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Q3UDW8

- HGNAT_MOUSE

UniProt

Q3UDW8 - HGNAT_MOUSE

Protein

Heparan-alpha-glucosaminide N-acetyltransferase

Gene

Hgsnat

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 72 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Lysosomal acetyltransferase that acetylates the non-reducing terminal alpha-glucosamine residue of intralysosomal heparin or heparan sulfate, converting it into a substrate for luminal alpha-N-acetyl glucosaminidase.1 Publication

    Catalytic activityi

    Acetyl-CoA + heparan sulfate alpha-D-glucosaminide = CoA + heparan sulfate N-acetyl-alpha-D-glucosaminide.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei290 – 2901By similarity

    GO - Molecular functioni

    1. heparan-alpha-glucosaminide N-acetyltransferase activity Source: UniProtKB-EC
    2. transferase activity, transferring acyl groups Source: UniProtKB

    GO - Biological processi

    1. lysosomal transport Source: UniProtKB
    2. metabolic process Source: GOC
    3. protein oligomerization Source: UniProtKB

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Enzyme and pathway databases

    ReactomeiREACT_198967. HS-GAG degradation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Heparan-alpha-glucosaminide N-acetyltransferase (EC:2.3.1.78)
    Alternative name(s):
    Transmembrane protein 76
    Gene namesi
    Name:Hgsnat
    Synonyms:D8Ertd354e, Tmem76
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 8

    Organism-specific databases

    MGIiMGI:1196297. Hgsnat.

    Subcellular locationi

    Lysosome membrane 1 Publication; Multi-pass membrane protein 1 Publication
    Note: Colocalizes with the lysosomal marker LAMP2. The signal peptide is not cleaved upon translocation into the endoplasmic reticulum; the precursor is probably targeted to the lysosomes via the adapter protein complex-mediated pathway that involves tyrosine- and/or dileucine-based conserved amino acid motifs in the last C-terminus 16-amino acid domain By similarity.By similarity

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. lysosomal membrane Source: UniProtKB

    Keywords - Cellular componenti

    Lysosome, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 656656Heparan-alpha-glucosaminide N-acetyltransferasePRO_0000273154Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi137 – 1371N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi146 ↔ 455By similarity
    Glycosylationi157 – 1571N-linked (GlcNAc...)1 Publication
    Modified residuei240 – 2401PhosphoserineBy similarity
    Modified residuei249 – 2491Phosphotyrosine1 Publication

    Post-translational modificationi

    Undergoes intralysosomal proteolytic cleavage; occurs within the end of the first and/or the beginning of the second luminal domain and is essential for the activation of the enzyme.By similarity
    Glycosylated.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiQ3UDW8.
    PRIDEiQ3UDW8.

    PTM databases

    PhosphoSiteiQ3UDW8.

    Expressioni

    Gene expression databases

    BgeeiQ3UDW8.
    CleanExiMM_HGSNAT.
    GenevestigatoriQ3UDW8.

    Interactioni

    Subunit structurei

    Homooligomer. Homooligomerization is necessary for enzyme activity By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ3UDW8.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 185185Lumenal, vesicleSequence AnalysisAdd
    BLAST
    Topological domaini207 – 26862CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini290 – 2956Lumenal, vesicleSequence Analysis
    Topological domaini317 – 33822CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini360 – 3678Lumenal, vesicleSequence Analysis
    Topological domaini389 – 41325CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini435 – 49359Lumenal, vesicleSequence AnalysisAdd
    BLAST
    Topological domaini515 – 5228CytoplasmicSequence Analysis
    Topological domaini544 – 55714Lumenal, vesicleSequence AnalysisAdd
    BLAST
    Topological domaini579 – 5857CytoplasmicSequence Analysis
    Topological domaini607 – 62721Lumenal, vesicleSequence AnalysisAdd
    BLAST
    Topological domaini649 – 6568CytoplasmicSequence Analysis

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei186 – 20621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei269 – 28921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei296 – 31621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei339 – 35921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei368 – 38821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei414 – 43421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei494 – 51421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei523 – 54321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei558 – 57821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei586 – 60621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei628 – 64821HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni641 – 65616Lysosomal targeting regionBy similarityAdd
    BLAST

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG4299.
    GeneTreeiENSGT00390000001491.
    HOGENOMiHOG000006803.
    HOVERGENiHBG081599.
    InParanoidiQ3UDW8.
    KOiK10532.
    OMAiNSERCYH.
    OrthoDBiEOG7PS1F9.
    TreeFamiTF324790.

    Family and domain databases

    InterProiIPR012429. DUF1624.
    [Graphical view]
    PfamiPF07786. DUF1624. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative initiation. Align

    Isoform 1 (identifier: Q3UDW8-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MTGGSSSRRR RAEERSSAAG TERNSRREAV GGMGAGPALA ALLLAGSVLS    50
    ATLLAPGRRA EPDLDEKRNV ELKMDQALLL IHNELLGTSL TVYWKSDDCY 100
    QCTFQPLANV SHGGKPAKPS VAPVSVSTQH GSILQVNSTS EERAACRLEY 150
    KFGEFGNYSL LVQHASSGAN KIACDIIVNE NPVDSNLPVS IAFLVGLALI 200
    VAVSLLRLLL SLDDVNNWIS KTIASRETDR LINSELGSPS RADPLSADYQ 250
    PETRRSSANR LRCVDTFRGL ALVLMVFVNY GGGKYWYFKH SSWNGLTVAD 300
    LVFPWFVFIM GTSIFLSMTS ILQRGCSKLK LLGKIVWRSF LLICIGVIIV 350
    NPNYCLGPLS WDKVRIPGVL QRLGVTYFVV AVLEFFFWKP VPDSCTLESS 400
    CFSLRDITSS WPQWLTILTL ESIWLALTFF LPVPGCPTGY LGPGGIGDLG 450
    KYPHCTGGAA GYIDRLLLGD NHLYQHPSST VLYHTEVAYD PEGVLGTINS 500
    IVMAFLGVQA GKILVYYKDQ TKAILTRFAA WCCILGLISI VLTKVSANEG 550
    FIPINKNLWS ISYVTTLSCF AFFILLILYP VVDVKGLWTG TPFFYPGMNS 600
    ILVYVGHEVL ENYFPFQWKL ADEQSHKEHL IQNIVATALW VLIAYVLYKK 650
    KLFWKI 656
    Length:656
    Mass (Da):72,504
    Last modified:July 27, 2011 - v2
    Checksum:i8FAE5EBECED5CCE3
    GO
    Isoform 2 (identifier: Q3UDW8-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-32: Missing.

