Q7TN73 · CASD1_MOUSE
- ProteinN-acetylneuraminate (7)9-O-acetyltransferase
- GeneCasd1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids797 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
Function
function
Key enzyme in the biosynthesis of O-acetylated (O-Ac) sialoglycans such as gangliosides O-AcGD3 and O-AcGD2, which affects various processes such as cell-cell interactions, host-pathogen recognition. Catalyzes the transfer of an acetyl group from a donor, the acetyl-coenzyme-A molecule (acetyl-CoA), to the C7/8/9 OH-position of a glycosidically bound sialic acid residue. The primary site of O-acetyl group transfer on sialic acid is thought to be C7, from which the O-acetyl group could subsequently migrate under acidic pH conditions to the C8 and to the C9 positions, which are more stable positions. Can also transfer the acetyl group from acetyl-CoA to free sialate (N-acetylneuraminate, Neu5Ac) in vitro, but has preferred substrate specificity for CMP-activated sialate (CMP-Neu5Ac), which can initially be acetylated at C7 and non-enzymatically migrate to C9, resulting in the formation of 9-O-acetylated CMP-Neu5Ac (CMP-Neu5,9Ac2). CMP-Neu5,9Ac2 may be used by sialyltransferases as a sialate donor for glycoconjugate acceptors. O-acetylation at position C9 of ganglioside GD3 can counteract the pro-apoptotic effects of the ganglioside GD3 in tumor cells.
Miscellaneous
The Casd1 locus is imprinted. Maternal inherited gene is expressed, while the paternal inherited gene is silenced.
Catalytic activity
- acetyl-CoA + N-acetylneuraminate = CoA + N-acetyl-7-O-acetylneuraminateThis reaction proceeds in the forward direction.
- a ganglioside GD3 (d18:1(4E)) + acetyl-CoA = a ganglioside Ac-O-7-GD3(d18:1(4E)) + CoAThis reaction proceeds in the forward direction.
- acetyl-CoA + CMP-N-acetyl-beta-neuraminate = CMP-N-beta-acetyl-7-O-acetylneuraminate + CoAThis reaction proceeds in the forward direction.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 94 | Acyl-ester intermediate | ||||
Sequence: S | ||||||
Active site | 270 | |||||
Sequence: D | ||||||
Active site | 273 | |||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | Golgi membrane | |
Molecular Function | N-acetylneuraminate 7-O(or 9-O)-acetyltransferase activity | |
Biological Process | carbohydrate metabolic process |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameN-acetylneuraminate (7)9-O-acetyltransferase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ7TN73
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Golgi apparatus membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-18 | Cytoplasmic | ||||
Sequence: MAALAYNLGKREINHYFS | ||||||
Transmembrane | 19-39 | Helical | ||||
Sequence: VRSAKVLALVAVLLLAACHLA | ||||||
Topological domain | 40-313 | Lumenal | ||||
Sequence: SRRYRGNDSCEYLLSSGRFLGEKVWQPHSCMMHKYKISEAKTCLVDKHIAFIGDSRIRQLFYSFVKIINPQFKEEGNKHENIPFEDKAASVKVDFLWHPEVNGSMKQCIKVWTEDSVLKPHVIVAGAATWSIKIHNGSEEALAQYKMNITSIAPLLEKLAKTSDVYWVLQDPVYEDLLSENRKMITNEKIDAYNEAAVSILNSSTRTSKSNVKMFSVSKLIAQETIMESLDGLHLPESSRETSAMILMNVYCNKVVKPVDGSCCQPRPPLTLIQ | ||||||
Transmembrane | 314-334 | Helical | ||||
Sequence: KLAACFFTLSIIGYFIFYVIH | ||||||
Topological domain | 335-363 | Cytoplasmic | ||||
Sequence: RNAHRKNKPCTDLESGEEKKNIINTPVSS | ||||||
Transmembrane | 364-384 | Helical | ||||
Sequence: LEILLQSFCKLGLIMAYFYMC | ||||||
Topological domain | 385-395 | Lumenal | ||||
Sequence: DRANLFMKENK | ||||||
Transmembrane | 396-416 | Helical | ||||
Sequence: FYTHSSFFIPIIYILVLGVFY | ||||||
Topological domain | 417-439 | Cytoplasmic | ||||
Sequence: NENTKETKVLNREQTDEWKGWMQ | ||||||
Transmembrane | 440-460 | Helical | ||||
Sequence: LVILIYHISGASTFLPVYMHI | ||||||
Topological domain | 461 | Lumenal | ||||
Sequence: R | ||||||
Transmembrane | 462-482 | Helical | ||||
Sequence: VLVAAYLFQTGYGHFSYFWIK | ||||||
