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Database: UniProt/SWISS-PROT
Entry: NEUR3_HUMAN
LinkDB: NEUR3_HUMAN
Original site: NEUR3_HUMAN 
ID   NEUR3_HUMAN             Reviewed;         428 AA.
AC   Q9UQ49; A8K327; Q9NQE1;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   18-JUL-2018, entry version 143.
DE   RecName: Full=Sialidase-3;
DE            EC=3.2.1.18;
DE   AltName: Full=Ganglioside sialidase;
DE   AltName: Full=Membrane sialidase;
DE   AltName: Full=N-acetyl-alpha-neuraminidase 3;
GN   Name=NEU3;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=10405317; DOI=10.1006/bbrc.1999.0973;
RA   Wada T., Yoshikawa Y., Tokuyama S., Kuwabara M., Akita H., Miyagi T.;
RT   "Cloning, expression, and chromosomal mapping of a human ganglioside
RT   sialidase.";
RL   Biochem. Biophys. Res. Commun. 261:21-27(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP   TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Skeletal muscle;
RX   PubMed=10861246; DOI=10.1042/0264-6021:3490343;
RA   Monti E., Bassi M.T., Papini N., Riboni M., Manzoni M., Venerando B.,
RA   Croci G., Preti A., Ballabio A., Tettamanti G., Borsani G.;
RT   "Identification and expression of NEU3, a novel human sialidase
RT   associated to the plasma membrane.";
RL   Biochem. J. 349:343-351(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Mammary gland;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA   Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA   FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA   Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA   Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA   Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Testis;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT   the kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, BINDING SITES, AND
RP   MUTAGENESIS OF ARG-45; ASP-50; TYR-179; TYR-181; GLU-225; ARG-245;
RP   ARG-340 AND TYR-370.
RX   PubMed=20511247; DOI=10.1093/glycob/cwq077;
RA   Albohy A., Li M.D., Zheng R.B., Zou C., Cairo C.W.;
RT   "Insight into substrate recognition and catalysis by the human
RT   neuraminidase 3 (NEU3) through molecular modeling and site-directed
RT   mutagenesis.";
RL   Glycobiology 20:1127-1138(2010).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
CC   -!- FUNCTION: Plays a role in modulating the ganglioside content of
CC       the lipid bilayer at the level of membrane-bound sialyl
CC       glycoconjugates. {ECO:0000269|PubMed:10861246,
CC       ECO:0000269|PubMed:20511247}.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of alpha-(2->3)-, alpha-(2->6)-,
CC       alpha-(2->8)- glycosidic linkages of terminal sialic acid residues
CC       in oligosaccharides, glycoproteins, glycolipids, colominic acid
CC       and synthetic substrates. {ECO:0000269|PubMed:10861246,
CC       ECO:0000269|PubMed:20511247}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 3.8.;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10861246};
CC       Peripheral membrane protein {ECO:0000269|PubMed:10861246}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9UQ49-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9UQ49-2; Sequence=VSP_054145;
CC   -!- TISSUE SPECIFICITY: Highly expressed in skeletal muscle, testis,
CC       adrenal gland and thymus, followed by pancreas, liver, heart and
CC       thymus. Weakly expressed in kidney, placenta, brain and lung.
CC       {ECO:0000269|PubMed:10861246}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 33 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB96131.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/NEU3ID44505ch11q13.html";
DR   EMBL; AB008185; BAA82611.1; -; mRNA.
DR   EMBL; Y18563; CAB96131.1; ALT_INIT; mRNA.
DR   EMBL; AK022450; BAG51074.1; -; mRNA.
DR   EMBL; AK290442; BAF83131.1; -; mRNA.
DR   EMBL; AP001992; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471076; EAW74953.1; -; Genomic_DNA.
DR   EMBL; BC136397; AAI36398.1; -; mRNA.
DR   EMBL; BC144059; AAI44060.1; -; mRNA.
DR   CCDS; CCDS44682.1; -. [Q9UQ49-2]
DR   RefSeq; NP_006647.3; NM_006656.5. [Q9UQ49-2]
DR   UniGene; Hs.191074; -.
DR   ProteinModelPortal; Q9UQ49; -.