    Show »
    Length:624
    Mass (Da):69,100
    Checksum:i5272EA184EB5BDA4
    GO

    Sequence cautioni

    The sequence AAH24084.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAC29006.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAE31601.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAE35261.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAE35603.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti23 – 231R → H in AAH24084. (PubMed:15489334)Curated
    Sequence conflicti24 – 241N → S in AAH24084. (PubMed:15489334)Curated
    Sequence conflicti222 – 2221T → A in AAH24084. (PubMed:15489334)Curated
    Sequence conflicti242 – 2421A → G in BAE35261. (PubMed:16141072)Curated
    Sequence conflicti329 – 3291L → F in BAE29143. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3232Missing in isoform 2. CuratedVSP_040505Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK035264 mRNA. Translation: BAC29006.1. Different initiation.
    AK149883 mRNA. Translation: BAE29143.1.
    AK152926 mRNA. Translation: BAE31601.1. Different initiation.
    AK159649 mRNA. Translation: BAE35261.1. Different initiation.
    AK160068 mRNA. Translation: BAE35603.1. Different initiation.
    AC093366 Genomic DNA. No translation available.
    BC024084 mRNA. Translation: AAH24084.1. Different initiation.
    CCDSiCCDS40309.1. [Q3UDW8-1]
    RefSeqiNP_084160.1. NM_029884.1. [Q3UDW8-1]
    UniGeneiMm.28326.

    Genome annotation databases

    EnsembliENSMUST00000037609; ENSMUSP00000040356; ENSMUSG00000037260. [Q3UDW8-1]
    GeneIDi52120.
    KEGGimmu:52120.
    UCSCiuc009lhg.1. mouse. [Q3UDW8-1]

    Keywords - Coding sequence diversityi

    Alternative initiation

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK035264 mRNA. Translation: BAC29006.1 . Different initiation.
    AK149883 mRNA. Translation: BAE29143.1 .
    AK152926 mRNA. Translation: BAE31601.1 . Different initiation.
    AK159649 mRNA. Translation: BAE35261.1 . Different initiation.
    AK160068 mRNA. Translation: BAE35603.1 . Different initiation.
    AC093366 Genomic DNA. No translation available.
    BC024084 mRNA. Translation: AAH24084.1 . Different initiation.
    CCDSi CCDS40309.1. [Q3UDW8-1 ]
    RefSeqi NP_084160.1. NM_029884.1. [Q3UDW8-1 ]
    UniGenei Mm.28326.

    3D structure databases

    ProteinModelPortali Q3UDW8.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q3UDW8.

    Proteomic databases

    PaxDbi Q3UDW8.
    PRIDEi Q3UDW8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000037609 ; ENSMUSP00000040356 ; ENSMUSG00000037260 . [Q3UDW8-1 ]
    GeneIDi 52120.
    KEGGi mmu:52120.
    UCSCi uc009lhg.1. mouse. [Q3UDW8-1 ]

    Organism-specific databases

    CTDi 138050.
    MGIi MGI:1196297. Hgsnat.

    Phylogenomic databases

    eggNOGi COG4299.
    GeneTreei ENSGT00390000001491.
    HOGENOMi HOG000006803.
    HOVERGENi HBG081599.
    InParanoidi Q3UDW8.
    KOi K10532.
    OMAi NSERCYH.
    OrthoDBi EOG7PS1F9.
    TreeFami TF324790.

    Enzyme and pathway databases

    Reactomei REACT_198967. HS-GAG degradation.

    Miscellaneous databases

    ChiTaRSi HGSNAT. mouse.
    NextBioi 308520.
    PROi Q3UDW8.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q3UDW8.
    CleanExi MM_HGSNAT.
    Genevestigatori Q3UDW8.

    Family and domain databases

    InterProi IPR012429. DUF1624.
    [Graphical view ]
    Pfami PF07786. DUF1624. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1/2).
      Strain: C57BL/6J.
      Tissue: Bone marrow and Urinary bladder.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    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] OF 21-656 (ISOFORM 1/2).
      Strain: FVB/N.
      Tissue: Liver.
    4. "Identification of the gene encoding the enzyme deficient in mucopolysaccharidosis IIIC (Sanfilippo disease type C)."
      Fan X., Zhang H., Zhang S., Bagshaw R.D., Tropak M.B., Callahan J.W., Mahuran D.J.
      Am. J. Hum. Genet. 79:738-744(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    5. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
      Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
      J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-249, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Mast cell.
    6. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
      Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
      Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-157.

    Entry informationi

    Entry nameiHGNAT_MOUSE
    AccessioniPrimary (citable) accession number: Q3UDW8
    Secondary accession number(s): E9QNP9
    , Q3TWK5, Q8CBU7, Q8CIE1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 23, 2007
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 72 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    A signal sequence is predicted but has been shown not to be cleaved in the reticulum endoplasmic.By similarity

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

    External Data

    Dasty 3