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Heparan-sulfate 6-O-sulfotransferase 2 (HS6ST-2) (mHS6ST-2) (EC 2.8.2.-)

 H6ST2_MOUSE             Reviewed;         612 AA.
Q80UW0; A2AEM4; Q3TAR0; Q6P4N9; Q8C785; Q9QYK6;
11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
09-JAN-2007, sequence version 3.
05-DEC-2018, entry version 121.
RecName: Full=Heparan-sulfate 6-O-sulfotransferase 2;
Short=HS6ST-2;
Short=mHS6ST-2;
EC=2.8.2.-;
Name=Hs6st2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 75-409 (ISOFORM 3).
STRAIN=C57BL/6J; TISSUE=Heart;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 78-612 (ISOFORM 1).
STRAIN=FVB/N-3; TISSUE=Brain, and Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 147-612 (ISOFORM 3).
TISSUE=Brain;
PubMed=10644753; DOI=10.1074/jbc.275.4.2859;
Habuchi H., Tanaka M., Habuchi O., Yoshida K., Suzuki H., Ban K.,
Kimata K.;
"The occurrence of three isoforms of heparan sulfate 6-O-
sulfotransferase having different specificities for hexuronic acid
adjacent to the targeted N-sulfoglucosamine.";
J. Biol. Chem. 275:2859-2868(2000).
-!- FUNCTION: 6-O-sulfation enzyme which catalyzes the transfer of
sulfate from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to
position 6 of the N-sulfoglucosamine residue (GlcNS) of heparan
sulfate.
-!- CATALYTIC ACTIVITY:
Reaction=3'-phosphoadenylyl sulfate + alpha-D-glucosaminyl-
[heparan sulfate](n) = 6-sulfo-alpha-D-glucosaminyl-[heparan
sulfate](n) + adenosine 3',5'-bisphosphate + H(+);
Xref=Rhea:RHEA:56604, Rhea:RHEA-COMP:9830, Rhea:RHEA-COMP:14621,
ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343,
ChEBI:CHEBI:58388, ChEBI:CHEBI:140604;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
membrane protein {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q80UW0-1; Sequence=Displayed;
Name=2;
IsoId=Q80UW0-2; Sequence=VSP_015848;
Name=3;
IsoId=Q80UW0-3; Sequence=VSP_015849;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the sulfotransferase 6 family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAC34950.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AK052348; BAC34950.1; ALT_INIT; mRNA.
EMBL; AK171680; BAE42608.1; -; mRNA.
EMBL; AL671918; CAM16284.1; -; Genomic_DNA.
EMBL; AL672057; CAM16284.1; JOINED; Genomic_DNA.
EMBL; AL672057; CAM21295.1; -; Genomic_DNA.
EMBL; AL671918; CAM21295.1; JOINED; Genomic_DNA.
EMBL; AL672099; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC047151; AAH47151.1; -; mRNA.
EMBL; BC063327; AAH63327.1; -; mRNA.
EMBL; AB024565; BAA89247.1; -; mRNA.
CCDS; CCDS40970.1; -. [Q80UW0-3]
CCDS; CCDS72379.1; -. [Q80UW0-1]
RefSeq; NP_001070670.1; NM_001077202.2. [Q80UW0-3]
RefSeq; NP_001277396.1; NM_001290467.1. [Q80UW0-1]
RefSeq; NP_001277397.1; NM_001290468.1.
RefSeq; NP_056634.3; NM_015819.4. [Q80UW0-2]
RefSeq; XP_006541581.1; XM_006541518.2.
RefSeq; XP_006541582.1; XM_006541519.3.
UniGene; Mm.252561; -.
ProteinModelPortal; Q80UW0; -.
SMR; Q80UW0; -.
PhosphoSitePlus; Q80UW0; -.
PeptideAtlas; Q80UW0; -.
PRIDE; Q80UW0; -.
