H6ST2_MOUSE
ID H6ST2_MOUSE Reviewed; 612 AA.
AC Q80UW0; A2AEM4; Q3TAR0; Q6P4N9; Q8C785; Q9QYK6;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Heparan-sulfate 6-O-sulfotransferase 2;
DE Short=HS6ST-2;
DE Short=mHS6ST-2;
DE EC=2.8.2.-;
GN Name=Hs6st2;
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 75-409 (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Heart;
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 [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 78-612 (ISOFORM 1).
RC STRAIN=FVB/N-3; TISSUE=Brain, and 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 NUCLEOTIDE SEQUENCE [MRNA] OF 147-612 (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=10644753; DOI=10.1074/jbc.275.4.2859;
RA Habuchi H., Tanaka M., Habuchi O., Yoshida K., Suzuki H., Ban K.,
RA Kimata K.;
RT "The occurrence of three isoforms of heparan sulfate 6-O-sulfotransferase
RT having different specificities for hexuronic acid adjacent to the targeted
RT N-sulfoglucosamine.";
RL J. Biol. Chem. 275:2859-2868(2000).
CC -!- FUNCTION: 6-O-sulfation enzyme which catalyzes the transfer of sulfate
CC from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to position 6 of the
CC N-sulfoglucosamine residue (GlcNS) of heparan sulfate.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + alpha-D-glucosaminyl-[heparan
CC sulfate](n) = 6-sulfo-alpha-D-glucosaminyl-[heparan sulfate](n) +
CC adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:56604, Rhea:RHEA-
CC COMP:9830, Rhea:RHEA-COMP:14621, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:58388,
CC ChEBI:CHEBI:140604;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q80UW0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80UW0-2; Sequence=VSP_015848;
CC Name=3;
CC IsoId=Q80UW0-3; Sequence=VSP_015849;
CC -!- SIMILARITY: Belongs to the sulfotransferase 6 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC34950.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK052348; BAC34950.1; ALT_INIT; mRNA.
DR EMBL; AK171680; BAE42608.1; -; mRNA.
DR EMBL; AL671918; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL672057; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL672099; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC047151; AAH47151.1; -; mRNA.
DR EMBL; BC063327; AAH63327.1; -; mRNA.
DR EMBL; AB024565; BAA89247.1; -; mRNA.
DR CCDS; CCDS40970.1; -. [Q80UW0-3]
DR CCDS; CCDS72379.1; -. [Q80UW0-1]
DR RefSeq; NP_001070670.1; NM_001077202.2. [Q80UW0-3]
DR RefSeq; NP_001277396.1; NM_001290467.1. [Q80UW0-1]
DR RefSeq; NP_001277397.1; NM_001290468.1.
DR RefSeq; NP_056634.3; NM_015819.4. [Q80UW0-2]
DR RefSeq; XP_006541581.1; XM_006541518.2.
DR RefSeq; XP_006541582.1; XM_006541519.3.
DR AlphaFoldDB; Q80UW0; -.
DR SMR; Q80UW0; -.
DR STRING; 10090.ENSMUSP00000085497; -.
DR GlyGen; Q80UW0; 8 sites.
DR PhosphoSitePlus; Q80UW0; -.
DR MaxQB; Q80UW0; -.
DR PeptideAtlas; Q80UW0; -.
DR PRIDE; Q80UW0; -.
DR ProteomicsDB; 269669; -. [Q80UW0-1]
DR ProteomicsDB; 269670; -. [Q80UW0-2]
DR ProteomicsDB; 269671; -. [Q80UW0-3]
DR ABCD; Q80UW0; 2 sequenced antibodies.
DR Antibodypedia; 30253; 59 antibodies from 19 providers.
DR DNASU; 50786; -.
DR Ensembl; ENSMUST00000088172; ENSMUSP00000085497; ENSMUSG00000062184. [Q80UW0-3]
DR Ensembl; ENSMUST00000114871; ENSMUSP00000110521; ENSMUSG00000062184. [Q80UW0-1]
DR GeneID; 50786; -.
