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Protein

Sialate O-acetylesterase

Gene

Siae

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Enzyme and pathway databases

BRENDAi3.1.1.53. 3474.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:104803. Siae.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323By similarityAdd
BLAST
Chaini24 – 275252Sialate O-acetylesterase small subunitPRO_0000022714Add
BLAST
Chaini276 – 541266Sialate O-acetylesterase large subunitPRO_0000022715Add
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
Glycosylationi293 – 2931N-linked (GlcNAc...)Sequence Analysis
Glycosylationi356 – 3561N-linked (GlcNAc...)Sequence Analysis
Glycosylationi427 – 4271N-linked (GlcNAc...)Sequence Analysis
Glycosylationi448 – 4481N-linked (GlcNAc...)Sequence Analysis
Glycosylationi462 – 4621N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

The two subunits are derived from a single precursor by proteolytic cleavage.By similarity
The lysosomal isoform is glycosylated.

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP70665.
PaxDbiP70665.
PRIDEiP70665.

PTM databases

PhosphoSiteiP70665.

Expressioni

Tissue specificityi

Isoform 1 is widely expressed. Isoform 2 shows a more restricted distribution with highest expression in brain and ovary and lower levels in liver and thymus.

Gene expression databases

BgeeiP70665.
CleanExiMM_SIAE.
ExpressionAtlasiP70665. baseline and differential.
GenevisibleiP70665. MM.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiP70665. 1 interaction.
MINTiMINT-4115423.

Structurei

3D structure databases

ProteinModelPortaliP70665.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG41492.
GeneTreeiENSGT00390000010608.
HOVERGENiHBG007955.
InParanoidiP70665.
KOiK05970.
OMAiLRFASYY.
OrthoDBiEOG7H1JKC.
PhylomeDBiP70665.
TreeFamiTF328611.

Family and domain databases

InterProiIPR005181. DUF303_acetylest.
IPR013830. SGNH_hydro.
[Graphical view]
PfamiPF03629. DUF303. 1 hit.
[Graphical view]
SUPFAMiSSF52266. SSF52266. 2 hits.

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P70665-1) [UniParc]FASTAAdd to basket

Also known as: Lse

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MVSPGPVFGI VLLIIARVSR SAGIGFRFAS YIDNYMVLQK EPSGAVIWGF
60 70 80 90 100
GTPGATVTVT LCQGQETIMK KVTSVKEPSN TWMVVLDPMK PGGPFEVMAQ
110 120 130 140 150
QTLGTMNFTL RVHDVLFGDV WLCSGQSNMQ MTVSQIFNAS KELSDTAAYQ
160 170 180 190 200
SVRIFSVSLI QSEEELDDLT EVDLSWSKPT AGNLGHGNFT YMSAVCWLFG
210 220 230 240 250
RYLYDTLQYP IGLVSSSWGG TYIEVWSSRR TLKACGVPNT RDERVGQPEI
260 270 280 290 300
KPMRNECNSE ESSCPFRVVP SVRVTGPTRH SVLWNAMIHP LQNMTLKGVV
310 320 330 340 350
WYQGESNADY NRDLYTCMFP ELIEDWRQTF HYGSQGQTDR FFPFGFVQLS
360 370 380 390 400
SYMLKNSSDY GFPEIRWHQT ADFGHVPNPK MPNTFMAVAI DLCDRDSPFG
410 420 430 440 450
SIHPRDKQTV AYRLHLGARA VAYGEKNLTF QGPLPKKIEL LASNGLLNLT
460 470 480 490 500
YDQEIQVQMQ DNKTFEISCC SDRHCKWLPA PVNTFSTQTL ILDLNACLGT
510 520 530 540
VVAVRYAWTT WPCEYKQCAV YHTSSMLPAP PFIAQISHRG I
Length:541
Mass (Da):60,775
Last modified:May 30, 2006 - v3
Checksum:i944936C45C4A2E6B
GO
Isoform 2 (identifier: P70665-2) [UniParc]FASTAAdd to basket

Also known as: Cse

The sequence of this isoform differs from the canonical sequence as follows:
     1-97: Missing.

Show »
Length:444
Mass (Da):50,389
Checksum:i0AFDFCCEF3549C53
GO
Isoform 3 (identifier: P70665-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     349-390: LSSYMLKNSS...MPNTFMAVAI → VCIQRIHIQC...NICPNSMSWR
     391-541: Missing.

Note: No experimental confirmation available.
Show »
Length:390
Mass (Da):43,888
Checksum:i7EED447751832279
GO

