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Heparan-sulfate 6-O-sulfotransferase 1 (HS6ST-1) (mHS6ST-1) (EC 2.8.2.-)

 H6ST1_MOUSE             Reviewed;         411 AA.
Q9QYK5; Q3TK52; Q3TKK0; Q3TND4; Q3TZT5;
11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
05-MAY-2009, sequence version 4.
05-DEC-2018, entry version 110.
RecName: Full=Heparan-sulfate 6-O-sulfotransferase 1;
Short=HS6ST-1;
Short=mHS6ST-1;
EC=2.8.2.-;
Name=Hs6st1;
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 [MRNA], BIOPHYSICOCHEMICAL PROPERTIES, TISSUE
SPECIFICITY, DOMAIN, AND FUNCTION.
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD; TISSUE=Blastocyst, and Spleen;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Olfactory epithelium;
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]
DISRUPTION PHENOTYPE.
PubMed=17405882; DOI=10.1074/jbc.M607434200;
Habuchi H., Nagai N., Sugaya N., Atsumi F., Stevens R.L., Kimata K.;
"Mice deficient in heparan sulfate 6-O-sulfotransferase-1 exhibit
defective heparan sulfate biosynthesis, abnormal placentation, and
late embryonic lethality.";
J. Biol. Chem. 282:15578-15588(2007).
[5]
DISRUPTION PHENOTYPE.
PubMed=18196599; DOI=10.1002/dvg.20355;
Izvolsky K.I., Lu J., Martin G., Albrecht K.H., Cardoso W.V.;
"Systemic inactivation of Hs6st1 in mice is associated with late
postnatal mortality without major defects in organogenesis.";
Genesis 46:8-18(2008).
-!- 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. Critical for normal neuronal development where it may
play a role in neuron branching. May also play a role in limb
development. May prefer iduronic acid.
{ECO:0000269|PubMed:10644753}.
-!- 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;
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=10 uM for CDSNS-heparin {ECO:0000269|PubMed:10644753};
KM=100 uM for NS-heparosan {ECO:0000269|PubMed:10644753};
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
membrane protein {ECO:0000305}.
-!- TISSUE SPECIFICITY: Expressed in fetal brain and liver.
{ECO:0000269|PubMed:10644753}.
-!- PTM: N-glycosylated. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: According to PubMed:17405882 most mice die
between embryonic day 15.5 and the perinatal stage. Those that
survive are considerably smaller than their wild-type littermates
and exhibit development abnormalities including a reduction in the
number of fetal microvessels in the labyrinthine zone of the
placenta. However, according to PubMed:18196599, pups are viable
and grossly normal at birth. During early adulthood, however, mice
fail to thrive and exhibit growth retardation, bodyweight loss,
enlargement of airspaces in the lung and, in some cases,
lethality. {ECO:0000269|PubMed:17405882,
ECO:0000269|PubMed:18196599}.
-!- SIMILARITY: Belongs to the sulfotransferase 6 family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH52316.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAA89248.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AB024566; BAA89248.1; ALT_INIT; mRNA.
EMBL; AK157556; BAE34122.1; -; mRNA.
EMBL; AK165385; BAE38155.1; -; mRNA.
EMBL; AK166962; BAE39145.1; -; mRNA.
EMBL; AK167151; BAE39293.1; -; mRNA.
EMBL; BC052316; AAH52316.1; ALT_INIT; mRNA.
CCDS; CCDS48237.1; -.
RefSeq; NP_056633.2; NM_015818.2.
UniGene; Mm.213566; -.
ProteinModelPortal; Q9QYK5; -.
SMR; Q9QYK5; -.
STRING; 10090.ENSMUSP00000085499; -.
PhosphoSitePlus; Q9QYK5; -.
MaxQB; Q9QYK5; -.
PaxDb; Q9QYK5; -.
PeptideAtlas; Q9QYK5; -.
PRIDE; Q9QYK5; -.
Ensembl; ENSMUST00000088174; ENSMUSP00000085499; ENSMUSG00000045216.
GeneID; 50785; -.
KEGG; mmu:50785; -.
UCSC; uc007apn.2; mouse.
CTD; 9394; -.
MGI; MGI:1354958; Hs6st1.
eggNOG; KOG3955; Eukaryota.
eggNOG; ENOG410XSW4; LUCA.
GeneTree; ENSGT00940000154073; -.
