SIAE_MOUSE
ID SIAE_MOUSE Reviewed; 541 AA.
AC P70665; Q3TNZ5; Q544V7; Q61044; Q8C902; Q8CBM6; Q8CC41; Q8CEB7; Q922L0;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 3.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Sialate O-acetylesterase;
DE EC=3.1.1.53;
DE AltName: Full=Sialic acid-specific 9-O-acetylesterase;
DE AltName: Full=Yolk sac protein 2;
DE Contains:
DE RecName: Full=Sialate O-acetylesterase small subunit;
DE Contains:
DE RecName: Full=Sialate O-acetylesterase large subunit;
DE Flags: Precursor;
GN Name=Siae; Synonyms=Ysg2;
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] (ISOFORM 1).
RC STRAIN=C57BL/6 X DBA/2;
RX PubMed=8918804; DOI=10.1093/nar/24.20.4003;
RA Stoddart A., Zhang Y., Paige C.J.;
RT "Molecular cloning of the cDNA encoding a murine sialic acid-specific 9-O-
RT acetylesterase and RNA expression in cells of hematopoietic and non-
RT hematopoietic origin.";
RL Nucleic Acids Res. 24:4003-4008(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=8662838; DOI=10.1074/jbc.271.23.13697;
RA Guimaraes M.J., Bazan J.F., Castagnola J., Diaz S., Copeland N.G.,
RA Gilbert D.J., Jenkins N.A., Varki A., Zlotnik A.;
RT "Molecular cloning and characterization of lysosomal sialic acid O-
RT acetylesterase.";
RL J. Biol. Chem. 271:13697-13705(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=B-cell;
RX PubMed=10464298; DOI=10.1074/jbc.274.36.25623;
RA Takematsu H., Diaz S., Stoddart A., Zhang Y., Varki A.;
RT "Lysosomal and cytosolic sialic acid 9-O-acetylesterase activities can be
RT encoded by one gene via differential usage of a signal peptide-encoding
RT exon at the N-terminus.";
RL J. Biol. Chem. 274:25623-25631(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J;
RC TISSUE=Blastocyst, Cerebellum, Diencephalon, Embryonic head, Skin, and
RC Urinary bladder;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Catalyzes the removal of O-acetyl ester groups from position
CC 9 of the parent sialic acid, N-acetylneuraminic acid.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-acetyl-9-O-acetylneuraminate = acetate + H(+) + N-
CC acetylneuraminate; Xref=Rhea:RHEA:22600, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28999, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:35418; EC=3.1.1.53;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-acetyl-4-O-acetylneuraminate = acetate + H(+) + N-
CC acetylneuraminate; Xref=Rhea:RHEA:25564, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29006, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:35418; EC=3.1.1.53;
CC -!- ACTIVITY REGULATION: Inhibited by diisopropyl fluorophosphate and
CC diethyl-P-nitrophenyl phosphate. {ECO:0000250}.
CC -!- SUBUNIT: Disulfide-linked heterodimer of a small subunit and a large
CC subunit. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Lysosome.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Lse;
CC IsoId=P70665-1; Sequence=Displayed;
CC Name=2; Synonyms=Cse;
CC IsoId=P70665-2; Sequence=VSP_004077;
CC Name=3;
CC IsoId=P70665-3; Sequence=VSP_018996, VSP_018997;
CC -!- TISSUE SPECIFICITY: Isoform 1 is widely expressed. Isoform 2 shows a
CC more restricted distribution with highest expression in brain and ovary
CC and lower levels in liver and thymus.
CC -!- PTM: The two subunits are derived from a single precursor by
CC proteolytic cleavage. {ECO:0000250}.
CC -!- PTM: The lysosomal isoform is glycosylated.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC29164.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U61183; AAC52880.1; -; mRNA.
DR EMBL; X98625; CAA67214.1; -; mRNA.
DR EMBL; U40408; AAB07813.1; -; mRNA.
DR EMBL; AF156856; AAD55976.1; -; mRNA.
DR EMBL; AK028598; BAC26026.1; -; mRNA.
DR EMBL; AK028656; BAC26049.1; -; mRNA.
DR EMBL; AK033980; BAC28536.1; -; mRNA.
DR EMBL; AK035715; BAC29164.1; ALT_INIT; mRNA.
DR EMBL; AK043392; BAC31534.1; -; mRNA.
DR EMBL; AK164852; BAE37942.1; -; mRNA.
DR EMBL; AK167103; BAE39252.1; -; mRNA.
DR EMBL; BC007136; AAH07136.1; -; mRNA.
DR CCDS; CCDS22983.1; -. [P70665-1]
DR RefSeq; NP_035864.2; NM_011734.3. [P70665-1]
DR AlphaFoldDB; P70665; -.
DR SMR; P70665; -.
DR BioGRID; 204616; 17.
DR STRING; 10090.ENSMUSP00000002007; -.
DR GlyConnect; 2708; 3 N-Linked glycans (2 sites).
DR GlyGen; P70665; 8 sites, 3 N-linked glycans (2 sites).
DR PhosphoSitePlus; P70665; -.
