NAGLU

NAGLU
Dostupne strukture PDB Pretraga ortologa: PDBe RCSB Spisak PDB ID kodova 4XWH
Identifikatori
Aliasi	NAGLU
Vanjski ID-jevi	OMIM: 609701 MGI: 1351641 HomoloGene: 222 GeneCards: NAGLU
Lokacija gena (čovjek) Hrom. Hromosom 17 (čovjek) Bend 17q21.2 Početak 42,536,241 bp Kraj 42,544,449 bp
Lokacija gena (miš) Hrom. Hromosom 11 (miš) Bend 11|11 D Početak 100,960,838 bp Kraj 100,968,498 bp
Ontologija gena Molekularna funkcija • alpha-N-acetylglucosaminidase activity • hydrolase activity • hydrolase activity, acting on glycosyl bonds Ćelijska komponenta • Lizozom • lysosomal lumen • Egzosom Biološki proces • metabolizam • inner ear receptor cell development • lysosome organization • glycosaminoglycan catabolic process • retinal rod cell development • cerebellar Purkinje cell layer development • nervous system development • middle ear morphogenesis • locomotor rhythm Izvori:Amigo / QuickGO
Ortolozi
Vrste	Čovjek	Miš
Entrez	4669	27419
Ensembl	ENSG00000108784	ENSMUSG00000001751
UniProt	P54802	O88325
RefSeq (mRNK)	NM_000263	NM_013792
RefSeq (bjelančevina)	NP_000254	NP_038820
Lokacija (UCSC)	Chr 17: 42.54 – 42.54 Mb	Chr 11: 100.96 – 100.97 Mb
PubMed pretraga
Wikipodaci
Pogledaj/uredi – čovjek Pogledaj/uredi – miš

N-acetilglukozaminidaza alfa je protein koji je kod ljudi kodiran genom NAGLU.

Dužina polipeptidnog lanca je 743 aminokiseline, a molekulska težina 82.266 Da.

Aminokiselinska sekvenca

Simboli

C: Cistein
D: Asparaginska kiselina
E: Glutaminska kiselina
F: Fenilalanin
G: Glicin
H: Histidin
I: Izoleucin
K: Lizin
L: Leucin
M: Metionin
N: Asparagin
P: Prolin
Q: Glutamin
R: Arginin
S: Serin
T: Treonin
V: Valin
W: Triptofan
Y: Tirozin

10		20		30		40		50
MEAVAVAAAV		GVLLLAGAGG		AAGDEAREAA		AVRALVARLL		GPGPAADFSV
SVERALAAKP		GLDTYSLGGG		GAARVRVRGS		TGVAAAAGLH		RYLRDFCGCH
VAWSGSQLRL		PRPLPAVPGE		LTEATPNRYR		YYQNVCTQSY		SFVWWDWARW
EREIDWMALN		GINLALAWSG		QEAIWQRVYL		ALGLTQAEIN		EFFTGPAFLA
WGRMGNLHTW		DGPLPPSWHI		KQLYLQHRVL		DQMRSFGMTP		VLPAFAGHVP
EAVTRVFPQV		NVTKMGSWGH		FNCSYSCSFL		LAPEDPIFPI		IGSLFLRELI
KEFGTDHIYG		ADTFNEMQPP		SSEPSYLAAA		TTAVYEAMTA		VDTEAVWLLQ
GWLFQHQPQF		WGPAQIRAVL		GAVPRGRLLV		LDLFAESQPV		YTRTASFQGQ
PFIWCMLHNF		GGNHGLFGAL		EAVNGGPEAA		RLFPNSTMVG		TGMAPEGISQ
NEVVYSLMAE		LGWRKDPVPD		LAAWVTSFAA		RRYGVSHPDA		GAAWRLLLRS
VYNCSGEACR		GHNRSPLVRR		PSLQMNTSIW		YNRSDVFEAW		RLLLTSAPSL
ATSPAFRYDL		LDLTRQAVQE		LVSLYYEEAR		SAYLSKELAS		LLRAGGVLAY
ELLPALDEVL		ASDSRFLLGS		WLEQARAAAV		SEAEADFYEQ		NSRYQLTLWG
PEGNILDYAN		KQLAGLVANY		YTPRWRLFLE		ALVDSVAQGI		PFQQHQFDKN
VFQLEQAFVL		SKQRYPSQPR		GDTVDLAKKI		FLKYYPRWVA		GSW

Funkcija

Ovaj gen kodira enzim koji razgrađuje heparan sulfat hidrolizom krajnjih ostataka N-acetil-D-glukozamina u N-acetil-alfa-D-glukozaminidima.

