269|PubMed:15060080"
FT MUTAGEN 197
FT /note="R->A: Weakly decrease the enzymatic activity."
FT /evidence="ECO:0000269|PubMed:15060080"
FT MUTAGEN 271
FT /note="H->A: No effect."
FT /evidence="ECO:0000269|PubMed:15060080"
FT MUTAGEN 271
FT /note="H->F: Decreases the enzymatic activity."
FT /evidence="ECO:0000269|PubMed:15060080"
FT MUTAGEN 273
FT /note="S->A: Weakly decrease the enzymatic activity."
FT /evidence="ECO:0000269|PubMed:15060080"
FT MUTAGEN 274
FT /note="K->A: Strongly decrease the enzymatic activity."
FT /evidence="ECO:0000269|PubMed:15060080"
FT MUTAGEN 276
FT /note="R->A: Abolishes the enzymatic activity."
FT /evidence="ECO:0000269|PubMed:15060080"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:3UAN"
FT HELIX 71..78
FT /evidence="ECO:0007829|PDB:3UAN"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:3UAN"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:3UAN"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:3UAN"
FT HELIX 104..109
FT /evidence="ECO:0007829|PDB:3UAN"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:3UAN"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:3UAN"
FT HELIX 133..140
FT /evidence="ECO:0007829|PDB:3UAN"
FT STRAND 145..150
FT /evidence="ECO:0007829|PDB:3UAN"
FT HELIX 153..170
FT /evidence="ECO:0007829|PDB:3UAN"
FT HELIX 178..182
FT /evidence="ECO:0007829|PDB:3UAN"
FT HELIX 193..197
FT /evidence="ECO:0007829|PDB:3UAN"
FT HELIX 200..208
FT /evidence="ECO:0007829|PDB:3UAN"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:3UAN"
FT STRAND 216..220
FT /evidence="ECO:0007829|PDB:3UAN"
FT HELIX 221..226
FT /evidence="ECO:0007829|PDB:3UAN"
FT HELIX 228..238
FT /evidence="ECO:0007829|PDB:3UAN"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:3UAN"
FT STRAND 250..253
FT /evidence="ECO:0007829|PDB:3UAN"
FT TURN 254..257
FT /evidence="ECO:0007829|PDB:3UAN"
FT STRAND 258..263
FT /evidence="ECO:0007829|PDB:3UAN"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:3UAN"
FT HELIX 283..304
FT /evidence="ECO:0007829|PDB:3UAN"
SQ SEQUENCE 311 AA; 35899 MW; 7DCFAC494C838FD7 CRC64;
MTLLLLGAVL LVAQPQLVHS HPAAPGPGLK QQELLRKVII LPEDTGEGTA SNGSTQQLPQ
TIIIGVRKGG TRALLEMLSL HPDVAAAENE VHFFDWEEHY SQGLGWYLTQ MPFSSPHQLT
VEKTPAYFTS PKVPERIHSM NPTIRLLLIL RDPSERVLSD YTQVLYNHLQ KHKPYPPIED
LLMRDGRLNL DYKALNRSLY HAHMLNWLRF FPLGHIHIVD GDRLIRDPFP EIQKVERFLK
LSPQINASNF YFNKTKGFYC LRDSGKDRCL HESKGRAHPQ VDPKLLDKLH EYFHEPNKKF
FKLVGRTFDW H