Topological domain | 483-486 | Cytoplasmic | ||||
Sequence: GDFG | ||||||
Transmembrane | 487-507 | Helical | ||||
Sequence: IHRVCQVLFRLNFLVVVLCIV | ||||||
Topological domain | 508-513 | Lumenal | ||||
Sequence: MDRPYQ | ||||||
Transmembrane | 514-534 | Helical | ||||
Sequence: FYYFVPLVTVWFMVIYVTLAL | ||||||
Topological domain | 535-546 | Cytoplasmic | ||||
Sequence: WPQITQKKANGN | ||||||
Transmembrane | 547-567 | Helical | ||||
Sequence: FFWYLGLLLKLGLLLLCIWFL | ||||||
Topological domain | 568-599 | Lumenal | ||||
Sequence: AYSQGAFEKIFSLWPLSKCFELEGSVYEWWFR | ||||||
Transmembrane | 600-620 | Helical | ||||
Sequence: WRLDRYVVFHGVLFAFIYLAL | ||||||
Topological domain | 621-638 | Cytoplasmic | ||||
Sequence: QRRQILSEGKGEPLFSNK | ||||||
Transmembrane | 639-659 | Helical | ||||
Sequence: ISNFLLFVSVVSFLTYSIWAS | ||||||
Topological domain | 660-671 | Lumenal | ||||
Sequence: SCKNKAECNELH | ||||||
Transmembrane | 672-692 | Helical | ||||
Sequence: PSVSVVQIVAFILIRNIPGYA | ||||||
Topological domain | 693-698 | Cytoplasmic | ||||
Sequence: RSIYSS | ||||||
Transmembrane | 699-719 | Helical | ||||
Sequence: FFAWFGKISLELFICQYHIWL | ||||||
Topological domain | 720-725 | Lumenal | ||||
Sequence: AADTRG | ||||||
Transmembrane | 726-746 | Helical | ||||
Sequence: ILVLIPGNPTLNIIVSTFIFV | ||||||
Topological domain | 747-770 | Cytoplasmic | ||||
Sequence: CVAHEISQITTDLAQVVIPKDNPS | ||||||
Transmembrane | 771-791 | Helical | ||||
Sequence: LFRRLACTIAFFGGVLILSSI | ||||||
Topological domain | 792-797 | Lumenal | ||||
Sequence: QDKSRL |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000307231 | 1-797 | N-acetylneuraminate 79-O-acetyltransferase | |||
Sequence: MAALAYNLGKREINHYFSVRSAKVLALVAVLLLAACHLASRRYRGNDSCEYLLSSGRFLGEKVWQPHSCMMHKYKISEAKTCLVDKHIAFIGDSRIRQLFYSFVKIINPQFKEEGNKHENIPFEDKAASVKVDFLWHPEVNGSMKQCIKVWTEDSVLKPHVIVAGAATWSIKIHNGSEEALAQYKMNITSIAPLLEKLAKTSDVYWVLQDPVYEDLLSENRKMITNEKIDAYNEAAVSILNSSTRTSKSNVKMFSVSKLIAQETIMESLDGLHLPESSRETSAMILMNVYCNKVVKPVDGSCCQPRPPLTLIQKLAACFFTLSIIGYFIFYVIHRNAHRKNKPCTDLESGEEKKNIINTPVSSLEILLQSFCKLGLIMAYFYMCDRANLFMKENKFYTHSSFFIPIIYILVLGVFYNENTKETKVLNREQTDEWKGWMQLVILIYHISGASTFLPVYMHIRVLVAAYLFQTGYGHFSYFWIKGDFGIHRVCQVLFRLNFLVVVLCIVMDRPYQFYYFVPLVTVWFMVIYVTLALWPQITQKKANGNFFWYLGLLLKLGLLLLCIWFLAYSQGAFEKIFSLWPLSKCFELEGSVYEWWFRWRLDRYVVFHGVLFAFIYLALQRRQILSEGKGEPLFSNKISNFLLFVSVVSFLTYSIWASSCKNKAECNELHPSVSVVQIVAFILIRNIPGYARSIYSSFFAWFGKISLELFICQYHIWLAADTRGILVLIPGNPTLNIIVSTFIFVCVAHEISQITTDLAQVVIPKDNPSLFRRLACTIAFFGGVLILSSIQDKSRL | ||||||
Glycosylation | 46 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 175 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 187 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
N-glycosylated.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Ubiquitously expressed.
Developmental stage
Expressed in neonatal brain and in day 10 and 13 embryo.
Gene expression databases
Structure
Family & Domains
Sequence similarities
Belongs to the PC-esterase family. CASD1 subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length797
- Mass (Da)91,603
- Last updated2003-10-01 v1
- Checksum9FF23144DDDA8741
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
M0QWG8 | M0QWG8_MOUSE | Casd1 | 220 | ||
A0A0N4SWB0 | A0A0N4SWB0_MOUSE | Casd1 | 71 | ||
A0A0N4SW49 | A0A0N4SW49_MOUSE | Casd1 | 132 | ||
F6TUA2 | F6TUA2_MOUSE | Casd1 | 182 |
Sequence caution
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB091829 EMBL· GenBank· DDBJ | BAC77246.1 EMBL· GenBank· DDBJ | mRNA | ||
BC018542 EMBL· GenBank· DDBJ | AAH18542.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC038009 EMBL· GenBank· DDBJ | AAH38009.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC058953 EMBL· GenBank· DDBJ | AAH58953.1 EMBL· GenBank· DDBJ | mRNA | ||
BC125377 EMBL· GenBank· DDBJ | AAI25378.1 EMBL· GenBank· DDBJ | mRNA | ||
BC125379 EMBL· GenBank· DDBJ | AAI25380.1 EMBL· GenBank· DDBJ | mRNA |