DR EPD; P70665; -.
DR MaxQB; P70665; -.
DR PaxDb; P70665; -.
DR PeptideAtlas; P70665; -.
DR PRIDE; P70665; -.
DR ProteomicsDB; 257240; -. [P70665-1]
DR ProteomicsDB; 257241; -. [P70665-2]
DR ProteomicsDB; 257242; -. [P70665-3]
DR Antibodypedia; 32895; 67 antibodies from 16 providers.
DR Ensembl; ENSMUST00000215474; ENSMUSP00000149505; ENSMUSG00000001942. [P70665-1]
DR GeneID; 22619; -.
DR KEGG; mmu:22619; -.
DR UCSC; uc009ove.1; mouse. [P70665-3]
DR UCSC; uc009ovf.1; mouse. [P70665-1]
DR CTD; 54414; -.
DR MGI; MGI:104803; Siae.
DR VEuPathDB; HostDB:ENSMUSG00000001942; -.
DR eggNOG; ENOG502QUKD; Eukaryota.
DR GeneTree; ENSGT00390000010608; -.
DR HOGENOM; CLU_015150_1_0_1; -.
DR InParanoid; P70665; -.
DR OMA; PCEFKAC; -.
DR OrthoDB; 745508at2759; -.
DR PhylomeDB; P70665; -.
DR TreeFam; TF328611; -.
DR BRENDA; 3.1.1.53; 3474.
DR BioGRID-ORCS; 22619; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Siae; mouse.
DR PRO; PR:P70665; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P70665; protein.
DR Bgee; ENSMUSG00000001942; Expressed in small intestine Peyer's patch and 230 other tissues.
DR ExpressionAtlas; P70665; baseline and differential.
DR Genevisible; P70665; MM.
DR GO; GO:0005764; C:lysosome; IDA:MGI.
DR GO; GO:0106331; F:sialate 4-O-acetylesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0106330; F:sialate 9-O-acetylesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0001681; F:sialate O-acetylesterase activity; ISO:MGI.
DR GO; GO:0005975; P:carbohydrate metabolic process; ISO:MGI.
DR GO; GO:0002682; P:regulation of immune system process; ISO:MGI.
DR Gene3D; 3.40.50.1110; -; 1.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR InterPro; IPR039329; SIAE.
DR PANTHER; PTHR22901; PTHR22901; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Disulfide bond; Glycoprotein; Hydrolase;
KW Lysosome; Reference proteome; Serine esterase; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000250"
FT CHAIN 24..275
FT /note="Sialate O-acetylesterase small subunit"
FT /id="PRO_0000022714"
FT CHAIN 276..541
FT /note="Sialate O-acetylesterase large subunit"
FT /id="PRO_0000022715"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 427
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 448
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 462
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..97
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10464298"
FT /id="VSP_004077"
FT VAR_SEQ 349..390
FT /note="LSSYMLKNSSDYGFPEIRWHQTADFGHVPNPKMPNTFMAVAI -> VCIQRI
FT HIQCLEFMGLCGECGLCTCLYWDLQPNICPNSMSWR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018996"
FT VAR_SEQ 391..541
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018997"
FT CONFLICT 114
FT /note="D -> N (in Ref. 4; BAE37942)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="I -> T (in Ref. 2; AAB07813 and 5; AAH07136)"
FT /evidence="ECO:0000305"
FT CONFLICT 349
FT /note="L -> Q (in Ref. 4; BAC26026)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="F -> L (in Ref. 4; BAC29164)"
FT /evidence="ECO:0000305"
FT CONFLICT 379
FT /note="P -> L (in Ref. 5; AAH07136)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 541 AA; 60775 MW; 944936C45C4A2E6B CRC64;
MVSPGPVFGI VLLIIARVSR SAGIGFRFAS YIDNYMVLQK EPSGAVIWGF GTPGATVTVT
LCQGQETIMK KVTSVKEPSN TWMVVLDPMK PGGPFEVMAQ QTLGTMNFTL RVHDVLFGDV
WLCSGQSNMQ MTVSQIFNAS KELSDTAAYQ SVRIFSVSLI QSEEELDDLT EVDLSWSKPT
AGNLGHGNFT YMSAVCWLFG RYLYDTLQYP IGLVSSSWGG TYIEVWSSRR TLKACGVPNT
RDERVGQPEI KPMRNECNSE ESSCPFRVVP SVRVTGPTRH SVLWNAMIHP LQNMTLKGVV
WYQGESNADY NRDLYTCMFP ELIEDWRQTF HYGSQGQTDR FFPFGFVQLS SYMLKNSSDY
GFPEIRWHQT ADFGHVPNPK MPNTFMAVAI DLCDRDSPFG SIHPRDKQTV AYRLHLGARA
VAYGEKNLTF QGPLPKKIEL LASNGLLNLT YDQEIQVQMQ DNKTFEISCC SDRHCKWLPA
PVNTFSTQTL ILDLNACLGT VVAVRYAWTT WPCEYKQCAV YHTSSMLPAP PFIAQISHRG
I
