SIAS_MOUSE
ID SIAS_MOUSE Reviewed; 359 AA.
AC Q99J77; Q9JJH0;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Sialic acid synthase {ECO:0000305|PubMed:10873658};
DE AltName: Full=N-acetylneuraminate-9-phosphate synthase {ECO:0000303|PubMed:10873658};
DE EC=2.5.1.57 {ECO:0000269|PubMed:10873658};
DE AltName: Full=N-acetylneuraminic acid phosphate synthase {ECO:0000303|PubMed:10873658};
GN Name=Nans {ECO:0000312|MGI:MGI:2149820};
GN Synonyms=Sas {ECO:0000312|MGI:MGI:2149820};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000312|Proteomes:UP000000589};
RN [1] {ECO:0000312|EMBL:BAA98131.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10873658; DOI=10.1006/bbrc.2000.2983;
RA Nakata D., Close B.E., Colley K.J., Matsuda T., Kitajima K.;
RT "Molecular cloning and expression of the mouse N-acetylneuraminic acid 9-
RT phosphate synthase which does not have deaminoneuraminic acid (KDN) 9-
RT phosphate synthase activity.";
RL Biochem. Biophys. Res. Commun. 273:642-648(2000).
RN [2] {ECO:0000312|EMBL:BAC36290.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC36290.1}, and
RC NOD {ECO:0000312|EMBL:BAE33642.1};
RC TISSUE=Skin {ECO:0000312|EMBL:BAC36290.1}, and
RC Spleen {ECO:0000312|EMBL:BAE33642.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4] {ECO:0000312|EMBL:EDL02367.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000312|EMBL:AAH03307.1, ECO:0000312|EMBL:AAH57977.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH57977.1};
RC TISSUE=Liver {ECO:0000312|EMBL:AAH57977.1}, and
RC Mammary tumor {ECO:0000312|EMBL:AAH03307.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-61; LYS-74; LYS-79 AND LYS-290,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Produces N-acetylneuraminate-9-phosphate (Neu5Ac-9-P) from N-
CC acetylmannosamine 6-phosphate. Has no detectable activity towards N-
CC acetylmannosamine or mannose 6-phosphate.
CC {ECO:0000269|PubMed:10873658}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acyl-D-mannosamine 6-phosphate + H2O +
CC phosphoenolpyruvate = an N-acylneuraminate 9-phosphate + phosphate;
CC Xref=Rhea:RHEA:13421, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57537, ChEBI:CHEBI:57666, ChEBI:CHEBI:58702; EC=2.5.1.57;
CC Evidence={ECO:0000269|PubMed:10873658};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10873658}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10873658}.
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DR EMBL; AB041263; BAA98131.1; -; mRNA.
DR EMBL; AK076290; BAC36290.1; -; mRNA.
DR EMBL; AK156254; BAE33642.1; -; mRNA.
DR EMBL; AL683884; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466565; EDL02367.1; -; Genomic_DNA.
DR EMBL; BC003307; AAH03307.1; -; mRNA.
DR EMBL; BC057977; AAH57977.1; -; mRNA.
DR CCDS; CCDS18152.1; -.
DR PIR; JC7321; JC7321.
DR RefSeq; NP_444409.1; NM_053179.3.
DR AlphaFoldDB; Q99J77; -.
DR SMR; Q99J77; -.
DR IntAct; Q99J77; 1.
DR STRING; 10090.ENSMUSP00000030018; -.
DR iPTMnet; Q99J77; -.
DR PhosphoSitePlus; Q99J77; -.
DR SwissPalm; Q99J77; -.
DR EPD; Q99J77; -.
DR jPOST; Q99J77; -.
DR MaxQB; Q99J77; -.
DR PaxDb; Q99J77; -.
DR PeptideAtlas; Q99J77; -.
DR PRIDE; Q99J77; -.
DR ProteomicsDB; 261038; -.
DR Antibodypedia; 14440; 226 antibodies from 26 providers.
DR DNASU; 94181; -.
DR Ensembl; ENSMUST00000030018; ENSMUSP00000030018; ENSMUSG00000028334.
DR GeneID; 94181; -.
DR KEGG; mmu:94181; -.
DR UCSC; uc008stv.1; mouse.
DR CTD; 54187; -.
DR MGI; MGI:2149820; Nans.
DR VEuPathDB; HostDB:ENSMUSG00000028334; -.
DR eggNOG; ENOG502QR5J; Eukaryota.
DR GeneTree; ENSGT00390000011081; -.
DR HOGENOM; CLU_040465_1_0_1; -.
DR InParanoid; Q99J77; -.
DR OMA; YRHRVEF; -.
DR OrthoDB; 1117607at2759; -.
DR PhylomeDB; Q99J77; -.
DR TreeFam; TF324826; -.
DR BioCyc; MetaCyc:MON-14514; -.
DR BRENDA; 2.5.1.57; 3474.
DR Reactome; R-MMU-4085001; Sialic acid metabolism.
DR BioGRID-ORCS; 94181; 11 hits in 76 CRISPR screens.
DR ChiTaRS; Nans; mouse.
DR PRO; PR:Q99J77; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q99J77; protein.
DR Bgee; ENSMUSG00000028334; Expressed in left colon and 282 other tissues.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0047444; F:N-acylneuraminate-9-phosphate synthase activity; IDA:MGI.
DR GO; GO:0016051; P:carbohydrate biosynthetic process; IEA:InterPro.
DR GO; GO:0070085; P:glycosylation; IBA:GO_Central.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR006190; AFP_Neu5c_C.
DR InterPro; IPR036732; AFP_Neu5c_C_sf.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR006013; Antifreeze_III.
DR InterPro; IPR013132; Neu5Ac_N.
DR InterPro; IPR013974; SAF.
DR Pfam; PF03102; NeuB; 1.
DR Pfam; PF08666; SAF; 1.
DR PRINTS; PR00357; ANTIFREEZIII.
DR SMART; SM00858; SAF; 1.
DR SUPFAM; SSF51269; SSF51269; 1.
DR PROSITE; PS50844; AFP_LIKE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..359
FT /note="Sialic acid synthase"
FT /evidence="ECO:0000250|UniProtKB:Q9NR45"
FT /id="PRO_0000438681"
FT DOMAIN 294..353
FT /note="AFP-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00021"
FT MOD_RES 61
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 74
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 79
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 290
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CONFLICT 311
FT /note="M -> T (in Ref. 1; BAA98131)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 359 AA; 40024 MW; 4C66CB883558A373 CRC64;
MPLELELCPG RWVGGKHPCF IIAEIGQNHQ GDIDVAKRMI RTAKECGADC AKFQKSELEF
KFNRKALERP YTSKHSWGKT YGEHKRHLEF SHDQYKELQS YAQEIGIFFT ASGMDEMAVE
FLHELNVPFF KVGSGDTNNF PYLEKTAKKG RPMVISSGMQ SMDTMKQVYQ IVKPLNPNFC
FLQCTSAYPL QPEDANLRVI SEYQKLFPDI PIGYSGHETG IAISVAAVAL GAKVLERHIT
LDKTWKGSDH SASLEPGELA ELVRSVRLVE RALGSPTKQL LPCEMACNEK LGKSVVAKVK
IPAGTTLTLD MLTVKVGEPK GYPPEDIFNL AGKKVLVTIE EDDTVMEESV ESHSKKIKA
