P70665 (SIAE_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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:

1. Sialate O-acetylesterase small subunit
2. Sialate O-acetylesterase large subunit

Gene names

Name:	Siae
Synonyms:	Ysg2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	541 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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 By similarity.
Subunit structure	Disulfide-linked heterodimer of a small subunit and a large subunit By similarity.
Subcellular location	Isoform 1: Lysosome. Isoform 2: Cytoplasm.
Tissue specificity	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.
Post-translational modification	The two subunits are derived from a single precursor by proteolytic cleavage By similarity. The lysosomal isoform is glycosylated.
Sequence caution	The sequence BAC29164.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cytoplasm Lysosome
Coding sequence diversity	Alternative splicing
Domain	Signal
Molecular function	Hydrolase Serine esterase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	lysosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	carboxylesterase activity Inferred from electronic annotation. Source: UniProtKB-KW sialate O-acetylesterase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P70665-1)

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.

Isoform 2 (identifier: P70665-2)

Also known as: Cse;

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

Isoform 3 (identifier: P70665-3)

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.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 23	23	By similarity
	Chain	24 – 275	252	Sialate O-acetylesterase small subunit		PRO_0000022714
	Chain	276 – 541	266	Sialate O-acetylesterase large subunit		PRO_0000022715
Amino acid modifications
	Glycosylation	107	1	N-linked (GlcNAc...) Potential
	Glycosylation	138	1	N-linked (GlcNAc...) Potential
	Glycosylation	188	1	N-linked (GlcNAc...) Potential
	Glycosylation	293	1	N-linked (GlcNAc...) Potential
	Glycosylation	356	1	N-linked (GlcNAc...) Potential
	Glycosylation	427	1	N-linked (GlcNAc...) Potential
	Glycosylation	448	1	N-linked (GlcNAc...) Potential
	Glycosylation	462	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	1 – 97	97	Missing in isoform 2.		VSP_004077
	Alternative sequence	349 – 390	42	LSSYM…MAVAI → VCIQRIHIQCLEFMGLCGEC GLCTCLYWDLQPNICPNSMS WR in isoform 3.		VSP_018996
	Alternative sequence	391 – 541	151	Missing in isoform 3.		VSP_018997
Experimental info
	Sequence conflict	114	1	D → N in BAE37942. Ref.4
	Sequence conflict	160	1	I → T in AAB07813. Ref.2
	Sequence conflict	160	1	I → T in AAH07136. Ref.5
	Sequence conflict	349	1	L → Q in BAC26026. Ref.4
	Sequence conflict	373	1	F → L in BAC29164. Ref.4
	Sequence conflict	379	1	P → L in AAH07136. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Lse) [UniParc]. Last modified May 30, 2006. Version 3. Checksum: 944936C45C4A2E6B	FASTA	541	60,775