DR   SMR; Q9UQ49; -.
DR   BioGrid; 116038; 7.
DR   STRING; 9606.ENSP00000294064; -.
DR   BindingDB; Q9UQ49; -.
DR   ChEMBL; CHEMBL3046; -.
DR   SwissLipids; SLP:000001372; -. [Q9UQ49-1]
DR   CAZy; GH33; Glycoside Hydrolase Family 33.
DR   iPTMnet; Q9UQ49; -.
DR   PhosphoSitePlus; Q9UQ49; -.
DR   SwissPalm; Q9UQ49; -.
DR   DMDM; 17369720; -.
DR   EPD; Q9UQ49; -.
DR   PaxDb; Q9UQ49; -.
DR   PeptideAtlas; Q9UQ49; -.
DR   PRIDE; Q9UQ49; -.
DR   ProteomicsDB; 85507; -.
DR   Ensembl; ENST00000294064; ENSP00000294064; ENSG00000162139. [Q9UQ49-2]
DR   Ensembl; ENST00000531509; ENSP00000432097; ENSG00000162139. [Q9UQ49-2]
DR   GeneID; 10825; -.
DR   KEGG; hsa:10825; -.
DR   UCSC; uc001ovw.4; human. [Q9UQ49-1]
DR   CTD; 10825; -.
DR   DisGeNET; 10825; -.
DR   EuPathDB; HostDB:ENSG00000162139.9; -.
DR   GeneCards; NEU3; -.
DR   HGNC; HGNC:7760; NEU3.
DR   HPA; HPA038729; -.
DR   HPA; HPA038730; -.
DR   HPA; HPA070381; -.
DR   MIM; 604617; gene.
DR   neXtProt; NX_Q9UQ49; -.
DR   OpenTargets; ENSG00000162139; -.
DR   PharmGKB; PA31562; -.
DR   eggNOG; ENOG410IFVF; Eukaryota.
DR   eggNOG; ENOG410Y74Z; LUCA.
DR   GeneTree; ENSGT00390000011171; -.
DR   HOGENOM; HOG000233778; -.
DR   HOVERGEN; HBG052608; -.
DR   InParanoid; Q9UQ49; -.
DR   KO; K12357; -.
DR   OMA; HSLMIYS; -.
DR   OrthoDB; EOG091G08BI; -.
DR   PhylomeDB; Q9UQ49; -.
DR   BRENDA; 3.2.1.18; 2681.
DR   Reactome; R-HSA-1660662; Glycosphingolipid metabolism.
DR   Reactome; R-HSA-4085001; Sialic acid metabolism.
DR   SABIO-RK; Q9UQ49; -.
DR   GeneWiki; NEU3; -.
DR   GenomeRNAi; 10825; -.
DR   PRO; PR:Q9UQ49; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   Bgee; ENSG00000162139; -.
DR   CleanEx; HS_NEU3; -.
DR   ExpressionAtlas; Q9UQ49; baseline and differential.
DR   Genevisible; Q9UQ49; HS.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0016997; F:alpha-sialidase activity; IDA:MGI.
DR   GO; GO:0052794; F:exo-alpha-(2->3)-sialidase activity; ISS:UniProtKB.
DR   GO; GO:0052795; F:exo-alpha-(2->6)-sialidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052796; F:exo-alpha-(2->8)-sialidase activity; ISS:UniProtKB.
DR   GO; GO:0004308; F:exo-alpha-sialidase activity; IDA:UniProtKB.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IDA:MGI.
DR   GO; GO:0006689; P:ganglioside catabolic process; IDA:UniProtKB.
DR   GO; GO:0006687; P:glycosphingolipid metabolic process; TAS:Reactome.
DR   GO; GO:0009313; P:oligosaccharide catabolic process; IDA:UniProtKB.
DR   InterPro; IPR011040; Sialidase.
DR   InterPro; IPR026944; Sialidase-3.
DR   InterPro; IPR026856; Sialidase_fam.
DR   InterPro; IPR036278; Sialidase_sf.
DR   PANTHER; PTHR10628; PTHR10628; 1.
DR   PANTHER; PTHR10628:SF23; PTHR10628:SF23; 1.
