HS3SA_MOUSE
ID HS3SA_MOUSE Reviewed; 393 AA.
AC Q8BKN6;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Heparan sulfate glucosamine 3-O-sulfotransferase 3A1;
DE EC=2.8.2.23 {ECO:0000250|UniProtKB:Q9Y663};
DE AltName: Full=Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 3A1;
DE Short=Heparan sulfate 3-O-sulfotransferase 3A1;
GN Name=Hs3st3a1; Synonyms=3ost3a1, Hs3st3a;
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].
RC STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
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).
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
CC sulfate. Catalyzes the O-sulfation of glucosamine in IdoUA2S-GlcNS and
CC also in IdoUA2S-GlcNH2. Unlike HS3ST1/3-OST-1, does not convert non-
CC anticoagulant heparan sulfate to anticoagulant heparan sulfate (By
CC similarity). {ECO:0000250|UniProtKB:Q9Y663}.
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:0000250|UniProtKB:Q9Y663};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR EMBL; AK051284; BAC34592.1; -; mRNA.
DR EMBL; AL646051; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL672141; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS24840.1; -.
DR RefSeq; NP_849201.1; NM_178870.5.
DR AlphaFoldDB; Q8BKN6; -.
DR SMR; Q8BKN6; -.
DR STRING; 10090.ENSMUSP00000055930; -.
DR GlyGen; Q8BKN6; 2 sites.
DR iPTMnet; Q8BKN6; -.
DR PhosphoSitePlus; Q8BKN6; -.
DR PaxDb; Q8BKN6; -.
DR PRIDE; Q8BKN6; -.
DR ProteomicsDB; 267165; -.
DR Antibodypedia; 25095; 42 antibodies from 11 providers.
DR DNASU; 15478; -.
DR Ensembl; ENSMUST00000058652; ENSMUSP00000055930; ENSMUSG00000047759.
DR GeneID; 15478; -.
DR KEGG; mmu:15478; -.
DR UCSC; uc007jkr.1; mouse.
DR CTD; 9955; -.
DR MGI; MGI:1333861; Hs3st3a1.
DR VEuPathDB; HostDB:ENSMUSG00000047759; -.
DR eggNOG; KOG3704; Eukaryota.
DR GeneTree; ENSGT00940000162249; -.
DR HOGENOM; CLU_017703_0_1_1; -.
DR InParanoid; Q8BKN6; -.
DR OMA; HFFDHHY; -.
DR OrthoDB; 712400at2759; -.
DR PhylomeDB; Q8BKN6; -.
DR TreeFam; TF350755; -.
DR Reactome; R-MMU-2022928; HS-GAG biosynthesis.
DR BioGRID-ORCS; 15478; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Hs3st3a1; mouse.
DR PRO; PR:Q8BKN6; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8BKN6; protein.
DR Bgee; ENSMUSG00000047759; Expressed in mesenchyme of handplate and 128 other tissues.
DR ExpressionAtlas; Q8BKN6; baseline and differential.
DR Genevisible; Q8BKN6; 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:0001658; P:branching involved in ureteric bud morphogenesis; IGI: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 Disulfide bond; Glycoprotein; Golgi apparatus; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..393
FT /note="Heparan sulfate glucosamine 3-O-sulfotransferase
FT 3A1"
FT /id="PRO_0000085218"
FT TOPO_DOM 1..24
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 25..43
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..393
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 85..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 149..153
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:Q9Y663"
FT BINDING 171..177
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y663"
FT BINDING 202..205
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y663"
FT BINDING 230
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:Q9Y663"
FT BINDING 238
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:Q9Y663"
FT BINDING 270..271
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y663"
FT BINDING 355..359
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:Q9Y663"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 338..350
FT /evidence="ECO:0000250|UniProtKB:Q9Y663"
SQ SEQUENCE 393 AA; 43483 MW; 0B3EFF6EBDB80412 CRC64;
MAPSGPTGAQ PSPAEPLSRS IFRKFLLMLC SLLTSLYVFY CLAERCPPGS GPVAGVPGRG
VPAGPRELAM WPAGAPRKRL LQLRQRRRRG RSGPGDSSDQ EEQSPGLAAA PGGSGAGSSV
AEAQPGTLAL LLDEGSKQLP QAIIIGVKKG GTRALLEFLR VHPDVRAVGA EPHFFDRSYH
KGLAWYRDLM PRTLEGQITM EKTPSYFVTR EAPARISAMS KDTKLIVVVR DPVTRAISDY
TQTLSKRPDI PSFESLTFRN RSAGLIDTSW SAIQIGLYAK HLEPWLRHFP LGQMLFVSGE
RLVSDPAGEL RRVQDFLGLK RIITDKHFYF NQTKGFPCLK KAEGSGKPHC LGKTKGRAHP
TIAREVLRQL RDFYRPFNRK FYQMTGRDFG WDG
