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Heparan-alpha-glucosaminide N-acetyltransferase (EC 2.3.1.78) (Transmembrane protein 76)

 HGNAT_MOUSE             Reviewed;         656 AA.
Q3UDW8; E9QNP9; Q3TWK5; Q8CBU7; Q8CIE1;
23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
23-MAY-2018, entry version 97.
RecName: Full=Heparan-alpha-glucosaminide N-acetyltransferase;
EC=2.3.1.78;
AltName: Full=Transmembrane protein 76;
Name=Hgsnat; Synonyms=D8Ertd354e, Tmem76;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1/2).
STRAIN=C57BL/6J; TISSUE=Bone marrow, and Urinary bladder;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
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.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 21-656 (ISOFORM 1/2).
STRAIN=FVB/N; TISSUE=Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=16960811; DOI=10.1086/508068;
Fan X., Zhang H., Zhang S., Bagshaw R.D., Tropak M.B., Callahan J.W.,
Mahuran D.J.;
"Identification of the gene encoding the enzyme deficient in
mucopolysaccharidosis IIIC (Sanfilippo disease type C).";
Am. J. Hum. Genet. 79:738-744(2006).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-249, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Mast cell;
PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
Kawakami T., Salomon A.R.;
"Quantitative time-resolved phosphoproteomic analysis of mast cell
signaling.";
J. Immunol. 179:5864-5876(2007).
[6]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-157.
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[8]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=25859010; DOI=10.1093/hmg/ddv118;
Haer-Wigman L., Newman H., Leibu R., Bax N.M., Baris H.N., Rizel L.,
Banin E., Massarweh A., Roosing S., Lefeber D.J.,
Zonneveld-Vrieling M.N., Isakov O., Shomron N., Sharon D.,
Den Hollander A.I., Hoyng C.B., Cremers F.P., Ben-Yosef T.;
"Non-syndromic retinitis pigmentosa due to mutations in the
mucopolysaccharidosis type IIIC gene, heparan-alpha-glucosaminide N-
acetyltransferase (HGSNAT).";
Hum. Mol. Genet. 24:3742-3751(2015).
-!- 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.
{ECO:0000269|PubMed:16960811}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + heparan sulfate alpha-D-
glucosaminide = CoA + heparan sulfate N-acetyl-alpha-D-
glucosaminide. {ECO:0000269|PubMed:16960811}.
-!- SUBUNIT: Homooligomer. Homooligomerization is necessary for enzyme
activity (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Lysosome membrane
{ECO:0000269|PubMed:16960811}; Multi-pass membrane protein
{ECO:0000269|PubMed:16960811}. 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). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=2;
Name=1;
IsoId=Q3UDW8-1; Sequence=Displayed;
Name=2;
IsoId=Q3UDW8-2; Sequence=VSP_040505;
-!- TISSUE SPECIFICITY: Expressed in the retina.
{ECO:0000269|PubMed:25859010}.
-!- DEVELOPMENTAL STAGE: Expressed in the developing eye as early as
embryonic day 14 (E14), with equal high expression levels after
birth (postnatal day 0 (P0) and postnatal day 30 (P30)).
{ECO:0000269|PubMed:25859010}.
-!- PTM: 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.
{ECO:0000250}.
-!- PTM: Glycosylated. {ECO:0000250}.
-!- MISCELLANEOUS: A signal sequence is predicted but has been shown
not to be cleaved in the reticulum endoplasmic. {ECO:0000250}.
-!- SEQUENCE CAUTION:
Sequence=AAH24084.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAC29006.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAE31601.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAE35261.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAE35603.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AK035264; BAC29006.1; ALT_INIT; mRNA.
EMBL; AK149883; BAE29143.1; -; mRNA.
EMBL; AK152926; BAE31601.1; ALT_INIT; mRNA.
EMBL; AK159649; BAE35261.1; ALT_INIT; mRNA.
EMBL; AK160068; BAE35603.1; ALT_INIT; mRNA.
EMBL; AC093366; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC024084; AAH24084.1; ALT_INIT; mRNA.
CCDS; CCDS40309.1; -. [Q3UDW8-1]
RefSeq; NP_084160.1; NM_029884.1. [Q3UDW8-1]
UniGene; Mm.235663; -.
UniGene; Mm.28326; -.
UniGene; Mm.285785; -.
ProteinModelPortal; Q3UDW8; -.
STRING; 10090.ENSMUSP00000040356; -.
iPTMnet; Q3UDW8; -.
PhosphoSitePlus; Q3UDW8; -.
SwissPalm; Q3UDW8; -.
MaxQB; Q3UDW8; -.
PaxDb; Q3UDW8; -.
PeptideAtlas; Q3UDW8; -.
PRIDE; Q3UDW8; -.
Ensembl; ENSMUST00000037609; ENSMUSP00000040356; ENSMUSG00000037260. [Q3UDW8-1]
GeneID; 52120; -.
KEGG; mmu:52120; -.
UCSC; uc009lhg.1; mouse. [Q3UDW8-1]
CTD; 138050; -.
MGI; MGI:1196297; Hgsnat.
eggNOG; KOG4683; Eukaryota.
eggNOG; COG4299; LUCA.
GeneTree; ENSGT00390000001491; -.
HOGENOM; HOG000006803; -.
HOVERGEN; HBG081599; -.
InParanoid; Q3UDW8; -.
KO; K10532; -.
OMA; KHSSWNG; -.
OrthoDB; EOG091G042R; -.
TreeFam; TF324790; -.
BRENDA; 2.3.1.78; 3474.
Reactome; R-MMU-2024096; HS-GAG degradation.