HOGENOM; HOG000007772; -.
HOVERGEN; HBG083012; -.
InParanoid; Q9QYK5; -.
KO; K02514; -.
OMA; QNLRPDQ; -.
OrthoDB; EOG091G08UD; -.
PhylomeDB; Q9QYK5; -.
TreeFam; TF312835; -.
Reactome; R-MMU-2022928; HS-GAG biosynthesis.
SABIO-RK; Q9QYK5; -.
PRO; PR:Q9QYK5; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000045216; Expressed in 349 organ(s), highest expression level in prostate gland.
CleanEx; MM_HS6ST1; -.
Genevisible; Q9QYK5; MM.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0017095; F:heparan sulfate 6-O-sulfotransferase activity; IDA:MGI.
GO; GO:0001525; P:angiogenesis; IMP:MGI.
GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; IMP:MGI.
GO; GO:0015015; P:heparan sulfate proteoglycan biosynthetic process, enzymatic modification; IDA:MGI.
GO; GO:0060716; P:labyrinthine layer blood vessel development; IMP:MGI.
GO; GO:0048286; P:lung alveolus development; IMP:MGI.
GO; GO:0048666; P:neuron development; ISS:UniProtKB.
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.
1: Evidence at protein level;
Coiled coil; Complete proteome; Glycoprotein; Membrane;
Reference proteome; Signal-anchor; Transferase; Transmembrane;
Transmembrane helix.
CHAIN 1 411 Heparan-sulfate 6-O-sulfotransferase 1.
/FTId=PRO_0000190802.
TOPO_DOM 1 19 Cytoplasmic. {ECO:0000255}.
TRANSMEM 20 37 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 38 411 Lumenal. {ECO:0000255}.
REGION 93 101 PAPS binding.
{ECO:0000250|UniProtKB:A0MGZ7}.
REGION 123 124 Substrate binding.
{ECO:0000250|UniProtKB:A0MGZ7}.
REGION 317 319 PAPS binding.
{ECO:0000250|UniProtKB:A0MGZ7}.
REGION 323 324 PAPS binding.
{ECO:0000250|UniProtKB:A0MGZ7}.
COILED 352 386 {ECO:0000255}.
COMPBIAS 2 5 Poly-Arg.
ACT_SITE 150 150 Proton acceptor.
{ECO:0000250|UniProtKB:A0MGZ7}.
BINDING 140 140 Substrate.
{ECO:0000250|UniProtKB:A0MGZ7}.
BINDING 145 145 Substrate.
{ECO:0000250|UniProtKB:A0MGZ7}.
BINDING 150 150 Substrate.
{ECO:0000250|UniProtKB:A0MGZ7}.
BINDING 185 185 PAPS. {ECO:0000250|UniProtKB:A0MGZ7}.
BINDING 193 193 PAPS. {ECO:0000250|UniProtKB:A0MGZ7}.
BINDING 197 197 Substrate.
{ECO:0000250|UniProtKB:A0MGZ7}.
BINDING 204 204 Substrate.
{ECO:0000250|UniProtKB:A0MGZ7}.
CARBOHYD 264 264 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 320 320 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CONFLICT 125 125 C -> S (in Ref. 2; BAE38155).
{ECO:0000305}.
SEQUENCE 411 AA; 48302 MW; 8A618806A8A1D6AE CRC64;
MRRRRAGGRT MVERASKFVL VVAGSACFML ILYQYAGPGL SLGAPGGRVP PDDLDLFPTP
DPHYEKKYYF PVRELERSLR FDMKGDDVIV FLHIQKTGGT TFGRHLVQNV RLEVPCDCRP
GQKKCTCYRP NRRETWLFSR FSTGWSCGLH ADWTELTNCV PGVLDRRDPA GLRSPRKFYY
ITLLRDPVSR YLSEWRHVQR GATWKTSLHM CDGRTPTPEE LPPCYEGTDW SGCTLQEFMD
CPYNLANNRQ VRMLADLSLV GCYNLSFIPE SKRAQLLLES AKKNLRGMAF FGLTEFQRKT
QYLFERTFNL KFIRPFMQYN STRAGGVEVD EDTIRHIEEL NDLDMQLYDY AKDLFQQRYQ
YKRQLERREQ RLRNREERLL HRSKEALPRE DPEEPGRVPT EDYMSHIIEK W


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