Q5RC84 (HEXA_PONAB) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Beta-hexosaminidase subunit alpha
EC=3.2.1.52

Alternative name(s):
Beta-N-acetylhexosaminidase subunit alpha
Short name=Hexosaminidase subunit A
N-acetyl-beta-glucosaminidase subunit alpha

Gene names

Name:

HEXA

Organism

Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]

Taxonomic identifier

9601 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Ponginae › Pongo

Protein attributes

Sequence length	529 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Responsible for the degradation of GM2 gangliosides, and a variety of other molecules containing terminal N-acetyl hexosamines, in the brain and other tissues By similarity.
Catalytic activity	Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.
Subcellular location	Lysosome By similarity.
Sequence similarities	Belongs to the glycosyl hydrolase 20 family.

Ontologies

Keywords
Cellular component	Lysosome
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	adult walking behavior Inferred from electronic annotation. Source: Compara carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro cell morphogenesis involved in neuron differentiation Inferred from electronic annotation. Source: Compara ganglioside catabolic process Inferred from electronic annotation. Source: Compara glycosaminoglycan metabolic process Inferred from electronic annotation. Source: Compara lipid storage Inferred from electronic annotation. Source: Compara lysosome organization Inferred from electronic annotation. Source: Compara myelination Inferred from electronic annotation. Source: Compara neuromuscular process controlling balance Inferred from electronic annotation. Source: Compara neuromuscular process controlling posture Inferred from electronic annotation. Source: Compara sensory perception of sound Inferred from electronic annotation. Source: Compara sexual reproduction Inferred from electronic annotation. Source: Compara skeletal system development Inferred from electronic annotation. Source: Compara
Cellular_component	lysosome Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from electronic annotation. Source: Compara
Molecular_function	beta-N-acetylhexosaminidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 22	22	Potential
	Propeptide	23 – 88	66	By similarity		PRO_0000011997
	Chain	89 – 529	441	Beta-hexosaminidase subunit alpha		PRO_0000011998
Regions
	Region	423 – 424	2	Critical for hydrolyzis GM2 gangliosides By similarity
Sites
	Active site	323	1	Proton donor By similarity
Amino acid modifications
	Glycosylation	115	1	N-linked (GlcNAc...) Potential
	Glycosylation	157	1	N-linked (GlcNAc...) Potential
	Glycosylation	295	1	N-linked (GlcNAc...) Potential
	Disulfide bond	58 ↔ 104		By similarity
	Disulfide bond	277 ↔ 328		By similarity
	Disulfide bond	505 ↔ 522		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5RC84 [UniParc]. Last modified December 21, 2004. Version 1. Checksum: 8D00068F3EBDBA74	FASTA	529	60,605
	10 20 30 40 50 60 MASSRLWFSL LLAAALAGRA TALWPWPQNI QTSDQRYVLY PNNFQFQYDV SSAAQPGCSV 70 80 90 100 110 120 LDEAFQRYRD LLFGSGSWPR PYLTGKRHTL EKNVLVVSVV TPGCNQLPTL ESVENYTLTI 130 140 150 160 170 180 NDDQCLLLSE TVWGALRGLE TFSQLVWKSA EGTFFINKTE IEDFPRFPHR GLLLDTSRHY 190 200 210 220 230 240 LPLSSILDTL DVMAYNKLNV FHWHLVDDPS FPYESFTFPE LMRKGSYNPV THIYTAQDVK 250 260 270 280 290 300 EVIEYARLRG IRVLAEFDTP GHTLSWGPGI PGLLTPCYSG SEPSGTFGPV NPSLNNTYEF 310 320 330 340 350 360 MSTFFLEVSS VFPDFYLHLG GDEVDFTCWK SNPDIQDFMR KKGFGEDFKQ LESFYIQTLL 370 380 390 400 410 420 DIVSSYGKGY VVWQEVFDNK VKIRPDTIIQ VWREDIPVNY MKELELVTKA GFRALLSAPW 430 440 450 460 470 480 YLNRISYGPD WKDFYVVEPL AFEGTPEQKA LVIGGEACMW GEYVDNTNLV PRLWPRAGAV 490 500 510 520 AERLWSNKLT SDLTFAYERL SHFRCELLRR GVQAQPLNVG FCEQEFEQT

References

[1]	The German cDNA consortium Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain cortex.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR858396 Transcribed RNA. Translation: CAH90623.1.
RefSeq	NP_001192280.1. NM_001205351.1.
UniGene	Pab.19807.
3D structure databases
ProteinModelPortal	Q5RC84.
SMR	Q5RC84. Positions 23-528.
ModBase	Search...
Protein family/group databases
CAZy	GH20. Glycoside Hydrolase Family 20.
Proteomic databases
PRIDE	Q5RC84.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSPPYT00000007808; ENSPPYP00000007503; ENSPPYG00000006616.
GeneID	100438794.
KEGG	pon:100438794.
Organism-specific databases
CTD	3073.
Phylogenomic databases
GeneTree	ENSGT00390000008107.
HOVERGEN	HBG005961.
InParanoid	Q5RC84.
KO	K12373.
OMA	KVKVRPD.
Family and domain databases
Gene3D	3.20.20.80. 1 hit.
InterPro	IPR025705. Beta_hexosaminidase_sua/sub. IPR015883. Glyco_hydro_20_cat-core. IPR015882. Glyco_hydro_20b. IPR013781. Glyco_hydro_catalytic_dom. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
Pfam	PF00728. Glyco_hydro_20. 1 hit. PF02838. Glyco_hydro_20b. 1 hit. [Graphical view]
PIRSF	PIRSF001093. B-hxosamndse_ab_euk_. 1 hit.
PRINTS	PR00738. GLHYDRLASE20.
SUPFAM	SSF51445. Glyco_hydro_cat. 1 hit.
ProtoNet	Search...

Entry information

Entry name

HEXA_PONAB

Accession

Primary (citable) accession number: Q5RC84

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2005
Last sequence update:	December 21, 2004
Last modified:	May 1, 2013
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program