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P29416

- HEXA_MOUSE

UniProt

P29416 - HEXA_MOUSE

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Protein

Beta-hexosaminidase subunit alpha

Gene

Hexa

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript 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.

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 sitei323 – 3231Proton donorBy similarity

GO - Molecular functioni

  1. beta-N-acetylhexosaminidase activity Source: MGI

GO - Biological processi

  1. adult walking behavior Source: MGI
  2. carbohydrate metabolic process Source: InterPro
  3. cell morphogenesis involved in neuron differentiation Source: MGI
  4. ganglioside catabolic process Source: MGI
  5. glycosaminoglycan metabolic process Source: MGI
  6. lipid storage Source: MGI
  7. locomotory behavior Source: MGI
  8. lysosome organization Source: MGI
  9. myelination Source: MGI
  10. neuromuscular process controlling balance Source: MGI
  11. neuromuscular process controlling posture Source: MGI
  12. sensory perception of sound Source: MGI
  13. sexual reproduction Source: MGI
  14. skeletal system development Source: MGI
  15. SMAD protein signal transduction Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

ReactomeiREACT_196554. Hyaluronan uptake and degradation.
REACT_198960. Keratan sulfate degradation.
REACT_198981. CS/DS degradation.
REACT_199008. Glycosphingolipid metabolism.

Protein family/group databases

CAZyiGH20. Glycoside Hydrolase Family 20.

Names & Taxonomyi

Protein namesi
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 namesi
Name:Hexa
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 9

Organism-specific databases

MGIiMGI:96073. Hexa.

Subcellular locationi

GO - Cellular componenti

  1. lysosome Source: MGI
  2. membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222By similarityAdd
BLAST
Propeptidei23 – 8866By similarityPRO_0000011995Add
BLAST
Chaini89 – 528440Beta-hexosaminidase subunit alphaPRO_0000011996Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi58 ↔ 104By similarity
Glycosylationi115 – 1151N-linked (GlcNAc...)Sequence Analysis
Glycosylationi157 – 1571N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi277 ↔ 328By similarity
Glycosylationi295 – 2951N-linked (GlcNAc...)Sequence Analysis
Glycosylationi487 – 4871N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi504 ↔ 521By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

MaxQBiP29416.
PaxDbiP29416.
PRIDEiP29416.

PTM databases

PhosphoSiteiP29416.

Expressioni

Tissue specificityi

Ubiquitous. Most abundant in testis, adrenal, epididymis and heart. Low levels seen in the liver.1 Publication

Gene expression databases

BgeeiP29416.
CleanExiMM_HEXA.
ExpressionAtlasiP29416. baseline and differential.
GenevestigatoriP29416.

Interactioni

Subunit structurei

There are 3 forms of beta-hexosaminidase: hexosaminidase A is a trimer composed of one alpha chain, one beta-A chain and one beta-B chain; hexosaminidase B is a tetramer of two beta-A and two beta-B chains; hexosaminidase S is a homodimer of two alpha chains. The two beta chains are derived from the cleavage of a precursor chain (By similarity).By similarity

Protein-protein interaction databases

BioGridi200280. 1 interaction.
IntActiP29416. 1 interaction.
STRINGi10090.ENSMUSP00000026262.

Structurei

3D structure databases

ProteinModelPortaliP29416.
SMRiP29416. Positions 23-527.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni422 – 4232Critical for hydrolyzis GM2 gangliosidesBy similarity

Sequence similaritiesi

Belongs to the glycosyl hydrolase 20 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3525.
GeneTreeiENSGT00390000008107.
HOGENOMiHOG000157972.
HOVERGENiHBG005961.
InParanoidiP29416.
KOiK12373.
OMAiWHLVDDS.
OrthoDBiEOG7KDFB6.
TreeFamiTF313036.

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.

