CASD1_MOUSE
ID CASD1_MOUSE Reviewed; 797 AA.
AC Q7TN73; Q1RN01; Q6PD39; Q8VEF5;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=N-acetylneuraminate 9-O-acetyltransferase {ECO:0000250|UniProtKB:Q96PB1};
DE EC=2.3.1.45 {ECO:0000250|UniProtKB:Q96PB1};
DE AltName: Full=CAS1 domain-containing protein 1;
DE AltName: Full=Sialate O-acetyltransferase {ECO:0000250|UniProtKB:Q96PB1};
DE Short=SOAT {ECO:0000250|UniProtKB:Q96PB1};
GN Name=Casd1 {ECO:0000312|MGI:MGI:2384865}; Synonyms=Cas1, Cast1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J;
RX PubMed=12840045; DOI=10.1101/gr.906803;
RA Ono R., Shiura H., Aburatani H., Kohda T., Kaneko-Ishino T., Ishino F.;
RT "Identification of a large novel imprinted gene cluster on mouse proximal
RT chromosome 6.";
RL Genome Res. 13:1696-1705(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=129, and C57BL/6J; TISSUE=Brain, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IMPRINTING.
RX PubMed=19026546; DOI=10.1016/j.cub.2008.09.044;
RA Babak T., Deveale B., Armour C., Raymond C., Cleary M.A., van der Kooy D.,
RA Johnson J.M., Lim L.P.;
RT "Global survey of genomic imprinting by transcriptome sequencing.";
RL Curr. Biol. 18:1735-1741(2008).
CC -!- FUNCTION: O-acetyltransferase that catalyzes 9-O-acetylation of sialic
CC acids. Sialic acids are sugars at the reducing end of glycoproteins and
CC glycolipids, and are involved in various processes such as cell-cell
CC interactions, host-pathogen recognition.
CC {ECO:0000250|UniProtKB:Q96PB1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-acetylneuraminate = CoA + N-acetyl-9-O-
CC acetylneuraminate; Xref=Rhea:RHEA:26043, ChEBI:CHEBI:28999,
CC ChEBI:CHEBI:35418, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.45;
CC Evidence={ECO:0000250|UniProtKB:Q96PB1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-acetylneuraminate = CoA + N-acetyl-7-O-
CC acetylneuraminate; Xref=Rhea:RHEA:20808, ChEBI:CHEBI:28944,
CC ChEBI:CHEBI:35418, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.45;
CC Evidence={ECO:0000250|UniProtKB:Q96PB1};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q96PB1}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q96PB1}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:12840045}.
CC -!- DEVELOPMENTAL STAGE: Expressed in neonatal brain and in day 10 and 13
CC embryo. {ECO:0000269|PubMed:12840045}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q96PB1}.
CC -!- MISCELLANEOUS: The Casd1 locus is imprinted. Maternal inherited gene is
CC expressed, while the paternal inherited gene is silenced.
CC {ECO:0000269|PubMed:19026546}.
CC -!- SIMILARITY: Belongs to the PC-esterase family. CASD1 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH18542.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH38009.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB091829; BAC77246.1; -; mRNA.
DR EMBL; BC018542; AAH18542.1; ALT_INIT; mRNA.
DR EMBL; BC038009; AAH38009.1; ALT_INIT; mRNA.
DR EMBL; BC058953; AAH58953.1; -; mRNA.
DR EMBL; BC125377; AAI25378.1; -; mRNA.
DR EMBL; BC125379; AAI25380.1; -; mRNA.
DR CCDS; CCDS19896.1; -.
DR RefSeq; NP_663373.2; NM_145398.2.
DR AlphaFoldDB; Q7TN73; -.
DR BioGRID; 229474; 2.
DR STRING; 10090.ENSMUSP00000015333; -.
DR GlyGen; Q7TN73; 3 sites.
DR iPTMnet; Q7TN73; -.
DR PhosphoSitePlus; Q7TN73; -.
DR EPD; Q7TN73; -.
DR MaxQB; Q7TN73; -.
DR PaxDb; Q7TN73; -.
DR PRIDE; Q7TN73; -.
DR ProteomicsDB; 265437; -.
DR Antibodypedia; 45361; 113 antibodies from 15 providers.
DR DNASU; 213819; -.
DR Ensembl; ENSMUST00000015333; ENSMUSP00000015333; ENSMUSG00000015189.
DR GeneID; 213819; -.