Sequence cautioni

The sequence BAC29164.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti114 – 1141D → N in BAE37942 (PubMed:16141072).Curated
Sequence conflicti160 – 1601I → T in AAB07813 (PubMed:8662838).Curated
Sequence conflicti160 – 1601I → T in AAH07136 (PubMed:15489334).Curated
Sequence conflicti349 – 3491L → Q in BAC26026 (PubMed:16141072).Curated
Sequence conflicti373 – 3731F → L in BAC29164 (PubMed:16141072).Curated
Sequence conflicti379 – 3791P → L in AAH07136 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 9797Missing in isoform 2. 1 PublicationVSP_004077Add
BLAST
Alternative sequencei349 – 39042LSSYM…MAVAI → VCIQRIHIQCLEFMGLCGEC GLCTCLYWDLQPNICPNSMS WR in isoform 3. 1 PublicationVSP_018996Add
BLAST
Alternative sequencei391 – 541151Missing in isoform 3. 1 PublicationVSP_018997Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U61183 mRNA. Translation: AAC52880.1.
X98625 mRNA. Translation: CAA67214.1.
U40408 mRNA. Translation: AAB07813.1.
AF156856 mRNA. Translation: AAD55976.1.
AK028598 mRNA. Translation: BAC26026.1.
AK028656 mRNA. Translation: BAC26049.1.
AK033980 mRNA. Translation: BAC28536.1.
AK035715 mRNA. Translation: BAC29164.1. Different initiation.
AK043392 mRNA. Translation: BAC31534.1.
AK164852 mRNA. Translation: BAE37942.1.
AK167103 mRNA. Translation: BAE39252.1.
BC007136 mRNA. Translation: AAH07136.1.
CCDSiCCDS22983.1. [P70665-1]
RefSeqiNP_035864.2. NM_011734.3. [P70665-1]
UniGeneiMm.196345.

Genome annotation databases

EnsembliENSMUST00000002007; ENSMUSP00000002007; ENSMUSG00000001942. [P70665-1]
GeneIDi22619.
KEGGimmu:22619.
UCSCiuc009ove.1. mouse. [P70665-3]
uc009ovf.1. mouse. [P70665-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U61183 mRNA. Translation: AAC52880.1.
X98625 mRNA. Translation: CAA67214.1.
U40408 mRNA. Translation: AAB07813.1.
AF156856 mRNA. Translation: AAD55976.1.
AK028598 mRNA. Translation: BAC26026.1.
AK028656 mRNA. Translation: BAC26049.1.
AK033980 mRNA. Translation: BAC28536.1.
AK035715 mRNA. Translation: BAC29164.1. Different initiation.
AK043392 mRNA. Translation: BAC31534.1.
AK164852 mRNA. Translation: BAE37942.1.
AK167103 mRNA. Translation: BAE39252.1.
BC007136 mRNA. Translation: AAH07136.1.
CCDSiCCDS22983.1. [P70665-1]
RefSeqiNP_035864.2. NM_011734.3. [P70665-1]
UniGeneiMm.196345.

3D structure databases

ProteinModelPortaliP70665.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP70665. 1 interaction.
MINTiMINT-4115423.

PTM databases

PhosphoSiteiP70665.

Proteomic databases

MaxQBiP70665.
PaxDbiP70665.
PRIDEiP70665.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000002007; ENSMUSP00000002007; ENSMUSG00000001942. [P70665-1]
GeneIDi22619.
KEGGimmu:22619.
UCSCiuc009ove.1. mouse. [P70665-3]
uc009ovf.1. mouse. [P70665-1]

Organism-specific databases

CTDi54414.
MGIiMGI:104803. Siae.

Phylogenomic databases

eggNOGiNOG41492.
GeneTreeiENSGT00390000010608.
HOVERGENiHBG007955.
InParanoidiP70665.
KOiK05970.
OMAiLRFASYY.
OrthoDBiEOG7H1JKC.
PhylomeDBiP70665.
TreeFamiTF328611.

Enzyme and pathway databases

BRENDAi3.1.1.53. 3474.

Miscellaneous databases

NextBioi302973.
PROiP70665.
SOURCEiSearch...

Gene expression databases

BgeeiP70665.
CleanExiMM_SIAE.
ExpressionAtlasiP70665. baseline and differential.
GenevisibleiP70665. MM.

Family and domain databases

InterProiIPR005181. DUF303_acetylest.
IPR013830. SGNH_hydro.
[Graphical view]
PfamiPF03629. DUF303. 1 hit.
[Graphical view]
SUPFAMiSSF52266. SSF52266. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of the cDNA encoding a murine sialic acid-specific 9-O-acetylesterase and RNA expression in cells of hematopoietic and non-hematopoietic origin."
    Stoddart A., Zhang Y., Paige C.J.
    Nucleic Acids Res. 24:4003-4008(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: C57BL/6 X DBA/2.
  2. "Molecular cloning and characterization of lysosomal sialic acid O-acetylesterase."
    Guimaraes M.J., Bazan J.F., Castagnola J., Diaz S., Copeland N.G., Gilbert D.J., Jenkins N.A., Varki A., Zlotnik A.
    J. Biol. Chem. 271:13697-13705(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Lysosomal and cytosolic sialic acid 9-O-acetylesterase activities can be encoded by one gene via differential usage of a signal peptide-encoding exon at the N-terminus."
    Takematsu H., Diaz S., Stoddart A., Zhang Y., Varki A.
    J. Biol. Chem. 274:25623-25631(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: B-cell.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
    Strain: C57BL/6J.
    Tissue: Blastocyst, Cerebellum, Diencephalon, Embryonic head, Skin and Urinary bladder.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).

Entry informationi

Entry nameiSIAE_MOUSE
AccessioniPrimary (citable) accession number: P70665
Secondary accession number(s): Q3TNZ5
, Q544V7, Q61044, Q8C902, Q8CBM6, Q8CC41, Q8CEB7, Q922L0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: May 30, 2006
Last modified: June 24, 2015
This is version 112 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.