SIAE_RAT
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 25-MAY-2022, entry version 80.
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 GlyGen; P82450; 8 sites.
DR PaxDb; P82450; -.
DR PRIDE; P82450; -.
DR UCSC; RGD:1310431; rat.
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: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: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; -; 1.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR InterPro; IPR039329; SIAE.
DR PANTHER; PTHR22901; PTHR22901; 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