P29416-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAGCRLWVSL LLAAALACLA TALWPWPQYI QTYHRRYTLY PNNFQFRYHV
60 70 80 90 100
SSAAQAGCVV LDEAFRRYRN LLFGSGSWPR PSFSNKQQTL GKNILVVSVV
110 120 130 140 150
TAECNEFPNL ESVENYTLTI NDDQCLLASE TVWGALRGLE TFSQLVWKSA
160 170 180 190 200
EGTFFINKTK IKDFPRFPHR GVLLDTSRHY LPLSSILDTL DVMAYNKFNV
210 220 230 240 250
FHWHLVDDSS FPYESFTFPE LTRKGSFNPV THIYTAQDVK EVIEYARLRG
260 270 280 290 300
IRVLAEFDTP GHTLSWGPGA PGLLTPCYSG SHLSGTFGPV NPSLNSTYDF
310 320 330 340 350
MSTLFLEISS VFPDFYLHLG GDEVDFTCWK SNPNIQAFMK KKGFTDFKQL
360 370 380 390 400
ESFYIQTLLD IVSDYDKGYV VWQEVFDNKV KVRPDTIIQV WREEMPVEYM
410 420 430 440 450
LEMQDITRAG FRALLSAPWY LNRVKYGPDW KDMYKVEPLA FHGTPEQKAL
460 470 480 490 500
VIGGEACMWG EYVDSTNLVP RLWPRAGAVA ERLWSSNLTT NIDFAFKRLS
510 520
HFRCELVRRG IQAQPISVGY CEQEFEQT
Length:528
Mass (Da):60,613
Last modified:July 27, 2011 - v2
Checksum:i95DEA72D767094EF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti56 – 561A → G in CAA45615. (PubMed:1379046)Curated
Sequence conflicti56 – 561A → G in AAC53246. (PubMed:7833835)Curated
Sequence conflicti237 – 2371Q → E in X79061. (PubMed:7896264)Curated
Sequence conflicti237 – 2371Q → E in X79062. (PubMed:7896264)Curated
Sequence conflicti455 – 4551E → Q in X79061. (PubMed:7896264)Curated
Sequence conflicti455 – 4551E → Q in X79062. (PubMed:7896264)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64331 mRNA. Translation: CAA45615.1.
U05837
, U05824, U05825, U05826, U05827, U05828, U05829, U05830, U05831, U05832, U05833, U05834, U05835, U05836 Genomic DNA. Translation: AAC53246.1.
U07721
, U07709, U07710, U07711, U07712, U07713, U07714, U07715, U07716, U07717, U07718, U07719, U07720 Unassigned DNA. Translation: AAA18777.1.
U07631 mRNA. Translation: AAA18775.1.
X79061 Genomic DNA. No translation available.
X79062 Genomic DNA. No translation available.
AK075895 mRNA. Translation: BAC36036.1.
AK075911 mRNA. Translation: BAC36049.1.
AK144168 mRNA. Translation: BAE25744.1.
AK159814 mRNA. Translation: BAE35394.1.
CH466522 Genomic DNA. Translation: EDL25971.1.
BC010755 mRNA. Translation: AAH10755.1.
CCDSiCCDS23250.1.
PIRiI48253.
RefSeqiNP_034551.2. NM_010421.4.
UniGeneiMm.2284.

