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   24-JAN-2024, entry version 148.
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   GlyCosmos; Q80UW0; 8 sites, No reported glycans.
DR   GlyGen; Q80UW0; 8 sites.
DR   PhosphoSitePlus; Q80UW0; -.
DR   MaxQB; Q80UW0; -.
DR   PaxDb; 10090-ENSMUSP00000085497; -.
DR   PeptideAtlas; 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; 94 antibodies from 20 providers.
DR   DNASU; 50786; -.
DR   Ensembl; ENSMUST00000088172.12; ENSMUSP00000085497.6; ENSMUSG00000062184.12. [Q80UW0-3]
DR   Ensembl; ENSMUST00000114871.2; ENSMUSP00000110521.2; ENSMUSG00000062184.12. [Q80UW0-1]
DR   GeneID; 50786; -.
DR   KEGG; mmu:50786; -.
DR   UCSC; uc009tdw.2; mouse. [Q80UW0-1]
DR   UCSC; uc009tdx.2; mouse. [Q80UW0-3]
DR   AGR; MGI:1354959; -.
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; 2896660at2759; -.
DR   TreeFam; TF312835; -.
DR   Reactome; R-MMU-2022928; HS-GAG biosynthesis.
DR   SABIO-RK; Q80UW0; -.
DR   BioGRID-ORCS; 50786; 3 hits in 79 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 267 other cell types or tissues.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0017095; F:heparan sulfate 6-O-sulfotransferase activity; IDA:MGI.
DR   GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; IDA:MGI.
DR   GO; GO:0015015; P:heparan sulfate proteoglycan biosynthetic process, enzymatic modification; IBA:GO_Central.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR010635; Heparan_SO4-6-sulfoTrfase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005331; Sulfotransferase.
DR   PANTHER; PTHR12812; HEPARAN SULFATE 6-O-SULFOTRANSFERASE 3; 1.
DR   PANTHER; PTHR12812:SF6; HEPARAN-SULFATE 6-O-SULFOTRANSFERASE 2; 1.
DR   Pfam; PF03567; Sulfotransfer_2; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   Genevisible; Q80UW0; MM.
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
//