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P82450 (SIAE_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Sialate O-acetylesterase

EC=3.1.1.53
Alternative name(s):
Sialic acid-specific 9-O-acetylesterase
Yolk sac protein 2
Gene names
Name:Siae
Synonyms:Ysg2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length542 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the removal of O-acetyl ester groups from position 9 of the parent sialic acid, N-acetylneuraminic acid.

Catalytic activity

N-acetyl-O-acetylneuraminate + H2O = N-acetylneuraminate + acetate.

Enzyme regulation

Inhibited by diisopropyl fluorophosphate and diethyl-P-nitrophenyl phosphate.

Subunit structure

Disulfide-linked heterodimer of a small subunit and a large subunit.

Subcellular location

Lysosome.

Tissue specificity

Widely expressed.

Post-translational modification

The two subunits are derived from a single precursor by proteolytic cleavage.

Glycosylated.

Ontologies

Keywords
   Cellular componentLysosome
   DomainSignal
   Molecular functionHydrolase
Serine esterase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Cellular_componentlysosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionsialate O-acetylesterase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 By similarity
Chain24 – 276253Sialate O-acetylesterase small subunit By similarity
PRO_0000022716
Chain277 – 542266Sialate O-acetylesterase large subunit By similarity
PRO_0000022717

Amino acid modifications

Glycosylation1071N-linked (GlcNAc...) Potential
Glycosylation1381N-linked (GlcNAc...) Potential
Glycosylation1881N-linked (GlcNAc...) Potential
Glycosylation2941N-linked (GlcNAc...) Potential
Glycosylation3571N-linked (GlcNAc...) Potential
Glycosylation4281N-linked (GlcNAc...) Potential
Glycosylation4491N-linked (GlcNAc...) Potential
Glycosylation4631N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict25 – 273GFR → PFP AA sequence Ref.2
Sequence conflict481W → L AA sequence Ref.2
Sequence conflict501F → L AA sequence Ref.2
Sequence conflict2901Missing AA sequence Ref.2
Sequence conflict294 – 2963NMT → TMR AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
P82450 [UniParc].

Last modified May 31, 2011. Version 2.
Checksum: FC4BCD1295F2A830

FASTA54260,466
        10         20         30         40         50         60 
MVSPRPVGLM LLLIIARVSR GAGIGFRFAS YIDNYMVLQK EPSGAVIWGF GTAGATVTVT 

        70         80         90        100        110        120 
LCQGQETIMK KVTSVKGPSN TWMVVLDPMK PGGPFEVMAQ QTLETTNLTL RVHDVLFGDV 

       130        140        150        160        170        180 
WLCSGQSNMQ MTVLQIFNAS KELSDTAAYQ SVRIFSVSLT QAEEELADLD GVDLSWSKPT 

       190        200        210        220        230        240 
AGNLGHGNFT YMSAVCWLFG RYLYDTLQYP IGLVSSSWGG TPIEVWSSRR ALKACGVPNT 

       250        260        270        280        290        300 
RDERVLQPEI KPMRNGCESK ESSCPFRRFV PCDPVAGPAT HSVLWNAMIH PLQNMTLKGV 

       310        320        330        340        350        360 
VWYQGENNAN YNRDLYACMF PALIAGWRQT FHSGCQGQTE RFFPFGFVQL SSYLLMNSSD 

       370        380        390        400        410        420 
YGFPEIRWHQ TADFGSVPNP KMPNTFMAVA MDLCDRDSPF GSIHPRDKQT VAYRLHLGAR 

       430        440        450        460        470        480 
AVAYGEKNLT FQGPLPKKIE LLARNELLNL TYDQEIQVQR KDNKTFEISC CSDHQCKWLP 

       490        500        510        520        530        540 
APVNTFSTQT LILDLSACLG TVDAVRYAWT TWPCEYKQCA VYHTSSVLPA PPFTARITHR 


GI 

« Hide

References

« Hide 'large scale' references
[1]"Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. expand/collapse author list , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Brown Norway.
[2]"Structural, immunological, and biosynthetic studies of a sialic acid-specific O-acetylesterase from rat liver."
Butor C., Higa H.H., Varki A.
J. Biol. Chem. 268:10207-10213(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 24-50 AND 277-307.
Tissue: Liver.
[3]"O-acetylation and de-O-acetylation of sialic acids. Purification, characterization, and properties of a glycosylated rat liver esterase specific for 9-O-acetylated sialic acids."
Higa H.H., Manzi A., Varki A.
J. Biol. Chem. 264:19435-19442(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
Tissue: Liver.

Cross-references

Sequence databases

PIRA46690.
B46690.
UniGeneRn.21775.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000042202.

Proteomic databases

PaxDbP82450.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCRGD:1310431. rat.

Organism-specific databases

RGD1310431. Siae.

Phylogenomic databases

eggNOGNOG41492.
OrthoDBEOG7H1JKC.
PhylomeDBP82450.
TreeFamTF328611.

Gene expression databases

GenevestigatorP82450.

Family and domain databases

InterProIPR005181. DUF303_acetylest.
[Graphical view]
PfamPF03629. DUF303. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROP82450.

Entry information

Entry nameSIAE_RAT
AccessionPrimary (citable) accession number: P82450
Entry history
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: May 31, 2011
Last modified: April 16, 2014
This is version 55 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program