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Q29548

- HEXB_PIG

UniProt

Q29548 - HEXB_PIG

Protein

Beta-hexosaminidase subunit beta

Gene

HEXB

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 2 (10 May 2005)
      Previous versions | rss
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    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

    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-SubCell

    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.
    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

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    MEVLPGLLRL LAALVVAERW ARDTSGAESL GLWPLPFAVD ISPRSLHLSP    50
    NNFFFGHSPT SKAGSSCEIL QEAFRRYYDF IFGFYKWHQG SYQLCFGTEL 100
    QQLQVHVESE CDTFPSISSN ESYVLHVKGP EALLRANTVW GALRGLETFS 150
    QLIYQDSYGT FTVNESEIID FPRFPHRGIL IDTGRHFLSV KTIFKTLDAM 200
    AFNKFNVLHW HIVDDQSFPY QSINFGVLSS KGSYSLSHVY TPNDVRMVIE 250
    YARIRGIRVM PEFDTPGHSR SWGKGQKDLL TPCYRKQVLS GTFGPINPIL 300
    NTTYNFLSKF FKEISTVFPD EFIHIGGDEV DFDCWASNSE ILQFMQEKGF 350
    SQISLNSNLC TVFKISNMIS AMKKRPIVWQ EAFDGRDKFM PGTVVQVWKI 400
    EDYKWEQSLI TKAGFPVILS APWYLDLISY GQDWKNYYEV EPQDFPGSDK 450
    ERKRVLGGEA CLWGEYVDAT NLTPRLWPRA SAVGERLWSH KDVRDIHDAY 500
    SRLTIHRCRM VRRGIAAEPL FTGYCNHEHR M 531
    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.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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.
    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 1, 2014
    This is version 91 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