HS3S5_MOUSE
ID HS3S5_MOUSE Reviewed; 346 AA.
AC Q8BSL4;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Heparan sulfate glucosamine 3-O-sulfotransferase 5;
DE EC=2.8.2.23;
DE AltName: Full=Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 5;
DE Short=Heparan sulfate 3-O-sulfotransferase 5;
GN Name=Hs3st5; Synonyms=Hs3ost5;
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].
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).
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. Catalyzes the rate limiting step in
CC the biosynthesis of heparan sulfate (HSact). 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. Also generates GlcUA-GlcNS or IdoUA-GlcNS and IdoUA2S-GlcNH2 (By
CC similarity). {ECO:0000250}.
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 -!- 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; AK031910; BAC27601.1; -; mRNA.
DR CCDS; CCDS35881.1; -.
DR RefSeq; NP_001074677.1; NM_001081208.2.
DR RefSeq; NP_001240284.1; NM_001253355.1.
DR RefSeq; NP_001240285.1; NM_001253356.1.
DR RefSeq; XP_006512824.1; XM_006512761.2.
DR AlphaFoldDB; Q8BSL4; -.
DR SMR; Q8BSL4; -.
DR STRING; 10090.ENSMUSP00000060229; -.
DR GlyGen; Q8BSL4; 4 sites.
DR iPTMnet; Q8BSL4; -.
DR PhosphoSitePlus; Q8BSL4; -.
DR PaxDb; Q8BSL4; -.
DR PRIDE; Q8BSL4; -.
DR Antibodypedia; 50950; 42 antibodies from 15 providers.
DR Ensembl; ENSMUST00000058738; ENSMUSP00000060229; ENSMUSG00000044499.
DR Ensembl; ENSMUST00000167191; ENSMUSP00000130778; ENSMUSG00000044499.
DR Ensembl; ENSMUST00000168572; ENSMUSP00000129434; ENSMUSG00000044499.
DR GeneID; 319415; -.
DR KEGG; mmu:319415; -.
DR UCSC; uc007evc.1; mouse.
DR CTD; 222537; -.
DR MGI; MGI:2441996; Hs3st5.
DR VEuPathDB; HostDB:ENSMUSG00000044499; -.
DR eggNOG; KOG3704; Eukaryota.
DR GeneTree; ENSGT00940000158991; -.
DR HOGENOM; CLU_017703_0_0_1; -.
DR InParanoid; Q8BSL4; -.
DR OMA; MHRWLEV; -.
DR OrthoDB; 712400at2759; -.
DR PhylomeDB; Q8BSL4; -.
DR TreeFam; TF350755; -.
DR Reactome; R-MMU-2022928; HS-GAG biosynthesis.
DR BioGRID-ORCS; 319415; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Hs3st5; mouse.
DR PRO; PR:Q8BSL4; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8BSL4; protein.
DR Bgee; ENSMUSG00000044499; Expressed in animal zygote and 91 other tissues.
DR ExpressionAtlas; Q8BSL4; baseline and differential.
DR Genevisible; Q8BSL4; 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:0015015; P:heparan sulfate proteoglycan biosynthetic process, enzymatic modification; ISS:UniProtKB.
DR GO; GO:0050819; P:negative regulation of coagulation; ISO:MGI.
DR GO; GO:0006477; P:protein sulfation; ISO:MGI.
DR GO; GO:0046596; P:regulation of viral entry into host cell; 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..346
FT /note="Heparan sulfate glucosamine 3-O-sulfotransferase 5"
FT /id="PRO_0000085223"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..32
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..346
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT BINDING 100..104
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 122..128
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 155..158
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 183
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 226..227
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 293
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 309..313
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 294..304
FT /evidence="ECO:0000250"
SQ SEQUENCE 346 AA; 40471 MW; 0A66AF72E495753B CRC64;
MLFKQQVWLR QKLLVLGSLA VGSLLYLVAR VGSLDRLQPI CPVESRFGGA HNQAELPLRA
LQFKRGLLHE FRKGNSSKEQ VHLHDLVQQL PKAIIIGVRK GGTRALLEML NLHPAVVKAS
QEIHFFDNDE NYAKGIEWYR KKMPFSYPQQ ITIEKSPAYF ITEEVPERIY KMNSSIKLLI
IVREPTTRAI SDYTQVLEGK ERKNKTYYKF EKLAIDPNTC EVNTKYKAVR TSIYTKHLER
WLKYFPIEQF HIVDGDRLIT EPLPELQLVE KFLNLPPRIS QYNLYFNATR GFYCLRFNII
FNKCLAGSKG RIHPEVDPSV ITKLRKFFHP FNQKFYQITG RTLNWP
