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Protein

Heparan-sulfate 6-O-sulfotransferase 1

Gene

Hs6st1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 6-sulfate.

Kineticsi

  1. KM=10 µM for CDSNS-heparin1 Publication
  2. KM=100 µM for NS-heparosan1 Publication

    GO - Molecular functioni

    • heparan sulfate 6-O-sulfotransferase activity Source: MGI

    GO - Biological processi

    • angiogenesis Source: MGI
    • heparan sulfate proteoglycan biosynthetic process Source: MGI
    • heparan sulfate proteoglycan biosynthetic process, enzymatic modification Source: MGI
    • labyrinthine layer blood vessel development Source: MGI
    • lung alveolus development Source: MGI
    • neuron development Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Enzyme and pathway databases

    ReactomeiR-MMU-2022928. HS-GAG biosynthesis.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Heparan-sulfate 6-O-sulfotransferase 1 (EC:2.8.2.-)
    Short name:
    HS6ST-1
    Short name:
    mHS6ST-1
    Gene namesi
    Name:Hs6st1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    Proteomesi
    • UP000000589 Componenti: Chromosome 1

    Organism-specific databases

    MGIiMGI:1354958. Hs6st1.

    Subcellular locationi

    Topology

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1919CytoplasmicSequence analysisAdd
    BLAST
    Transmembranei20 – 3718Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
    BLAST
    Topological domaini38 – 411374LumenalSequence analysisAdd
    BLAST

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Disruption phenotypei

    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.2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 411411Heparan-sulfate 6-O-sulfotransferase 1PRO_0000190802Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi264 – 2641N-linked (GlcNAc...)Sequence analysis
    Glycosylationi320 – 3201N-linked (GlcNAc...)Sequence analysis

    Post-translational modificationi

    N-glycosylated.By similarity

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiQ9QYK5.
    PaxDbiQ9QYK5.
    PeptideAtlasiQ9QYK5.
    PRIDEiQ9QYK5.

    PTM databases

    PhosphoSiteiQ9QYK5.

    Expressioni

    Tissue specificityi

    Expressed in fetal brain and liver.1 Publication

    Gene expression databases

    BgeeiQ9QYK5.
    CleanExiMM_HS6ST1.
    GenevisibleiQ9QYK5. MM.

    Interactioni

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000085499.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9QYK5.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni96 – 10275'-phosphosulfate-bindingSequence analysis
    Regioni185 – 19393'-phosphate bindingSequence analysis

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili352 – 38635Sequence analysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi2 – 54Poly-Arg

    Sequence similaritiesi

    Belongs to the sulfotransferase 6 family.Curated

    Keywords - Domaini

    Coiled coil, Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiKOG3955. Eukaryota.
    ENOG410XSW4. LUCA.
    GeneTreeiENSGT00390000013468.
    HOGENOMiHOG000007772.
    HOVERGENiHBG083012.
    InParanoidiQ9QYK5.
    KOiK02514.
    OMAiQNLRPDQ.
    OrthoDBiEOG75MVW3.
    PhylomeDBiQ9QYK5.
    TreeFamiTF312835.

    Family and domain databases

    InterProiIPR010635. Heparan_SO4-6-sulfoTrfase.
    IPR027417. P-loop_NTPase.
    IPR005331. Sulfotransferase.
    [Graphical view]
    PANTHERiPTHR12812. PTHR12812. 1 hit.
    PfamiPF03567. Sulfotransfer_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9QYK5-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MRRRRAGGRT MVERASKFVL VVAGSACFML ILYQYAGPGL SLGAPGGRVP
    60 70 80 90 100
    PDDLDLFPTP DPHYEKKYYF PVRELERSLR FDMKGDDVIV FLHIQKTGGT
    110 120 130 140 150
    TFGRHLVQNV RLEVPCDCRP GQKKCTCYRP NRRETWLFSR FSTGWSCGLH
    160 170 180 190 200
    ADWTELTNCV PGVLDRRDPA GLRSPRKFYY ITLLRDPVSR YLSEWRHVQR
    210 220 230 240 250
    GATWKTSLHM CDGRTPTPEE LPPCYEGTDW SGCTLQEFMD CPYNLANNRQ
    260 270 280 290 300
    VRMLADLSLV GCYNLSFIPE SKRAQLLLES AKKNLRGMAF FGLTEFQRKT
    310 320 330 340 350
    QYLFERTFNL KFIRPFMQYN STRAGGVEVD EDTIRHIEEL NDLDMQLYDY
    360 370 380 390 400
    AKDLFQQRYQ YKRQLERREQ RLRNREERLL HRSKEALPRE DPEEPGRVPT
    410
    EDYMSHIIEK W
    Length:411
    Mass (Da):48,302
    Last modified:May 5, 2009 - v4
    Checksum:i8A618806A8A1D6AE
    GO

