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Q3UDW8 (HGNAT_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Heparan-alpha-glucosaminide N-acetyltransferase

EC=2.3.1.78
Alternative name(s):
Transmembrane protein 76
Gene names
Name:Hgsnat
Synonyms:D8Ertd354e, Tmem76
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length656 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4

Catalytic activity

Acetyl-CoA + heparan sulfate alpha-D-glucosaminide = CoA + heparan sulfate N-acetyl-alpha-D-glucosaminide. Ref.4

Subunit structure

Homooligomer. Homooligomerization is necessary for enzyme activity By similarity.

Subcellular location

Lysosome membrane; Multi-pass membrane protein. 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. Ref.4

Post-translational modification

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.

Miscellaneous

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

Sequence caution

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.

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]
Isoform 1 (identifier: Q3UDW8-1)

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.
Isoform 2 (identifier: Q3UDW8-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 656656Heparan-alpha-glucosaminide N-acetyltransferase
PRO_0000273154

Regions

Topological domain1 – 185185Lumenal, vesicle Potential
Transmembrane186 – 20621Helical; Potential
Topological domain207 – 26862Cytoplasmic Potential
Transmembrane269 – 28921Helical; Potential
Topological domain290 – 2956Lumenal, vesicle Potential
Transmembrane296 – 31621Helical; Potential
Topological domain317 – 33822Cytoplasmic Potential
Transmembrane339 – 35921Helical; Potential
Topological domain360 – 3678Lumenal, vesicle Potential
Transmembrane368 – 38821Helical; Potential
Topological domain389 – 41325Cytoplasmic Potential
Transmembrane414 – 43421Helical; Potential
Topological domain435 – 49359Lumenal, vesicle Potential
Transmembrane494 – 51421Helical; Potential
Topological domain515 – 5228Cytoplasmic Potential
Transmembrane523 – 54321Helical; Potential
Topological domain544 – 55714Lumenal, vesicle Potential
Transmembrane558 – 57821Helical; Potential
Topological domain579 – 5857Cytoplasmic Potential
Transmembrane586 – 60621Helical; Potential
Topological domain607 – 62721Lumenal, vesicle Potential
Transmembrane628 – 64821Helical; Potential
Topological domain649 – 6568Cytoplasmic Potential
Region641 – 65616Lysosomal targeting region By similarity

Sites

Active site2901 By similarity

Amino acid modifications

Modified residue2401Phosphoserine By similarity
Modified residue2491Phosphotyrosine Ref.5
Glycosylation1371N-linked (GlcNAc...) Potential
Glycosylation1571N-linked (GlcNAc...) Ref.6
Disulfide bond146 ↔ 455 By similarity

Natural variations

Alternative sequence1 – 3232Missing in isoform 2.
VSP_040505

Experimental info

Sequence conflict231R → H in AAH24084. Ref.3
Sequence conflict241N → S in AAH24084. Ref.3
Sequence conflict2221T → A in AAH24084. Ref.3
Sequence conflict2421A → G in BAE35261. Ref.1
Sequence conflict3291L → F in BAE29143. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 8FAE5EBECED5CCE3

FASTA65672,504
        10         20         30         40         50         60 
MTGGSSSRRR RAEERSSAAG TERNSRREAV GGMGAGPALA ALLLAGSVLS ATLLAPGRRA 

        70         80         90        100        110        120 
EPDLDEKRNV ELKMDQALLL IHNELLGTSL TVYWKSDDCY QCTFQPLANV SHGGKPAKPS 

       130        140        150        160        170        180 
VAPVSVSTQH GSILQVNSTS EERAACRLEY KFGEFGNYSL LVQHASSGAN KIACDIIVNE 

       190        200        210        220        230        240 
NPVDSNLPVS IAFLVGLALI VAVSLLRLLL SLDDVNNWIS KTIASRETDR LINSELGSPS 

       250        260        270        280        290        300 
RADPLSADYQ PETRRSSANR LRCVDTFRGL ALVLMVFVNY GGGKYWYFKH SSWNGLTVAD 

       310        320        330        340        350        360 
LVFPWFVFIM GTSIFLSMTS ILQRGCSKLK LLGKIVWRSF LLICIGVIIV NPNYCLGPLS 

       370        380        390        400        410        420 
WDKVRIPGVL QRLGVTYFVV AVLEFFFWKP VPDSCTLESS CFSLRDITSS WPQWLTILTL 

       430        440        450        460        470        480 
ESIWLALTFF LPVPGCPTGY LGPGGIGDLG KYPHCTGGAA GYIDRLLLGD NHLYQHPSST 

       490        500        510        520        530        540 
VLYHTEVAYD PEGVLGTINS IVMAFLGVQA GKILVYYKDQ TKAILTRFAA WCCILGLISI 

       550        560        570        580        590        600 
VLTKVSANEG FIPINKNLWS ISYVTTLSCF AFFILLILYP VVDVKGLWTG TPFFYPGMNS 

       610        620        630        640        650 
ILVYVGHEVL ENYFPFQWKL ADEQSHKEHL IQNIVATALW VLIAYVLYKK KLFWKI 

« Hide

Isoform 2 [UniParc].

Checksum: 5272EA184EB5BDA4
Show »

FASTA62469,100

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
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. expand/collapse author list , 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.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS40309.1. [Q3UDW8-1]
RefSeqNP_084160.1. NM_029884.1. [Q3UDW8-1]
UniGeneMm.28326.

3D structure databases

ProteinModelPortalQ3UDW8.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ3UDW8.

Proteomic databases

PaxDbQ3UDW8.
PRIDEQ3UDW8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000037609; ENSMUSP00000040356; ENSMUSG00000037260. [Q3UDW8-1]
GeneID52120.
KEGGmmu:52120.
UCSCuc009lhg.1. mouse. [Q3UDW8-1]

Organism-specific databases

CTD138050.
MGIMGI:1196297. Hgsnat.

Phylogenomic databases

eggNOGCOG4299.
GeneTreeENSGT00390000001491.
HOGENOMHOG000006803.
HOVERGENHBG081599.
InParanoidQ3UDW8.
KOK10532.
OMANSERCYH.
OrthoDBEOG7PS1F9.
TreeFamTF324790.

Gene expression databases

BgeeQ3UDW8.
CleanExMM_HGSNAT.
GenevestigatorQ3UDW8.

Family and domain databases

InterProIPR012429. DUF1624.
[Graphical view]
PfamPF07786. DUF1624. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHGSNAT. mouse.
NextBio308520.
PROQ3UDW8.
SOURCESearch...

Entry information

Entry nameHGNAT_MOUSE
AccessionPrimary (citable) accession number: Q3UDW8
Secondary accession number(s): E9QNP9 expand/collapse secondary AC list , Q3TWK5, Q8CBU7, Q8CIE1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 70 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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