DR KEGG; mmu:50786; -.
DR UCSC; uc009tdw.2; mouse. [Q80UW0-1]
DR UCSC; uc009tdx.2; mouse. [Q80UW0-3]
DR CTD; 90161; -.
DR MGI; MGI:1354959; Hs6st2.
DR VEuPathDB; HostDB:ENSMUSG00000062184; -.
DR eggNOG; KOG3955; Eukaryota.
DR GeneTree; ENSGT00950000183071; -.
DR HOGENOM; CLU_027877_1_0_1; -.
DR InParanoid; Q80UW0; -.
DR OMA; WWDLDEN; -.
DR OrthoDB; 1167623at2759; -.
DR TreeFam; TF312835; -.
DR Reactome; R-MMU-2022928; HS-GAG biosynthesis.
DR SABIO-RK; Q80UW0; -.
DR BioGRID-ORCS; 50786; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Hs6st2; mouse.
DR PRO; PR:Q80UW0; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q80UW0; protein.
DR Bgee; ENSMUSG00000062184; Expressed in choroid plexus epithelium and 264 other tissues.
DR Genevisible; Q80UW0; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0017095; F:heparan sulfate 6-O-sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0015015; P:heparan sulfate proteoglycan biosynthetic process, enzymatic modification; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR010635; Heparan_SO4-6-sulfoTrfase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005331; Sulfotransferase.
DR PANTHER; PTHR12812; PTHR12812; 1.
DR Pfam; PF03567; Sulfotransfer_2; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Glycoprotein; Membrane; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..612
FT /note="Heparan-sulfate 6-O-sulfotransferase 2"
FT /id="PRO_0000190806"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 5..27
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..612
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 9..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 290
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 233..241
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 263..264
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 280
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 285
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 290
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 325
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 333
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 337
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 344
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 457..459
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 463..464
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 404
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 460
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 546
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 558
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 562
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 574
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 599
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..146
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_015848"
FT VAR_SEQ 316
FT /note="R -> RWRIFQILDGTSKDRWGSSNFNSGANSPSSTKPRSTSKSGK (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:10644753,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_015849"
FT CONFLICT 419
FT /note="E -> D (in Ref. 1; BAE42608)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 612 AA; 69198 MW; 12551E4408936D8D CRC64;
MALPAFAARA LGPPLQPEQG APARTTCPRR HSRVEAELAA SRPGSVAASV RAGPPRGVSL
GFNSPPLQDK PPKAFSSLAG ALRAPLFALL PRGRRRRMHD LRRRWDLGSL CRALLTRGLA
AVGHSLKHVL SAIFSKIFGP LASVGNMDEK SNKLLLALVM LFLFAVIVLQ YVCPGTECQL
LRLQAFSSPV PDPYRSEDES SARFVPRYNF SRGDLLRKVD FDIKGDDLIV FLHIQKTGGT
TFGRHLVRNI QLEQPCECRV GQKKCTCHRP GKRETWLFSR FSTGWSCGLH ADWTELTSCV
PAVVDGKRDA RLRPSRNFHY ITILRDPVSR YLSEWRHVQR GATWKASLHV CDGRPPTSEE
LPSCYTGDDW SGCPLKEFMD CPYNLANNRQ VRMLSDLTLV GCYNLSVMPE KQRNKVLLES
AKSNLKHMAF FGLTEFQRKT QYLFEKTFNM NFISPFTQYN TTRASSVEIN EEIQKRIEGL
NFLDMELYSY AKDLFLQRYQ FMRQKEHQDA RRKRQEQRKF LKGRFLQTHF QSQSQGQSQS
QSPGQNLSQN PNPNPNQNLT QNLSHNLTPS SNPNSTQREN RGSQKQGSGQ GQGDSGTSNG
TNDYIGSVET WR