	10 20 30 40 50 60 MVSPGPVFGI VLLIIARVSR SAGIGFRFAS YIDNYMVLQK EPSGAVIWGF GTPGATVTVT 70 80 90 100 110 120 LCQGQETIMK KVTSVKEPSN TWMVVLDPMK PGGPFEVMAQ QTLGTMNFTL RVHDVLFGDV 130 140 150 160 170 180 WLCSGQSNMQ MTVSQIFNAS KELSDTAAYQ SVRIFSVSLI QSEEELDDLT EVDLSWSKPT 190 200 210 220 230 240 AGNLGHGNFT YMSAVCWLFG RYLYDTLQYP IGLVSSSWGG TYIEVWSSRR TLKACGVPNT 250 260 270 280 290 300 RDERVGQPEI KPMRNECNSE ESSCPFRVVP SVRVTGPTRH SVLWNAMIHP LQNMTLKGVV 310 320 330 340 350 360 WYQGESNADY NRDLYTCMFP ELIEDWRQTF HYGSQGQTDR FFPFGFVQLS SYMLKNSSDY 370 380 390 400 410 420 GFPEIRWHQT ADFGHVPNPK MPNTFMAVAI DLCDRDSPFG SIHPRDKQTV AYRLHLGARA 430 440 450 460 470 480 VAYGEKNLTF QGPLPKKIEL LASNGLLNLT YDQEIQVQMQ DNKTFEISCC SDRHCKWLPA 490 500 510 520 530 540 PVNTFSTQTL ILDLNACLGT VVAVRYAWTT WPCEYKQCAV YHTSSMLPAP PFIAQISHRG I
	Isoform 2 (Cse) [UniParc]. Checksum: 0AFDFCCEF3549C53	FASTA	444	50,389
	10 20 30 40 50 60 MAQQTLGTMN FTLRVHDVLF GDVWLCSGQS NMQMTVSQIF NASKELSDTA AYQSVRIFSV 70 80 90 100 110 120 SLIQSEEELD DLTEVDLSWS KPTAGNLGHG NFTYMSAVCW LFGRYLYDTL QYPIGLVSSS 130 140 150 160 170 180 WGGTYIEVWS SRRTLKACGV PNTRDERVGQ PEIKPMRNEC NSEESSCPFR VVPSVRVTGP 190 200 210 220 230 240 TRHSVLWNAM IHPLQNMTLK GVVWYQGESN ADYNRDLYTC MFPELIEDWR QTFHYGSQGQ 250 260 270 280 290 300 TDRFFPFGFV QLSSYMLKNS SDYGFPEIRW HQTADFGHVP NPKMPNTFMA VAIDLCDRDS 310 320 330 340 350 360 PFGSIHPRDK QTVAYRLHLG ARAVAYGEKN LTFQGPLPKK IELLASNGLL NLTYDQEIQV 370 380 390 400 410 420 QMQDNKTFEI SCCSDRHCKW LPAPVNTFST QTLILDLNAC LGTVVAVRYA WTTWPCEYKQ 430 440 CAVYHTSSML PAPPFIAQIS HRGI
	Isoform 3 [UniParc]. Checksum: 7EED447751832279	FASTA	390	43,888
	10 20 30 40 50 60 MVSPGPVFGI VLLIIARVSR SAGIGFRFAS YIDNYMVLQK EPSGAVIWGF GTPGATVTVT 70 80 90 100 110 120 LCQGQETIMK KVTSVKEPSN TWMVVLDPMK PGGPFEVMAQ QTLGTMNFTL RVHDVLFGDV 130 140 150 160 170 180 WLCSGQSNMQ MTVSQIFNAS KELSDTAAYQ SVRIFSVSLI QSEEELDDLT EVDLSWSKPT 190 200 210 220 230 240 AGNLGHGNFT YMSAVCWLFG RYLYDTLQYP IGLVSSSWGG TYIEVWSSRR TLKACGVPNT 250 260 270 280 290 300 RDERVGQPEI KPMRNECNSE ESSCPFRVVP SVRVTGPTRH SVLWNAMIHP LQNMTLKGVV 310 320 330 340 350 360 WYQGESNADY NRDLYTCMFP ELIEDWRQTF HYGSQGQTDR FFPFGFVQVC IQRIHIQCLE 370 380 390 FMGLCGECGL CTCLYWDLQP NICPNSMSWR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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).
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00111794. IPI00459781. IPI00606747.
RefSeq	NP_035864.2. NM_011734.3.
UniGene	Mm.196345.
3D structure databases
ProteinModelPortal	P70665.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000002007.
PTM databases
PhosphoSite	P70665.
Proteomic databases
PaxDb	P70665.
PRIDE	P70665.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000002007; ENSMUSP00000002007; ENSMUSG00000001942.
GeneID	22619.
KEGG	mmu:22619.
UCSC	uc009ove.1. mouse. uc009ovf.1. mouse.
Organism-specific databases
CTD	54414.
MGI	MGI:104803. Siae.
Phylogenomic databases
eggNOG	NOG41492.
GeneTree	ENSGT00390000010608.
HOVERGEN	HBG007955.
InParanoid	P70665.
KO	K05970.
OMA	WLPASMN.
OrthoDB	EOG43R3MH.
Gene expression databases
ArrayExpress	P70665.
Bgee	P70665.
CleanEx	MM_SIAE.
Genevestigator	P70665.
GermOnline	ENSMUSG00000001942. Mus musculus.
Family and domain databases
InterPro	IPR005181. DUF303_acetylest. [Graphical view]
Pfam	PF03629. DUF303. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	302973.
SOURCE	Search...

Entry information

Entry name

SIAE_MOUSE

Accession

Primary (citable) accession number: P70665
Secondary accession number(s): Q3TNZ5 , Q544V7, Q61044, Q8C902, Q8CBM6, Q8CC41, Q8CEB7, Q922L0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 15, 2002
Last sequence update:	May 30, 2006
Last modified:	April 3, 2013
This is version 95 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program