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P82450

- SIAE_RAT

UniProt

P82450 - SIAE_RAT

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Protein
Sialate O-acetylesterase
Gene
Siae, Ysg2
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323 By similarity
Add
BLAST
Chaini24 – 276253Sialate O-acetylesterase small subunit By similarity
PRO_0000022716Add
BLAST
Chaini277 – 542266Sialate O-acetylesterase large subunit By similarity
PRO_0000022717Add
BLAST

Amino acid modifications

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

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

« Hide

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 273GFR → PFP AA sequence 1 Publication
Sequence conflicti48 – 481W → L AA sequence 1 Publication
Sequence conflicti50 – 501F → L AA sequence 1 Publication
Sequence conflicti290 – 2901Missing AA sequence 1 Publication
Sequence conflicti294 – 2963NMT → TMR AA sequence 1 Publication

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

« Hide 'large scale' publications
  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: April 16, 2014
This is version 55 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

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