DR   Pfam; PF13088; BNR_2; 1.
DR   SUPFAM; SSF50939; SSF50939; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Carbohydrate metabolism; Cell membrane;
KW   Complete proteome; Glycosidase; Hydrolase; Lipid degradation;
KW   Lipid metabolism; Membrane; Phosphoprotein; Polymorphism;
KW   Reference proteome; Repeat.
FT   CHAIN         1    428       Sialidase-3.
FT                                /FTId=PRO_0000208903.
FT   REPEAT      129    140       BNR 1.
FT   REPEAT      203    214       BNR 2.
FT   REPEAT      254    265       BNR 3.
FT   MOTIF        24     27       FRIP motif.
FT   ACT_SITE     50     50       Proton acceptor.
FT                                {ECO:0000269|PubMed:20511247}.
FT   ACT_SITE    370    370       Nucleophile.
FT                                {ECO:0000269|PubMed:20511247}.
FT   ACT_SITE    387    387       {ECO:0000255}.
FT   BINDING      25     25       Substrate. {ECO:0000250}.
FT   BINDING      45     45       Substrate. {ECO:0000305}.
FT   BINDING     179    179       Substrate. {ECO:0000305}.
FT   BINDING     181    181       Substrate. {ECO:0000305}.
FT   BINDING     225    225       Substrate. {ECO:0000305}.
FT   BINDING     245    245       Substrate. {ECO:0000305}.
FT   BINDING     340    340       Substrate. {ECO:0000305}.
FT   MOD_RES     313    313       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9JMH7}.
FT   VAR_SEQ       1      1       M -> MRPADLPPRPMEESPASSSAPTETEEPGSSAEVM
FT                                (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039,
FT                                ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_054145.
FT   VARIANT      15     15       R -> Q (in dbSNP:rs7115499).
FT                                /FTId=VAR_055839.
FT   MUTAGEN      45     45       R->V: Loss of enzyme activity.
FT                                {ECO:0000269|PubMed:20511247}.
FT   MUTAGEN      50     50       D->S: Nearly abolishes enzyme activity.
FT                                {ECO:0000269|PubMed:20511247}.
FT   MUTAGEN     179    179       Y->F: Loss of enzyme activity.
FT                                {ECO:0000269|PubMed:20511247}.
FT   MUTAGEN     181    181       Y->F: Nearly abolishes enzyme activity.
FT                                {ECO:0000269|PubMed:20511247}.
FT   MUTAGEN     225    225       E->S: Loss of enzyme activity.
FT                                {ECO:0000269|PubMed:20511247}.
FT   MUTAGEN     245    245       R->A: Loss of enzyme activity.
FT                                {ECO:0000269|PubMed:20511247}.
FT   MUTAGEN     340    340       R->A: Loss of enzyme activity.
FT                                {ECO:0000269|PubMed:20511247}.
FT   MUTAGEN     370    370       Y->F: Loss of enzyme activity.
FT                                {ECO:0000269|PubMed:20511247}.
SQ   SEQUENCE   428 AA;  48252 MW;  35D1DD9359A78C98 CRC64;
     MEEVTTCSFN SPLFRQEDDR GITYRIPALL YIPPTHTFLA FAEKRSTRRD EDALHLVLRR
     GLRIGQLVQW GPLKPLMEAT LPGHRTMNPC PVWEQKSGCV FLFFICVRGH VTERQQIVSG
     RNAARLCFIY SQDAGCSWSE VRDLTEEVIG SELKHWATFA VGPGHGIQLQ SGRLVIPAYT
     YYIPSWFFCF QLPCKTRPHS LMIYSDDLGV TWHHGRLIRP MVTVECEVAE VTGRAGHPVL
     YCSARTPNRC RAEALSTDHG EGFQRLALSR QLCEPPHGCQ GSVVSFRPLE IPHRCQDSSS
     KDAPTIQQSS PGSSLRLEEE AGTPSESWLL YSHPTSRKQR VDLGIYLNQT PLEAACWSRP
     WILHCGPCGY SDLAALEEEG LFGCLFECGT KQECEQIAFR LFTHREILSH LQGDCTSPGR
     NPSQFKSN
//
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