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P82450

- SIAE_RAT

UniProt

P82450 - SIAE_RAT

Protein

Sialate O-acetylesterase

Gene

Siae

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 56 (01 Oct 2014)
      Sequence version 2 (31 May 2011)
      Previous versions | rss
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    Functioni

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

    Catalytic activityi

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

    Enzyme regulationi

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

    GO - Molecular functioni

    1. sialate O-acetylesterase activity Source: UniProtKB-EC

    Keywords - Molecular functioni

    Hydrolase, Serine esterase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sialate O-acetylesterase (EC:3.1.1.53)
    Alternative name(s):
    Sialic acid-specific 9-O-acetylesterase
    Yolk sac protein 2
    Cleaved into the following 2 chains:
    Gene namesi
    Name:Siae
    Synonyms:Ysg2
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi1310431. Siae.

    Subcellular locationi

    GO - Cellular componenti

    1. lysosome Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Lysosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323By similarityAdd
    BLAST
    Chaini24 – 276253Sialate O-acetylesterase small subunitBy similarityPRO_0000022716Add
    BLAST
    Chaini277 – 542266Sialate O-acetylesterase large subunitBy similarityPRO_0000022717Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi107 – 1071N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi138 – 1381N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi188 – 1881N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi294 – 2941N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi357 – 3571N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi428 – 4281N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi449 – 4491N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi463 – 4631N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

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

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiP82450.

    Expressioni

    Tissue specificityi

    Widely expressed.

    Gene expression databases

    GenevestigatoriP82450.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000042202.

    Family & Domainsi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG41492.
    OrthoDBiEOG7H1JKC.
    PhylomeDBiP82450.
    TreeFamiTF328611.

    Family and domain databases

    InterProiIPR005181. DUF303_acetylest.
    [Graphical view]
    PfamiPF03629. DUF303. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P82450-1 [UniParc]FASTAAdd to Basket

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    MVSPRPVGLM LLLIIARVSR GAGIGFRFAS YIDNYMVLQK EPSGAVIWGF    50
    GTAGATVTVT LCQGQETIMK KVTSVKGPSN TWMVVLDPMK PGGPFEVMAQ 100
    QTLETTNLTL RVHDVLFGDV WLCSGQSNMQ MTVLQIFNAS KELSDTAAYQ 150
    SVRIFSVSLT QAEEELADLD GVDLSWSKPT AGNLGHGNFT YMSAVCWLFG 200
    RYLYDTLQYP IGLVSSSWGG TPIEVWSSRR ALKACGVPNT RDERVLQPEI 250
    KPMRNGCESK ESSCPFRRFV PCDPVAGPAT HSVLWNAMIH PLQNMTLKGV 300
    VWYQGENNAN YNRDLYACMF PALIAGWRQT FHSGCQGQTE RFFPFGFVQL 350
    SSYLLMNSSD YGFPEIRWHQ TADFGSVPNP KMPNTFMAVA MDLCDRDSPF 400
    GSIHPRDKQT VAYRLHLGAR AVAYGEKNLT FQGPLPKKIE LLARNELLNL 450
    TYDQEIQVQR KDNKTFEISC CSDHQCKWLP APVNTFSTQT LILDLSACLG 500
    TVDAVRYAWT TWPCEYKQCA VYHTSSVLPA PPFTARITHR GI 542
    Length:542
    Mass (Da):60,466
    Last modified:May 31, 2011 - v2
    Checksum:iFC4BCD1295F2A830
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti25 – 273GFR → PFP AA sequence (PubMed:8486688)Curated
    Sequence conflicti48 – 481W → L AA sequence (PubMed:8486688)Curated
    Sequence conflicti50 – 501F → L AA sequence (PubMed:8486688)Curated
    Sequence conflicti290 – 2901Missing AA sequence (PubMed:8486688)Curated
    Sequence conflicti294 – 2963NMT → TMR AA sequence (PubMed:8486688)Curated

    Sequence databases

    PIRiA46690.
    B46690.
    UniGeneiRn.21775.

    Genome annotation databases

    UCSCiRGD:1310431. rat.

    Cross-referencesi

    Sequence databases

    PIRi A46690.
    B46690.
    UniGenei Rn.21775.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000042202.

    Proteomic databases

    PaxDbi P82450.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    UCSCi RGD:1310431. rat.

    Organism-specific databases

    RGDi 1310431. Siae.

    Phylogenomic databases

    eggNOGi NOG41492.
    OrthoDBi EOG7H1JKC.
    PhylomeDBi P82450.
    TreeFami TF328611.

    Miscellaneous databases

    PROi P82450.

    Gene expression databases

    Genevestigatori P82450.

    Family and domain databases

    InterProi IPR005181. DUF303_acetylest.
    [Graphical view ]
    Pfami PF03629. DUF303. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.

    Entry informationi

    Entry nameiSIAE_RAT
    AccessioniPrimary (citable) accession number: P82450
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 15, 2002
    Last sequence update: May 31, 2011
    Last modified: October 1, 2014
    This is version 56 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    External Data

    Dasty 3