Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Heparan-alpha-glucosaminide N-acetyltransferase

Gene

Hgsnat

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

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Enzyme and pathway databases

BRENDAi2.3.1.78. 3474.
ReactomeiREACT_343711. 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 Componenti: 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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 185185Lumenal, vesicleSequence AnalysisAdd
BLAST
Transmembranei186 – 20621HelicalSequence AnalysisAdd
BLAST
Topological domaini207 – 26862CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei269 – 28921HelicalSequence AnalysisAdd
BLAST
Topological domaini290 – 2956Lumenal, vesicleSequence Analysis
Transmembranei296 – 31621HelicalSequence AnalysisAdd
BLAST
Topological domaini317 – 33822CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei339 – 35921HelicalSequence AnalysisAdd
BLAST
Topological domaini360 – 3678Lumenal, vesicleSequence Analysis
Transmembranei368 – 38821HelicalSequence AnalysisAdd
BLAST
Topological domaini389 – 41325CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei414 – 43421HelicalSequence AnalysisAdd
BLAST
Topological domaini435 – 49359Lumenal, vesicleSequence AnalysisAdd
BLAST
Transmembranei494 – 51421HelicalSequence AnalysisAdd
BLAST
Topological domaini515 – 5228CytoplasmicSequence Analysis
Transmembranei523 – 54321HelicalSequence AnalysisAdd
BLAST
Topological domaini544 – 55714Lumenal, vesicleSequence AnalysisAdd
BLAST
Transmembranei558 – 57821HelicalSequence AnalysisAdd
BLAST
Topological domaini579 – 5857CytoplasmicSequence Analysis
Transmembranei586 – 60621HelicalSequence AnalysisAdd
BLAST
Topological domaini607 – 62721Lumenal, vesicleSequence AnalysisAdd
BLAST
Transmembranei628 – 64821HelicalSequence AnalysisAdd
BLAST
Topological domaini649 – 6568CytoplasmicSequence Analysis

GO - Cellular componenti

Complete GO annotation...

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

MaxQBiQ3UDW8.
PaxDbiQ3UDW8.
PRIDEiQ3UDW8.

PTM databases

PhosphoSiteiQ3UDW8.

Expressioni

Gene expression databases

BgeeiQ3UDW8.
CleanExiMM_HGSNAT.
GenevisibleiQ3UDW8. MM.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000040356.

Structurei

3D structure databases

ProteinModelPortaliQ3UDW8.
ModBaseiSearch...
MobiDBiSearch...

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. AlignAdd to basket

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

        10         20         30         40         50
MTGGSSSRRR RAEERSSAAG TERNSRREAV GGMGAGPALA ALLLAGSVLS
60 70 80 90 100
ATLLAPGRRA EPDLDEKRNV ELKMDQALLL IHNELLGTSL TVYWKSDDCY
110 120 130 140 150
QCTFQPLANV SHGGKPAKPS VAPVSVSTQH GSILQVNSTS EERAACRLEY
160 170 180 190 200
KFGEFGNYSL LVQHASSGAN KIACDIIVNE NPVDSNLPVS IAFLVGLALI
210 220 230 240 250
VAVSLLRLLL SLDDVNNWIS KTIASRETDR LINSELGSPS RADPLSADYQ
260 270 280 290 300
PETRRSSANR LRCVDTFRGL ALVLMVFVNY GGGKYWYFKH SSWNGLTVAD
310 320 330 340 350
LVFPWFVFIM GTSIFLSMTS ILQRGCSKLK LLGKIVWRSF LLICIGVIIV
360 370 380 390 400
NPNYCLGPLS WDKVRIPGVL QRLGVTYFVV AVLEFFFWKP VPDSCTLESS
410 420 430 440 450
CFSLRDITSS WPQWLTILTL ESIWLALTFF LPVPGCPTGY LGPGGIGDLG
460 470 480 490 500
KYPHCTGGAA GYIDRLLLGD NHLYQHPSST VLYHTEVAYD PEGVLGTINS
510 520 530 540 550
IVMAFLGVQA GKILVYYKDQ TKAILTRFAA WCCILGLISI VLTKVSANEG
560 570 580 590 600
FIPINKNLWS ISYVTTLSCF AFFILLILYP VVDVKGLWTG TPFFYPGMNS
610 620 630 640 650
ILVYVGHEVL ENYFPFQWKL ADEQSHKEHL IQNIVATALW VLIAYVLYKK

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

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ3UDW8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000040356.

PTM databases

PhosphoSiteiQ3UDW8.

Proteomic databases

MaxQBiQ3UDW8.
PaxDbiQ3UDW8.
PRIDEiQ3UDW8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi138050.
MGIiMGI:1196297. Hgsnat.

Phylogenomic databases

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

Enzyme and pathway databases

BRENDAi2.3.1.78. 3474.
ReactomeiREACT_343711. HS-GAG degradation.

Miscellaneous databases

ChiTaRSiHgsnat. mouse.
NextBioi308520.
PROiQ3UDW8.
SOURCEiSearch...

Gene expression databases

BgeeiQ3UDW8.
CleanExiMM_HGSNAT.
GenevisibleiQ3UDW8. MM.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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: June 24, 2015
This is version 79 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

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 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.