Q3UDW8 (HGNAT_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Heparan-alpha-glucosaminide N-acetyltransferase
EC=2.3.1.78

Alternative name(s):
Transmembrane protein 76

Gene names

Name:	Hgsnat
Synonyms:	D8Ertd354e, Tmem76

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	656 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Lysosome Membrane
Coding sequence diversity	Alternative initiation
Domain	Transmembrane Transmembrane helix
Molecular function	Acyltransferase Transferase
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	lysosomal transport Inferred from sequence or structural similarity. Source: UniProtKB protein oligomerization Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW lysosomal membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	heparan-alpha-glucosaminide N-acetyltransferase activity Inferred from electronic annotation. Source: EC transferase activity, transferring acyl groups Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 656	656	Heparan-alpha-glucosaminide N-acetyltransferase		PRO_0000273154
Regions
	Topological domain	1 – 185	185	Lumenal, vesicle Potential
	Transmembrane	186 – 206	21	Helical; Potential
	Topological domain	207 – 268	62	Cytoplasmic Potential
	Transmembrane	269 – 289	21	Helical; Potential
	Topological domain	290 – 295	6	Lumenal, vesicle Potential
	Transmembrane	296 – 316	21	Helical; Potential
	Topological domain	317 – 338	22	Cytoplasmic Potential
	Transmembrane	339 – 359	21	Helical; Potential
	Topological domain	360 – 367	8	Lumenal, vesicle Potential
	Transmembrane	368 – 388	21	Helical; Potential
	Topological domain	389 – 413	25	Cytoplasmic Potential
	Transmembrane	414 – 434	21	Helical; Potential
	Topological domain	435 – 493	59	Lumenal, vesicle Potential
	Transmembrane	494 – 514	21	Helical; Potential
	Topological domain	515 – 522	8	Cytoplasmic Potential
	Transmembrane	523 – 543	21	Helical; Potential
	Topological domain	544 – 557	14	Lumenal, vesicle Potential
	Transmembrane	558 – 578	21	Helical; Potential
	Topological domain	579 – 585	7	Cytoplasmic Potential
	Transmembrane	586 – 606	21	Helical; Potential
	Topological domain	607 – 627	21	Lumenal, vesicle Potential
	Transmembrane	628 – 648	21	Helical; Potential
	Topological domain	649 – 656	8	Cytoplasmic Potential
	Region	641 – 656	16	Lysosomal targeting region By similarity
Sites
	Active site	290	1	By similarity
Amino acid modifications
	Modified residue	234	1	Phosphoserine Ref.6
	Modified residue	240	1	Phosphoserine By similarity
	Modified residue	249	1	Phosphotyrosine Ref.5
	Glycosylation	137	1	N-linked (GlcNAc...) Potential
	Glycosylation	157	1	N-linked (GlcNAc...) Ref.7
	Disulfide bond	146 ↔ 455		By similarity
Natural variations
	Alternative sequence	1 – 32	32	Missing in isoform 2.		VSP_040505
Experimental info
	Sequence conflict	23	1	R → H in AAH24084. Ref.3
	Sequence conflict	24	1	N → S in AAH24084. Ref.3
	Sequence conflict	222	1	T → A in AAH24084. Ref.3
	Sequence conflict	242	1	A → G in BAE35261. Ref.1
	Sequence conflict	329	1	L → F in BAE29143. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: 8FAE5EBECED5CCE3	FASTA	656	72,504
	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
	Isoform 2 [UniParc]. Checksum: 5272EA184EB5BDA4	FASTA	624	69,100
	10 20 30 40 50 60 MGAGPALAAL LLAGSVLSAT LLAPGRRAEP DLDEKRNVEL KMDQALLLIH NELLGTSLTV 70 80 90 100 110 120 YWKSDDCYQC TFQPLANVSH GGKPAKPSVA PVSVSTQHGS ILQVNSTSEE RAACRLEYKF 130 140 150 160 170 180 GEFGNYSLLV QHASSGANKI ACDIIVNENP VDSNLPVSIA FLVGLALIVA VSLLRLLLSL 190 200 210 220 230 240 DDVNNWISKT IASRETDRLI NSELGSPSRA DPLSADYQPE TRRSSANRLR CVDTFRGLAL 250 260 270 280 290 300 VLMVFVNYGG GKYWYFKHSS WNGLTVADLV FPWFVFIMGT SIFLSMTSIL QRGCSKLKLL 310 320 330 340 350 360 GKIVWRSFLL ICIGVIIVNP NYCLGPLSWD KVRIPGVLQR LGVTYFVVAV LEFFFWKPVP 370 380 390 400 410 420 DSCTLESSCF SLRDITSSWP QWLTILTLES IWLALTFFLP VPGCPTGYLG PGGIGDLGKY 430 440 450 460 470 480 PHCTGGAAGY IDRLLLGDNH LYQHPSSTVL YHTEVAYDPE GVLGTINSIV MAFLGVQAGK 490 500 510 520 530 540 ILVYYKDQTK AILTRFAAWC CILGLISIVL TKVSANEGFI PINKNLWSIS YVTTLSCFAF 550 560 570 580 590 600 FILLILYPVV DVKGLWTGTP FFYPGMNSIL VYVGHEVLEN YFPFQWKLAD EQSHKEHLIQ 610 620 NIVATALWVL IAYVLYKKKL FWKI

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY. Tissue: Mast cell.
[6]	"The phagosomal proteome in interferon-gamma-activated macrophages." Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P. Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234, MASS SPECTROMETRY. Tissue: Macrophage.
[7]	"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, MASS SPECTROMETRY.
+	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.
IPI	IPI00317488. IPI00975056.
RefSeq	NP_084160.1. NM_029884.1.
UniGene	Mm.28326.
3D structure databases
ProteinModelPortal	Q3UDW8.
ModBase	Search...
PTM databases
PhosphoSite	Q3UDW8.
Proteomic databases
PaxDb	Q3UDW8.
PRIDE	Q3UDW8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000037609; ENSMUSP00000040356; ENSMUSG00000037260.
GeneID	52120.
KEGG	mmu:52120.
UCSC	uc009lhg.1. mouse.
Organism-specific databases
CTD	138050.
MGI	MGI:1196297. Hgsnat.
Phylogenomic databases
eggNOG	COG4299.
GeneTree	ENSGT00390000001491.
HOGENOM	HOG000006803.
HOVERGEN	HBG081599.
InParanoid	Q3UDW8.
KO	K10532.
OMA	KHSSWNG.
OrthoDB	EOG4548Z7.
Gene expression databases
Bgee	Q3UDW8.
CleanEx	MM_HGSNAT.
Genevestigator	Q3UDW8.
Family and domain databases
InterPro	IPR012429. DUF1624. [Graphical view]
Pfam	PF07786. DUF1624. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	HGSNAT. mouse.
NextBio	308520.
SOURCE	Search...

Entry information

Entry name

HGNAT_MOUSE

Accession

Primary (citable) accession number: Q3UDW8
Secondary accession number(s): E9QNP9 , Q3TWK5, Q8CBU7, Q8CIE1

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2007
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 62 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program