Reviewed, UniProtKB/Swiss-Prot Q29548 (HEXB_PIG)

Names and origin

Protein names

Recommended name:
    Beta-hexosaminidase subunit beta
    EC=3.2.1.52
Alternative name(s):
    N-acetyl-beta-glucosaminidase subunit beta
    Beta-N-acetylhexosaminidase subunit beta
      Short name=Hexosaminidase subunit B
    65 kDa epididymal boar protein

Gene names

Name:

HEXB

Organism

Sus scrofa (Pig)

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length	531 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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.
Sequence similarities	Belongs to the glycosyl hydrolase 20 family.
Sequence caution	The sequence CAA63123.1 differs from that shown. Reason: Frameshift at positions 3 and 16.

Ontologies

Keywords
Cellular component	Lysosome
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	lysosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	beta-N-acetylhexosaminidase activity Inferred from electronic annotation. Source: EC cation binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 21	21	Potential
	Chain	22 – 531	510	Beta-hexosaminidase subunit beta		PRO_0000012007
Sites
	Active site	329	1	Proton donor By similarity
Amino acid modifications
	Glycosylation	120	1	N-linked (GlcNAc...) Potential
	Glycosylation	164	1	N-linked (GlcNAc...) Potential
	Glycosylation	301	1	N-linked (GlcNAc...) Potential
	Disulfide bond	67 ↔ 111		By similarity
	Disulfide bond	283 ↔ 334		By similarity
	Disulfide bond	508 ↔ 525		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q29548-1 [UniParc]. Last modified May 10, 2005. Version 2. Checksum: F55D62D6937E51C5	FASTA	531	61,050
	10 20 30 40 50 60 MEVLPGLLRL LAALVVAERW ARDTSGAESL GLWPLPFAVD ISPRSLHLSP NNFFFGHSPT 70 80 90 100 110 120 SKAGSSCEIL QEAFRRYYDF IFGFYKWHQG SYQLCFGTEL QQLQVHVESE CDTFPSISSN 130 140 150 160 170 180 ESYVLHVKGP EALLRANTVW GALRGLETFS QLIYQDSYGT FTVNESEIID FPRFPHRGIL 190 200 210 220 230 240 IDTGRHFLSV KTIFKTLDAM AFNKFNVLHW HIVDDQSFPY QSINFGVLSS KGSYSLSHVY 250 260 270 280 290 300 TPNDVRMVIE YARIRGIRVM PEFDTPGHSR SWGKGQKDLL TPCYRKQVLS GTFGPINPIL 310 320 330 340 350 360 NTTYNFLSKF FKEISTVFPD EFIHIGGDEV DFDCWASNSE ILQFMQEKGF SQISLNSNLC 370 380 390 400 410 420 TVFKISNMIS AMKKRPIVWQ EAFDGRDKFM PGTVVQVWKI EDYKWEQSLI TKAGFPVILS 430 440 450 460 470 480 APWYLDLISY GQDWKNYYEV EPQDFPGSDK ERKRVLGGEA CLWGEYVDAT NLTPRLWPRA 490 500 510 520 530 SAVGERLWSH KDVRDIHDAY SRLTIHRCRM VRRGIAAEPL FTGYCNHEHR M

References

[1]	"Purification, cloning and sequencing analysis of B-N-acetyl-hexosaminidase from epididymal boar." Syntin P., Okamura N., Guillou F., Dacheux F., Dacheux J.-L. Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Epididymis.
[2]	"Characterization and identification of proteins secreted in the various regions of the adult boar epididymis." Syntin P., Dacheux F., Druart X., Gatti J.L., Okamura N., Dacheux J.-L. Biol. Reprod. 55:956-974(1996) [PubMed: 8902205] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE. Tissue: Epididymis.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X92379 mRNA. Translation: CAA63123.1. Frameshift.
RefSeq	NP_999086.1.
UniGene	Ssc.3196
3D structure databases
HSSP	HSSP built from PDB template 1NOW based on UniProtKB P07686.
ModBase	Search...
Protein family/group databases
CAZy	GH20. Glycoside Hydrolase Family 20.
Genome annotation databases
GeneID	396958.
KEGG	ssc:396958.
Organism-specific databases
CTD	396958.
Phylogenomic databases
HOVERGEN	Q29548.
Enzyme and pathway databases
BRENDA	3.2.1.52. 249.
Family and domain databases
InterPro	IPR001540. Glyco_hydro_20. IPR015883. Glyco_hydro_20_cat-core. IPR013781. Glyco_hydro_sg_catalytic. IPR015882. HexNAc-like_b. [Graphical view]
Gene3D	G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PANTHER	PTHR22600. Glyco_hydro_20. 1 hit.
Pfam	PF00728. Glyco_hydro_20. 1 hit. PF02838. Glyco_hydro_20b. 1 hit. [Graphical view]
PRINTS	PR00738. GLHYDRLASE20.
ProtoNet	Search...

Entry information

Entry name

HEXB_PIG

Accession

Primary (citable) accession number: Q29548

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	May 10, 2005
Last modified:	September 1, 2009
This is version 59 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)