Ensembl; ENSMUST00000088172; ENSMUSP00000085497; ENSMUSG00000062184. [Q80UW0-3]
Ensembl; ENSMUST00000114871; ENSMUSP00000110521; ENSMUSG00000062184. [Q80UW0-1]
GeneID; 50786; -.
KEGG; mmu:50786; -.
UCSC; uc009tdw.2; mouse. [Q80UW0-1]
UCSC; uc009tdx.2; mouse. [Q80UW0-3]
CTD; 90161; -.
MGI; MGI:1354959; Hs6st2.
GeneTree; ENSGT00940000154073; -.
HOGENOM; HOG000007772; -.
HOVERGEN; HBG083012; -.
InParanoid; Q80UW0; -.
KO; K08102; -.
OMA; SRNYYYI; -.
OrthoDB; EOG091G08UD; -.
TreeFam; TF312835; -.
Reactome; R-MMU-2022928; HS-GAG biosynthesis.
PRO; PR:Q80UW0; -.
Proteomes; UP000000589; Chromosome X.
Bgee; ENSMUSG00000062184; Expressed in 280 organ(s), highest expression level in female gonad.
CleanEx; MM_HS6ST2; -.
Genevisible; Q80UW0; MM.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0017095; F:heparan sulfate 6-O-sulfotransferase activity; IDA:MGI.
GO; GO:0015015; P:heparan sulfate proteoglycan biosynthetic process, enzymatic modification; IDA:MGI.
InterPro; IPR010635; Heparan_SO4-6-sulfoTrfase.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR005331; Sulfotransferase.
PANTHER; PTHR12812; PTHR12812; 1.
Pfam; PF03567; Sulfotransfer_2; 1.
SUPFAM; SSF52540; SSF52540; 1.
2: Evidence at transcript level;
Alternative splicing; Complete proteome; Glycoprotein; Membrane;
Reference proteome; Signal-anchor; Transferase; Transmembrane;
Transmembrane helix.
CHAIN 1 612 Heparan-sulfate 6-O-sulfotransferase 2.
/FTId=PRO_0000190806.
TOPO_DOM 1 4 Cytoplasmic. {ECO:0000255}.
TRANSMEM 5 27 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 28 612 Lumenal. {ECO:0000255}.
REGION 233 241 PAPS binding.
{ECO:0000250|UniProtKB:A0MGZ7}.
REGION 263 264 Substrate binding.
{ECO:0000250|UniProtKB:A0MGZ7}.
REGION 457 459 PAPS binding.
{ECO:0000250|UniProtKB:A0MGZ7}.
REGION 463 464 PAPS binding.
{ECO:0000250|UniProtKB:A0MGZ7}.
ACT_SITE 290 290 Proton acceptor.
{ECO:0000250|UniProtKB:A0MGZ7}.
BINDING 280 280 Substrate.
{ECO:0000250|UniProtKB:A0MGZ7}.
BINDING 285 285 Substrate.
{ECO:0000250|UniProtKB:A0MGZ7}.
BINDING 290 290 Substrate.
{ECO:0000250|UniProtKB:A0MGZ7}.
BINDING 325 325 PAPS. {ECO:0000250|UniProtKB:A0MGZ7}.
BINDING 333 333 PAPS. {ECO:0000250|UniProtKB:A0MGZ7}.
BINDING 337 337 Substrate.
{ECO:0000250|UniProtKB:A0MGZ7}.
BINDING 344 344 Substrate.
{ECO:0000250|UniProtKB:A0MGZ7}.
CARBOHYD 209 209 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 404 404 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 460 460 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 546 546 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 558 558 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 562 562 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 574 574 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 599 599 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1 146 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_015848.
VAR_SEQ 316 316 R -> RWRIFQILDGTSKDRWGSSNFNSGANSPSSTKPRST
SKSGK (in isoform 3).
{ECO:0000303|PubMed:10644753,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_015849.
CONFLICT 419 419 E -> D (in Ref. 1; BAE42608).
{ECO:0000305}.
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


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