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Q29548

- HEXB_PIG

UniProt

Q29548 - HEXB_PIG

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Protein

Beta-hexosaminidase subunit beta

Gene

HEXB

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

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 activityi

Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei329 – 3291Proton donorBy similarity

GO - Molecular functioni

  1. beta-N-acetylhexosaminidase activity Source: UniProtKB-EC

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Protein family/group databases

CAZyiGH20. Glycoside Hydrolase Family 20.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-hexosaminidase subunit beta (EC:3.2.1.52)
Alternative name(s):
65 kDa epididymal boar protein
Beta-N-acetylhexosaminidase subunit beta
Short name:
Hexosaminidase subunit B
N-acetyl-beta-glucosaminidase subunit beta
Gene namesi
Name:HEXB
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. lysosome Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Chaini22 – 531510Beta-hexosaminidase subunit betaPRO_0000012007Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi67 ↔ 111By similarity
Glycosylationi120 – 1201N-linked (GlcNAc...)Sequence Analysis
Glycosylationi164 – 1641N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi283 ↔ 334By similarity
Glycosylationi301 – 3011N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi508 ↔ 525By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ29548.
PRIDEiQ29548.

Interactioni

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000014965.

Structurei

3D structure databases

ProteinModelPortaliQ29548.
SMRiQ29548. Positions 31-527.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 20 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3525.
HOGENOMiHOG000157972.
HOVERGENiHBG005961.
InParanoidiQ29548.
KOiK12373.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
3.30.379.10. 1 hit.
InterProiIPR025705. Beta_hexosaminidase_sua/sub.
IPR029018. Chitobiase/Hex_dom_2-like.
IPR015883. Glyco_hydro_20_cat-core.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR029019. HEX_eukaryotic_N.
[Graphical view]
PfamiPF00728. Glyco_hydro_20. 1 hit.
PF14845. Glycohydro_20b2. 1 hit.
[Graphical view]
PIRSFiPIRSF001093. B-hxosamndse_ab_euk_. 1 hit.
PRINTSiPR00738. GLHYDRLASE20.
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF55545. SSF55545. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q29548-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEVLPGLLRL LAALVVAERW ARDTSGAESL GLWPLPFAVD ISPRSLHLSP
60 70 80 90 100
NNFFFGHSPT SKAGSSCEIL QEAFRRYYDF IFGFYKWHQG SYQLCFGTEL
110 120 130 140 150
QQLQVHVESE CDTFPSISSN ESYVLHVKGP EALLRANTVW GALRGLETFS
160 170 180 190 200
QLIYQDSYGT FTVNESEIID FPRFPHRGIL IDTGRHFLSV KTIFKTLDAM
210 220 230 240 250
AFNKFNVLHW HIVDDQSFPY QSINFGVLSS KGSYSLSHVY TPNDVRMVIE
260 270 280 290 300
YARIRGIRVM PEFDTPGHSR SWGKGQKDLL TPCYRKQVLS GTFGPINPIL
310 320 330 340 350
NTTYNFLSKF FKEISTVFPD EFIHIGGDEV DFDCWASNSE ILQFMQEKGF
360 370 380 390 400
SQISLNSNLC TVFKISNMIS AMKKRPIVWQ EAFDGRDKFM PGTVVQVWKI
410 420 430 440 450
EDYKWEQSLI TKAGFPVILS APWYLDLISY GQDWKNYYEV EPQDFPGSDK
460 470 480 490 500
ERKRVLGGEA CLWGEYVDAT NLTPRLWPRA SAVGERLWSH KDVRDIHDAY
510 520 530
SRLTIHRCRM VRRGIAAEPL FTGYCNHEHR M
Length:531
Mass (Da):61,050
Last modified:May 10, 2005 - v2
Checksum:iF55D62D6937E51C5
GO

Sequence cautioni

The sequence CAA63123.1 differs from that shown. Reason: Frameshift at positions 3 and 16. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X92379 mRNA. Translation: CAA63123.1. Frameshift.
RefSeqiNP_999086.1. NM_213921.1.
UniGeneiSsc.3196.

Genome annotation databases

GeneIDi396958.
KEGGissc:396958.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X92379 mRNA. Translation: CAA63123.1 . Frameshift.
RefSeqi NP_999086.1. NM_213921.1.
UniGenei Ssc.3196.

3D structure databases

ProteinModelPortali Q29548.
SMRi Q29548. Positions 31-527.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9823.ENSSSCP00000014965.

Protein family/group databases

CAZyi GH20. Glycoside Hydrolase Family 20.

Proteomic databases

PaxDbi Q29548.
PRIDEi Q29548.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 396958.
KEGGi ssc:396958.

Organism-specific databases

CTDi 3074.

Phylogenomic databases

eggNOGi COG3525.
HOGENOMi HOG000157972.
HOVERGENi HBG005961.
InParanoidi Q29548.
KOi K12373.

Family and domain databases

Gene3Di 3.20.20.80. 1 hit.
3.30.379.10. 1 hit.
InterProi IPR025705. Beta_hexosaminidase_sua/sub.
IPR029018. Chitobiase/Hex_dom_2-like.
IPR015883. Glyco_hydro_20_cat-core.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR029019. HEX_eukaryotic_N.
[Graphical view ]
Pfami PF00728. Glyco_hydro_20. 1 hit.
PF14845. Glycohydro_20b2. 1 hit.
[Graphical view ]
PIRSFi PIRSF001093. B-hxosamndse_ab_euk_. 1 hit.
PRINTSi PR00738. GLHYDRLASE20.
SUPFAMi SSF51445. SSF51445. 1 hit.
SSF55545. SSF55545. 1 hit.
ProtoNeti Search...

Publicationsi

  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] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE.
    Tissue: Epididymis.

Entry informationi

Entry nameiHEXB_PIG
AccessioniPrimary (citable) accession number: Q29548
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 10, 2005
Last modified: October 29, 2014
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3