Genome annotation databases

EnsembliENSMUST00000026262; ENSMUSP00000026262; ENSMUSG00000025232.
GeneIDi15211.
KEGGimmu:15211.
UCSCiuc009pxw.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64331 mRNA. Translation: CAA45615.1 .
U05837
, U05824 , U05825 , U05826 , U05827 , U05828 , U05829 , U05830 , U05831 , U05832 , U05833 , U05834 , U05835 , U05836 Genomic DNA. Translation: AAC53246.1 .
U07721
, U07709 , U07710 , U07711 , U07712 , U07713 , U07714 , U07715 , U07716 , U07717 , U07718 , U07719 , U07720 Unassigned DNA. Translation: AAA18777.1 .
U07631 mRNA. Translation: AAA18775.1 .
X79061 Genomic DNA. No translation available.
X79062 Genomic DNA. No translation available.
AK075895 mRNA. Translation: BAC36036.1 .
AK075911 mRNA. Translation: BAC36049.1 .
AK144168 mRNA. Translation: BAE25744.1 .
AK159814 mRNA. Translation: BAE35394.1 .
CH466522 Genomic DNA. Translation: EDL25971.1 .
BC010755 mRNA. Translation: AAH10755.1 .
CCDSi CCDS23250.1.
PIRi I48253.
RefSeqi NP_034551.2. NM_010421.4.
UniGenei Mm.2284.

3D structure databases

ProteinModelPortali P29416.
SMRi P29416. Positions 23-527.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 200280. 1 interaction.
IntActi P29416. 1 interaction.
STRINGi 10090.ENSMUSP00000026262.

Protein family/group databases

CAZyi GH20. Glycoside Hydrolase Family 20.

PTM databases

PhosphoSitei P29416.

Proteomic databases

MaxQBi P29416.
PaxDbi P29416.
PRIDEi P29416.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000026262 ; ENSMUSP00000026262 ; ENSMUSG00000025232 .
GeneIDi 15211.
KEGGi mmu:15211.
UCSCi uc009pxw.1. mouse.

Organism-specific databases

CTDi 3073.
MGIi MGI:96073. Hexa.

Phylogenomic databases

eggNOGi COG3525.
GeneTreei ENSGT00390000008107.
HOGENOMi HOG000157972.
HOVERGENi HBG005961.
InParanoidi P29416.
KOi K12373.
OMAi WHLVDDS.
OrthoDBi EOG7KDFB6.
TreeFami TF313036.

Enzyme and pathway databases

Reactomei REACT_196554. Hyaluronan uptake and degradation.
REACT_198960. Keratan sulfate degradation.
REACT_198981. CS/DS degradation.
REACT_199008. Glycosphingolipid metabolism.

Miscellaneous databases

NextBioi 287777.
PROi P29416.
SOURCEi Search...

Gene expression databases

Bgeei P29416.
CleanExi MM_HEXA.
ExpressionAtlasi P29416. baseline and differential.
Genevestigatori P29416.

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

« Hide 'large scale' publications
  1. "Cloning and sequence analysis of a cDNA encoding the alpha-subunit of mouse beta-N-acetylhexosaminidase and comparison with the human enzyme."
    Beccari T., Hoade J., Orlacchio A., Stirling J.L.
    Biochem. J. 285:593-596(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Testis.
  2. "Organization of the gene for the alpha-subunit of mouse beta-N-acetylhexosaminidase (HEXa)."
    Bianconi S., Beccari T., Stirling J.L., Sheardown S., Orlacchio A.
    Biochem. Mol. Biol. Int. 34:579-586(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Structure and expression of the mouse beta-hexosaminidase genes, Hexa and Hexb."
    Yamanaka S., Johnson O.N., Norflus F., Boles D.J., Proia R.L.
    Genomics 21:588-596(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: C57BL/6 X CBA.
    Tissue: Liver.
  4. "Structural organization, sequence, and expression of the mouse HEXA gene encoding the alpha subunit of hexosaminidase A."
    Wakamatsu N., Benoit G., Lamhonwah A.-M., Zhang Z.-X., Trasler J.M., Triggs-Raine B.L., Gravel R.A.
    Genomics 24:110-119(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
    Strain: 129/Sv.
    Tissue: Liver.
  5. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: BALB/c and C57BL/6J.
    Tissue: Tongue.
  6. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Colon.

Entry informationi

Entry nameiHEXA_MOUSE
AccessioniPrimary (citable) accession number: P29416
Secondary accession number(s): Q64246, Q91XG3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: July 27, 2011
Last modified: October 29, 2014
This is version 117 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, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3