Reactome; R-MMU-6798695; Neutrophil degranulation.
ChiTaRS; Hgsnat; mouse.
PRO; PR:Q3UDW8; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000037260; -.
CleanEx; MM_HGSNAT; -.
ExpressionAtlas; Q3UDW8; baseline and differential.
Genevisible; Q3UDW8; MM.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
GO; GO:0015019; F:heparan-alpha-glucosaminide N-acetyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0016746; F:transferase activity, transferring acyl groups; ISS:UniProtKB.
GO; GO:0007041; P:lysosomal transport; ISS:UniProtKB.
GO; GO:0051259; P:protein complex oligomerization; ISS:UniProtKB.
InterPro; IPR012429; DUF1624.
Pfam; PF07786; DUF1624; 1.
1: Evidence at protein level;
Acyltransferase; Alternative initiation; Complete proteome;
Disulfide bond; Glycoprotein; Lysosome; Membrane; Phosphoprotein;
Reference proteome; Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 656 Heparan-alpha-glucosaminide N-
acetyltransferase.
/FTId=PRO_0000273154.
TOPO_DOM 1 185 Lumenal, vesicle. {ECO:0000255}.
TRANSMEM 186 206 Helical. {ECO:0000255}.
TOPO_DOM 207 268 Cytoplasmic. {ECO:0000255}.
TRANSMEM 269 289 Helical. {ECO:0000255}.
TOPO_DOM 290 295 Lumenal, vesicle. {ECO:0000255}.
TRANSMEM 296 316 Helical. {ECO:0000255}.
TOPO_DOM 317 338 Cytoplasmic. {ECO:0000255}.
TRANSMEM 339 359 Helical. {ECO:0000255}.
TOPO_DOM 360 367 Lumenal, vesicle. {ECO:0000255}.
TRANSMEM 368 388 Helical. {ECO:0000255}.
TOPO_DOM 389 413 Cytoplasmic. {ECO:0000255}.
TRANSMEM 414 434 Helical. {ECO:0000255}.
TOPO_DOM 435 493 Lumenal, vesicle. {ECO:0000255}.
TRANSMEM 494 514 Helical. {ECO:0000255}.
TOPO_DOM 515 522 Cytoplasmic. {ECO:0000255}.
TRANSMEM 523 543 Helical. {ECO:0000255}.
TOPO_DOM 544 557 Lumenal, vesicle. {ECO:0000255}.
TRANSMEM 558 578 Helical. {ECO:0000255}.
TOPO_DOM 579 585 Cytoplasmic. {ECO:0000255}.
TRANSMEM 586 606 Helical. {ECO:0000255}.
TOPO_DOM 607 627 Lumenal, vesicle. {ECO:0000255}.
TRANSMEM 628 648 Helical. {ECO:0000255}.
TOPO_DOM 649 656 Cytoplasmic. {ECO:0000255}.
REGION 641 656 Lysosomal targeting region.
{ECO:0000250}.
ACT_SITE 290 290 {ECO:0000250}.
MOD_RES 238 238 Phosphoserine.
{ECO:0000250|UniProtKB:Q68CP4}.
MOD_RES 240 240 Phosphoserine.
{ECO:0000250|UniProtKB:Q68CP4}.
MOD_RES 249 249 Phosphotyrosine.
{ECO:0000244|PubMed:17947660}.
CARBOHYD 137 137 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 157 157 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
DISULFID 146 455 {ECO:0000250}.
VAR_SEQ 1 32 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_040505.
CONFLICT 23 23 R -> H (in Ref. 3; AAH24084).
{ECO:0000305}.
CONFLICT 24 24 N -> S (in Ref. 3; AAH24084).
{ECO:0000305}.
CONFLICT 222 222 T -> A (in Ref. 3; AAH24084).
{ECO:0000305}.
CONFLICT 242 242 A -> G (in Ref. 1; BAE35261).
{ECO:0000305}.
CONFLICT 329 329 L -> F (in Ref. 1; BAE29143).
{ECO:0000305}.
SEQUENCE 656 AA; 72504 MW; 8FAE5EBECED5CCE3 CRC64;
MTGGSSSRRR RAEERSSAAG TERNSRREAV GGMGAGPALA ALLLAGSVLS ATLLAPGRRA
EPDLDEKRNV ELKMDQALLL IHNELLGTSL TVYWKSDDCY QCTFQPLANV SHGGKPAKPS
VAPVSVSTQH GSILQVNSTS EERAACRLEY KFGEFGNYSL LVQHASSGAN KIACDIIVNE
NPVDSNLPVS IAFLVGLALI VAVSLLRLLL SLDDVNNWIS KTIASRETDR LINSELGSPS
RADPLSADYQ PETRRSSANR LRCVDTFRGL ALVLMVFVNY GGGKYWYFKH SSWNGLTVAD
LVFPWFVFIM GTSIFLSMTS ILQRGCSKLK LLGKIVWRSF LLICIGVIIV NPNYCLGPLS
WDKVRIPGVL QRLGVTYFVV AVLEFFFWKP VPDSCTLESS CFSLRDITSS WPQWLTILTL
ESIWLALTFF LPVPGCPTGY LGPGGIGDLG KYPHCTGGAA GYIDRLLLGD NHLYQHPSST
VLYHTEVAYD PEGVLGTINS IVMAFLGVQA GKILVYYKDQ TKAILTRFAA WCCILGLISI
VLTKVSANEG FIPINKNLWS ISYVTTLSCF AFFILLILYP VVDVKGLWTG TPFFYPGMNS
ILVYVGHEVL ENYFPFQWKL ADEQSHKEHL IQNIVATALW VLIAYVLYKK KLFWKI


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