DR KEGG; mmu:213819; -.
DR UCSC; uc009avo.1; mouse.
DR CTD; 64921; -.
DR MGI; MGI:2384865; Casd1.
DR VEuPathDB; HostDB:ENSMUSG00000015189; -.
DR eggNOG; KOG1699; Eukaryota.
DR GeneTree; ENSGT00390000004037; -.
DR HOGENOM; CLU_008003_1_0_1; -.
DR InParanoid; Q7TN73; -.
DR OMA; MIYAACF; -.
DR OrthoDB; 120492at2759; -.
DR PhylomeDB; Q7TN73; -.
DR TreeFam; TF324898; -.
DR BioGRID-ORCS; 213819; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Casd1; mouse.
DR PRO; PR:Q7TN73; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q7TN73; protein.
DR Bgee; ENSMUSG00000015189; Expressed in CA1 field of hippocampus and 242 other tissues.
DR ExpressionAtlas; Q7TN73; baseline and differential.
DR Genevisible; Q7TN73; MM.
DR GO; GO:0030173; C:integral component of Golgi membrane; ISS:UniProtKB.
DR GO; GO:0047186; F:N-acetylneuraminate 7-O(or 9-O)-acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; ISS:UniProtKB.
DR InterPro; IPR012419; Cas1_AcylTrans_dom.
DR InterPro; IPR036915; Cyclin-like_sf.
DR Pfam; PF07779; Cas1_AcylT; 1.
DR SUPFAM; SSF47954; SSF47954; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Glycoprotein; Golgi apparatus; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..797
FT /note="N-acetylneuraminate 9-O-acetyltransferase"
FT /id="PRO_0000307231"
FT TOPO_DOM 1..18
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 40..313
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q96PB1"
FT TRANSMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 335..363
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 364..384
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 385..395
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 396..416
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 417..439
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 440..460
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 461
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 462..482
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 483..486
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 487..507
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 508..513
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 514..534
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 535..546
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 547..567
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 568..599
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 600..620
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 621..638
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 639..659
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 660..671
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 672..692
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 693..698
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 699..719
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 720..725
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 726..746
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 747..770
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 771..791
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 792..797
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT ACT_SITE 94
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q96PB1"
FT ACT_SITE 270
FT /evidence="ECO:0000250|UniProtKB:Q96PB1"
FT ACT_SITE 273
FT /evidence="ECO:0000250|UniProtKB:Q96PB1"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 797 AA; 91603 MW; 9FF23144DDDA8741 CRC64;
MAALAYNLGK REINHYFSVR SAKVLALVAV LLLAACHLAS RRYRGNDSCE YLLSSGRFLG
EKVWQPHSCM MHKYKISEAK TCLVDKHIAF IGDSRIRQLF YSFVKIINPQ FKEEGNKHEN
IPFEDKAASV KVDFLWHPEV NGSMKQCIKV WTEDSVLKPH VIVAGAATWS IKIHNGSEEA
LAQYKMNITS IAPLLEKLAK TSDVYWVLQD PVYEDLLSEN RKMITNEKID AYNEAAVSIL
NSSTRTSKSN VKMFSVSKLI AQETIMESLD GLHLPESSRE TSAMILMNVY CNKVVKPVDG
SCCQPRPPLT LIQKLAACFF TLSIIGYFIF YVIHRNAHRK NKPCTDLESG EEKKNIINTP
VSSLEILLQS FCKLGLIMAY FYMCDRANLF MKENKFYTHS SFFIPIIYIL VLGVFYNENT
KETKVLNREQ TDEWKGWMQL VILIYHISGA STFLPVYMHI RVLVAAYLFQ TGYGHFSYFW
IKGDFGIHRV CQVLFRLNFL VVVLCIVMDR PYQFYYFVPL VTVWFMVIYV TLALWPQITQ
KKANGNFFWY LGLLLKLGLL LLCIWFLAYS QGAFEKIFSL WPLSKCFELE GSVYEWWFRW
RLDRYVVFHG VLFAFIYLAL QRRQILSEGK GEPLFSNKIS NFLLFVSVVS FLTYSIWASS
CKNKAECNEL HPSVSVVQIV AFILIRNIPG YARSIYSSFF AWFGKISLEL FICQYHIWLA
ADTRGILVLI PGNPTLNIIV STFIFVCVAH EISQITTDLA QVVIPKDNPS LFRRLACTIA
FFGGVLILSS IQDKSRL
