CASD1_DANRE
ID CASD1_DANRE Reviewed; 781 AA.
AC Q1LW89; Q1JQ49; Q4V8Z8;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 84.
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 {ECO:0000250|UniProtKB:Q96PB1};
DE AltName: Full=Sialate O-acetyltransferase {ECO:0000250|UniProtKB:Q96PB1};
DE Short=SOAT {ECO:0000250|UniProtKB:Q96PB1};
GN Name=casd1 {ECO:0000250|UniProtKB:Q96PB1};
GN ORFNames=si:dkey-104m9.2 {ECO:0000303|PubMed:23594743},
GN zgc:136291 {ECO:0000303|Ref.2};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=SJD; TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the PC-esterase family. CASD1 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH97133.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAI16485.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence at C-terminus.; Evidence={ECO:0000305};
CC Sequence=CAK05066.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; BX640469; CAK05066.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC097133; AAH97133.1; ALT_SEQ; mRNA.
DR EMBL; BC116484; AAI16485.1; ALT_SEQ; mRNA.
DR AlphaFoldDB; Q1LW89; -.
DR SMR; Q1LW89; -.
DR STRING; 7955.ENSDARP00000114886; -.
DR ZFIN; ZDB-GENE-060503-329; casd1.
DR eggNOG; KOG1699; Eukaryota.
DR HOGENOM; CLU_008003_1_0_1; -.
DR InParanoid; Q1LW89; -.
DR PhylomeDB; Q1LW89; -.
DR TreeFam; TF324898; -.
DR PRO; PR:Q1LW89; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
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 Gene3D; 3.40.50.1110; -; 1.
DR InterPro; IPR012419; Cas1_AcylTrans_dom.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR Pfam; PF07779; Cas1_AcylT; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Glycoprotein; Golgi apparatus; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..781
FT /note="N-acetylneuraminate 9-O-acetyltransferase"
FT /id="PRO_0000307232"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..308
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q96PB1"
FT TRANSMEM 309..329
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 330..354
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 355..375
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 376..386
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 387..407
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 408..430
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 431..451
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 452
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 453..473
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 474..477
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 478..498
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 499..504
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 505..525
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 526..537
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 538..558
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 559..595
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 596..616
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 617..629
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 630..650
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 651..660
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 661..681
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 682..687
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 688..708
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 709..714
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 715..735
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 736..756
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 757..777
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 778..781
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 330..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..346
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 94
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q96PB1"
FT ACT_SITE 264
FT /evidence="ECO:0000250|UniProtKB:Q96PB1"
FT ACT_SITE 267
FT /evidence="ECO:0000250|UniProtKB:Q96PB1"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 654
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 781 AA; 88736 MW; DAC8FF1350F756E8 CRC64;
MAVLAYNLGK REINQYFSIK NAKLLAAAAV VLLTVFHAAS RHYGSSDTCD WLLSSGRFLG
DNVWQPYGCM LHKYKSTEAK FCLREKRIAF VGDSRIRQLF YSFIKMMNPE VKEVGNKHEN
IPFVDGDSTV NFLWYAEVNN SLKEQLMLWT EGSASKPHVI IIGAATWSIK LHNGKSEALF
QYKANLTAIA DTLEKLAEHS EVYWVLQDPV YEDVLSESRK MITNEQINLY NEAAVSTLNT
SKKKVKFLEA SRQAAMETIS QSVDGLHLPE STRDVGAMVL MNSMCNKILK PIDGSCCQSA
PPLSVLQKLA AAVLLVSVVC FVLLGFSSHR KSRPAPDVES GEEKKHPAAV GQLNPKGPLL
AIGKMSLIML YFYLCDRADI FMKEQKFYTH SAFFIPLIYI FVLGVFYSEN SKETKLLNRE
QTDEWKGWMQ LVILIYHISG ASAFIPVYMH VRVLVAAYLF QTGYGHFSFF WLKGDFGLYR
VCQVLFRLNF LVVVLCLVMD RPYQFYYFVP LVTFWFAVIY ATMALWPQIL QKQANGSAFW
NLALLLKLLG LLLFIGFFAY SQELFEGIFS VWPLSKLFEL QGSIHEWWFR WKLDRFAVVN
GMLFAFIYLL LQKYQLLSEG KGEPLFSNKI SNCLLFVSVV SFMTYSIWAS GCKNKSECNE
MHPYISVILA FILIRNIPGY ARSLYSSFFA WFGKISLELF ICQYHIWLAA DTKGILVLIP
GNPTLNIIVS TFIFVCVAHE ISQITNDLAQ VAIPKESGPL LKRLLGAGVF LVLVLTLSQK
D