Klinički značaj

Defekti u ovom genu uzrok su mukopolisaharidoza tipa IIIB (MPS-IIIB), takođe poznat kao Sanfilippov sindrom B. Ovu bolest karakterizira akumulacija lizosoma i izlučivanje heparan-sulfata urinom.

Dopunska literatura

• Weber B, Blanch L, Clements PR, Scott HS, Hopwood JJ (juni 1996). "Cloning and expression of the gene involved in Sanfilippo B syndrome (mucopolysaccharidosis III B)". Human Molecular Genetics. 5 (6): 771–7. doi:10.1093/hmg/5.6.771. PMID 8776591.
• Clark AG, Glanowski S, Nielsen R, Thomas PD, Kejariwal A, Todd MA, Tanenbaum DM, Civello D, Lu F, Murphy B, Ferriera S, Wang G, Zheng X, White TJ, Sninsky JJ, Adams MD, Cargill M (decembar 2003). "Inferring nonneutral evolution from human-chimp-mouse orthologous gene trios". Science. 302 (5652): 1960–3. doi:10.1126/science.1088821. PMID 14671302. S2CID 6682593.
• Yogalingam G, Hopwood JJ (oktobar 2001). "Molecular genetics of mucopolysaccharidosis type IIIA and IIIB: Diagnostic, clinical, and biological implications". Human Mutation. 18 (4): 264–81. doi:10.1002/humu.1189. PMID 11668611. S2CID 25731955.
• Zhao HG, Li HH, Bach G, Schmidtchen A, Neufeld EF (juni 1996). "The molecular basis of Sanfilippo syndrome type B". Proceedings of the National Academy of Sciences of the United States of America. 93 (12): 6101–5. doi:10.1073/pnas.93.12.6101. PMC 39196. PMID 8650226.
• Winder-Rhodes SE, Garcia-Reitböck P, Ban M, Evans JR, Jacques TS, Kemppinen A, Foltynie T, Williams-Gray CH, Chinnery PF, Hudson G, Burn DJ, Allcock LM, Sawcer SJ, Barker RA, Spillantini MG (februar 2012). "Genetic and pathological links between Parkinson's disease and the lysosomal disorder Sanfilippo syndrome". Movement Disorders. 27 (2): 312–5. doi:10.1002/mds.24029. PMID 22102531. S2CID 4834914.
• Sasaki T, Sukegawa K, Masue M, Fukuda S, Tomatsu S, Orii T (novembar 1991). "Purification and partial characterization of alpha-N-acetylglucosaminidase from human liver". Journal of Biochemistry. 110 (5): 842–6. doi:10.1093/oxfordjournals.jbchem.a123668. PMID 1783617.
• Vance JM, Pericak-Vance MA, Elston RC, Conneally PM, Namboodiri KK, Wappner RS, Yu PL (1980). "Evidence of genetic variation for alpha-N-acetyl-D-glucosaminidase in black and white populations: a new polymorphism". American Journal of Medical Genetics. 7 (2): 131–40. doi:10.1002/ajmg.1320070207. PMID 6781343.
• Schmidtchen A, Greenberg D, Zhao HG, Li HH, Huang Y, Tieu P, Zhao HZ, Cheng S, Zhao Z, Whitley CB, Di Natale P, Neufeld EF (januar 1998). "NAGLU mutations underlying Sanfilippo syndrome type B". American Journal of Human Genetics. 62 (1): 64–9. doi:10.1086/301685. PMC 1376809. PMID 9443878.
• Ayala JM, Goyal S, Liverton NJ, Claremon DA, O'Keefe SJ, Hanlon WA (juni 2000). "Serum-induced monocyte differentiation and monocyte chemotaxis are regulated by the p38 MAP kinase signal transduction pathway". Journal of Leukocyte Biology. 67 (6): 869–75. doi:10.1002/jlb.67.6.869. PMID 10857861. S2CID 28719955.