ID   SIAE_RAT                Reviewed;         542 AA.
AC   P82450;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 2.
DT   27-MAR-2024, entry version 85.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   PROTEIN SEQUENCE OF 24-50 AND 277-307.
RC   TISSUE=Liver;
RX   PubMed=8486688; DOI=10.1016/s0021-9258(18)82191-3;
RA   Butor C., Higa H.H., Varki A.;
RT   "Structural, immunological, and biosynthetic studies of a sialic acid-
RT   specific O-acetylesterase from rat liver.";
RL   J. Biol. Chem. 268:10207-10213(1993).
RN   [3]
RP   CHARACTERIZATION.
RC   TISSUE=Liver;
RX   PubMed=2808434; DOI=10.1016/s0021-9258(19)47319-5;
RA   Higa H.H., Manzi A., Varki A.;
RT   "O-acetylation and de-O-acetylation of sialic acids. Purification,
RT   characterization, and properties of a glycosylated rat liver esterase
RT   specific for 9-O-acetylated sialic acids.";
RL   J. Biol. Chem. 264:19435-19442(1989).
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.
CC   -!- SUBUNIT: Disulfide-linked heterodimer of a small subunit and a large
CC       subunit.
CC   -!- SUBCELLULAR LOCATION: Lysosome.
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC   -!- PTM: The two subunits are derived from a single precursor by
CC       proteolytic cleavage.
CC   -!- PTM: Glycosylated.
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DR   PIR; A46690; A46690.
DR   PIR; B46690; B46690.
DR   AlphaFoldDB; P82450; -.
DR   SMR; P82450; -.
DR   STRING; 10116.ENSRNOP00000042202; -.
DR   GlyCosmos; P82450; 8 sites, No reported glycans.
DR   GlyGen; P82450; 8 sites.
DR   PhosphoSitePlus; P82450; -.
DR   PaxDb; 10116-ENSRNOP00000042202; -.
DR   UCSC; RGD:1310431; rat.
DR   AGR; RGD:1310431; -.
DR   RGD; 1310431; Siae.
DR   eggNOG; ENOG502QUKD; Eukaryota.
DR   InParanoid; P82450; -.
DR   PhylomeDB; P82450; -.
DR   TreeFam; TF328611; -.
DR   PRO; PR:P82450; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005764; C:lysosome; ISO:RGD.
DR   GO; GO:0106331; F:sialate 4-O-acetylesterase activity; IEA:RHEA.
DR   GO; GO:0106330; F:sialate 9-O-acetylesterase activity; IEA:RHEA.
DR   GO; GO:0001681; F:sialate O-acetylesterase activity; ISO:RGD.
DR   GO; GO:0005975; P:carbohydrate metabolic process; ISO:RGD.
DR   GO; GO:0002682; P:regulation of immune system process; ISO:RGD.
DR   Gene3D; 3.40.50.1110; SGNH hydrolase; 1.
DR   InterPro; IPR036514; SGNH_hydro_sf.
DR   InterPro; IPR039329; SIAE.
DR   PANTHER; PTHR22901; SIALATE O-ACETYLESTERASE; 1.
DR   PANTHER; PTHR22901:SF0; SIALATE O-ACETYLESTERASE; 1.
DR   SUPFAM; SSF52266; SGNH hydrolase; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW   Lysosome; Reference proteome; Serine esterase; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000250"
FT   CHAIN           24..276
FT                   /note="Sialate O-acetylesterase small subunit"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000022716"
FT   CHAIN           277..542
FT                   /note="Sialate O-acetylesterase large subunit"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000022717"
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        294
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        357
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        428
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        449
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        463
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        25..27
FT                   /note="GFR -> PFP (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        48
FT                   /note="W -> L (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        50
FT                   /note="F -> L (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        290
FT                   /note="Missing (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        294..296
FT                   /note="NMT -> TMR (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   542 AA;  60466 MW;  FC4BCD1295F2A830 CRC64;
     MVSPRPVGLM LLLIIARVSR GAGIGFRFAS YIDNYMVLQK EPSGAVIWGF GTAGATVTVT
     LCQGQETIMK KVTSVKGPSN TWMVVLDPMK PGGPFEVMAQ QTLETTNLTL RVHDVLFGDV
     WLCSGQSNMQ MTVLQIFNAS KELSDTAAYQ SVRIFSVSLT QAEEELADLD GVDLSWSKPT
     AGNLGHGNFT YMSAVCWLFG RYLYDTLQYP IGLVSSSWGG TPIEVWSSRR ALKACGVPNT
     RDERVLQPEI KPMRNGCESK ESSCPFRRFV PCDPVAGPAT HSVLWNAMIH PLQNMTLKGV
     VWYQGENNAN YNRDLYACMF PALIAGWRQT FHSGCQGQTE RFFPFGFVQL SSYLLMNSSD
     YGFPEIRWHQ TADFGSVPNP KMPNTFMAVA MDLCDRDSPF GSIHPRDKQT VAYRLHLGAR
     AVAYGEKNLT FQGPLPKKIE LLARNELLNL TYDQEIQVQR KDNKTFEISC CSDHQCKWLP
     APVNTFSTQT LILDLSACLG TVDAVRYAWT TWPCEYKQCA VYHTSSVLPA PPFTARITHR
     GI
//