    Sequence cautioni

    The sequence AAH52316.1 differs from that shown. Reason: Erroneous initiation. Curated
    The sequence BAA89248.1 differs from that shown. Reason: Erroneous initiation. Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti125 – 1251C → S in BAE38155 (PubMed:16141072).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB024566 mRNA. Translation: BAA89248.1. Different initiation.
    AK157556 mRNA. Translation: BAE34122.1.
    AK165385 mRNA. Translation: BAE38155.1.
    AK166962 mRNA. Translation: BAE39145.1.
    AK167151 mRNA. Translation: BAE39293.1.
    BC052316 mRNA. Translation: AAH52316.1. Different initiation.
    CCDSiCCDS48237.1.
    RefSeqiNP_056633.2. NM_015818.2.
    UniGeneiMm.213566.

    Genome annotation databases

    EnsembliENSMUST00000088174; ENSMUSP00000085499; ENSMUSG00000045216.
    GeneIDi50785.
    KEGGimmu:50785.
    UCSCiuc007apn.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB024566 mRNA. Translation: BAA89248.1. Different initiation.
    AK157556 mRNA. Translation: BAE34122.1.
    AK165385 mRNA. Translation: BAE38155.1.
    AK166962 mRNA. Translation: BAE39145.1.
    AK167151 mRNA. Translation: BAE39293.1.
    BC052316 mRNA. Translation: AAH52316.1. Different initiation.
    CCDSiCCDS48237.1.
    RefSeqiNP_056633.2. NM_015818.2.
    UniGeneiMm.213566.

    3D structure databases

    ProteinModelPortaliQ9QYK5.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000085499.

    PTM databases

    PhosphoSiteiQ9QYK5.

    Proteomic databases

    MaxQBiQ9QYK5.
    PaxDbiQ9QYK5.
    PeptideAtlasiQ9QYK5.
    PRIDEiQ9QYK5.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENSMUST00000088174; ENSMUSP00000085499; ENSMUSG00000045216.
    GeneIDi50785.
    KEGGimmu:50785.
    UCSCiuc007apn.2. mouse.

    Organism-specific databases

    CTDi9394.
    MGIiMGI:1354958. Hs6st1.

    Phylogenomic databases

    eggNOGiKOG3955. Eukaryota.
    ENOG410XSW4. LUCA.
    GeneTreeiENSGT00390000013468.
    HOGENOMiHOG000007772.
    HOVERGENiHBG083012.
    InParanoidiQ9QYK5.
    KOiK02514.
    OMAiQNLRPDQ.
    OrthoDBiEOG75MVW3.
    PhylomeDBiQ9QYK5.
    TreeFamiTF312835.

    Enzyme and pathway databases

    ReactomeiR-MMU-2022928. HS-GAG biosynthesis.

    Miscellaneous databases

    PROiQ9QYK5.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ9QYK5.
    CleanExiMM_HS6ST1.
    GenevisibleiQ9QYK5. MM.

    Family and domain databases

    InterProiIPR010635. Heparan_SO4-6-sulfoTrfase.
    IPR027417. P-loop_NTPase.
    IPR005331. Sulfotransferase.
    [Graphical view]
    PANTHERiPTHR12812. PTHR12812. 1 hit.
    PfamiPF03567. Sulfotransfer_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "The occurrence of three isoforms of heparan sulfate 6-O-sulfotransferase having different specificities for hexuronic acid adjacent to the targeted N-sulfoglucosamine."
      Habuchi H., Tanaka M., Habuchi O., Yoshida K., Suzuki H., Ban K., Kimata K.
      J. Biol. Chem. 275:2859-2868(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, DOMAIN, FUNCTION.
      Tissue: Brain.
    2. "The transcriptional landscape of the mammalian genome."
      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.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J and NOD.
      Tissue: Blastocyst and Spleen.
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Olfactory epithelium.
    4. "Mice deficient in heparan sulfate 6-O-sulfotransferase-1 exhibit defective heparan sulfate biosynthesis, abnormal placentation, and late embryonic lethality."
      Habuchi H., Nagai N., Sugaya N., Atsumi F., Stevens R.L., Kimata K.
      J. Biol. Chem. 282:15578-15588(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    5. "Systemic inactivation of Hs6st1 in mice is associated with late postnatal mortality without major defects in organogenesis."
      Izvolsky K.I., Lu J., Martin G., Albrecht K.H., Cardoso W.V.
      Genesis 46:8-18(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.

    Entry informationi

    Entry nameiH6ST1_MOUSE
    AccessioniPrimary (citable) accession number: Q9QYK5
    Secondary accession number(s): Q3TK52
    , Q3TKK0, Q3TND4, Q3TZT5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 11, 2005
    Last sequence update: May 5, 2009
    Last modified: July 6, 2016
    This is version 99 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.