P70665 · SIAE_MOUSE

  • Protein
    Sialate O-acetylesterase
  • Gene
    Siae
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Catalyzes the removal of O-acetyl ester groups from position 9 of the parent sialic acid, N-acetylneuraminic acid.

Catalytic activity

Activity regulation

Inhibited by diisopropyl fluorophosphate and diethyl-P-nitrophenyl phosphate.

GO annotations

AspectTerm
Cellular Componentlysosome
Molecular Functionsialate 4-O-acetylesterase activity
Molecular Functionsialate 9-O-acetylesterase activity
Molecular Functionsialate O-acetylesterase activity
Biological Processcarbohydrate metabolic process
Biological Processregulation of immune system process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

Gene names

    • Name
      Siae
    • Synonyms
      Ysg2

Organism names

  • Taxonomic identifier
  • Strains
    • C57BL/6 X DBA/2
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    P70665
  • Secondary accessions
    • Q3TNZ5
    • Q544V7
    • Q61044
    • Q8C902
    • Q8CBM6

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, chain, glycosylation.

TypeIDPosition(s)Description
Signal1-23
ChainPRO_000002271424-275Sialate O-acetylesterase small subunit
Glycosylation107N-linked (GlcNAc...) asparagine
Glycosylation138N-linked (GlcNAc...) asparagine
Glycosylation188N-linked (GlcNAc...) asparagine
ChainPRO_0000022715276-541Sialate O-acetylesterase large subunit
Glycosylation293N-linked (GlcNAc...) asparagine
Glycosylation356N-linked (GlcNAc...) asparagine
Glycosylation427N-linked (GlcNAc...) asparagine
Glycosylation448N-linked (GlcNAc...) asparagine
Glycosylation462N-linked (GlcNAc...) asparagine

Post-translational modification

The two subunits are derived from a single precursor by proteolytic cleavage.
The lysosomal isoform is glycosylated.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Isoform 1 is widely expressed. Isoform 2 shows a more restricted distribution with highest expression in brain and ovary and lower levels in liver and thymus.

Gene expression databases

Interaction

Subunit

Disulfide-linked heterodimer of a small subunit and a large subunit.

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (3)
  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.

This entry describes 3 isoforms produced by Alternative splicing.

P70665-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Name
    1
  • Synonyms
    Lse
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Length
    541
  • Mass (Da)
    60,775
  • Last updated
    2006-05-30 v3
  • Checksum
    944936C45C4A2E6B
MVSPGPVFGIVLLIIARVSRSAGIGFRFASYIDNYMVLQKEPSGAVIWGFGTPGATVTVTLCQGQETIMKKVTSVKEPSNTWMVVLDPMKPGGPFEVMAQQTLGTMNFTLRVHDVLFGDVWLCSGQSNMQMTVSQIFNASKELSDTAAYQSVRIFSVSLIQSEEELDDLTEVDLSWSKPTAGNLGHGNFTYMSAVCWLFGRYLYDTLQYPIGLVSSSWGGTYIEVWSSRRTLKACGVPNTRDERVGQPEIKPMRNECNSEESSCPFRVVPSVRVTGPTRHSVLWNAMIHPLQNMTLKGVVWYQGESNADYNRDLYTCMFPELIEDWRQTFHYGSQGQTDRFFPFGFVQLSSYMLKNSSDYGFPEIRWHQTADFGHVPNPKMPNTFMAVAIDLCDRDSPFGSIHPRDKQTVAYRLHLGARAVAYGEKNLTFQGPLPKKIELLASNGLLNLTYDQEIQVQMQDNKTFEISCCSDRHCKWLPAPVNTFSTQTLILDLNACLGTVVAVRYAWTTWPCEYKQCAVYHTSSMLPAPPFIAQISHRGI

P70665-2

  • Name
    2
  • Synonyms
    Cse
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

P70665-3

  • Name
    3
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 349-390: LSSYMLKNSSDYGFPEIRWHQTADFGHVPNPKMPNTFMAVAI → VCIQRIHIQCLEFMGLCGECGLCTCLYWDLQPNICPNSMSWR
    • 391-541: Missing

Computationally mapped potential isoform sequences

There are 4 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A1N9M4K1A0A1N9M4K1_MOUSESiae469
A0A1L1SU77A0A1L1SU77_MOUSESiae506
A0A1L1SQX0A0A1L1SQX0_MOUSESiae111
A0A1L1SQF7A0A1L1SQF7_MOUSESiae134

Sequence caution

The sequence BAC29164.1 differs from that shown. Reason: Erroneous initiation

Features

Showing features for alternative sequence, sequence conflict.

TypeIDPosition(s)Description
Alternative sequenceVSP_0040771-97in isoform 2
Sequence conflict114in Ref. 4; BAE37942
Sequence conflict160in Ref. 2; AAB07813 and 5; AAH07136
Sequence conflict349in Ref. 4; BAC26026
Alternative sequenceVSP_018996349-390in isoform 3
Sequence conflict373in Ref. 4; BAC29164
Sequence conflict379in Ref. 5; AAH07136
Alternative sequenceVSP_018997391-541in isoform 3

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U61183
EMBL· GenBank· DDBJ
AAC52880.1
EMBL· GenBank· DDBJ
mRNA
X98625
EMBL· GenBank· DDBJ
CAA67214.1
EMBL· GenBank· DDBJ
mRNA
U40408
EMBL· GenBank· DDBJ
AAB07813.1
EMBL· GenBank· DDBJ
mRNA
AF156856
EMBL· GenBank· DDBJ
AAD55976.1
EMBL· GenBank· DDBJ
mRNA
AK028598
EMBL· GenBank· DDBJ
BAC26026.1
EMBL· GenBank· DDBJ
mRNA
AK028656
EMBL· GenBank· DDBJ
BAC26049.1
EMBL· GenBank· DDBJ
mRNA
AK033980
EMBL· GenBank· DDBJ
BAC28536.1
EMBL· GenBank· DDBJ
mRNA
AK035715
EMBL· GenBank· DDBJ
BAC29164.1
EMBL· GenBank· DDBJ
mRNA Different initiation
AK043392
EMBL· GenBank· DDBJ
BAC31534.1
EMBL· GenBank· DDBJ
mRNA
AK164852
EMBL· GenBank· DDBJ
BAE37942.1
EMBL· GenBank· DDBJ
mRNA
AK167103
EMBL· GenBank· DDBJ
BAE39252.1
EMBL· GenBank· DDBJ
mRNA
BC007136
EMBL· GenBank· DDBJ
AAH07136.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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