ID A0JMM3_DANRE Unreviewed; 402 AA.
AC A0JMM3; A0A2R8RYF3; F6P776;
DT 12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT 12-DEC-2006, sequence version 1.
DT 27-MAR-2024, entry version 125.
DE RecName: Full=exo-alpha-sialidase {ECO:0000256|ARBA:ARBA00012733};
DE EC=3.2.1.18 {ECO:0000256|ARBA:ARBA00012733};
GN Name=neu3.3 {ECO:0000313|EMBL:AAI25932.1,
GN ECO:0000313|Ensembl:ENSDARP00000075627,
GN ECO:0000313|RefSeq:NP_001071006.1,
GN ECO:0000313|ZFIN:ZDB-GENE-061103-511};
GN Synonyms=neuc.1 {ECO:0000313|RefSeq:NP_001071006.1}, zgc:153998
GN {ECO:0000313|RefSeq:NP_001071006.1};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000313|EMBL:ABO30989.1};
RN [1] {ECO:0000313|EMBL:AAI25932.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=PCR rescue {ECO:0000313|EMBL:AAI64496.1}, and Whole
RC {ECO:0000313|EMBL:AAI25932.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABO30989.1, ECO:0000313|RefSeq:NP_001071006.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=17708749; DOI=10.1042/BJ20070627;
RA Manzoni M., Colombi P., Papini N., Rubaga L., Tiso N., Preti A.,
RA Venerando B., Tettamanti G., Bresciani R., Argenton F., Borsani G.,
RA Monti E.;
RT "Molecular cloning and biochemical characterization of sialidases from
RT zebrafish (Danio rerio).";
RL Biochem. J. 408:395-406(2007).
RN [3] {ECO:0000313|Ensembl:ENSDARP00000075627}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000075627};
RG Ensembl;
RL Submitted (FEB-2012) to UniProtKB.
RN [4] {ECO:0000313|RefSeq:NP_001071006.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23032629; DOI=10.1016/j.biochi.2012.09.026;
RA Shiozaki K., Takeshita K., Ikeda M., Ikeda A., Harasaki Y., Komatsu M.,
RA Yamada S., Yamaguchi K., Miyagi T.;
RT "Molecular cloning and biochemical characterization of two novel Neu3
RT sialidases, neu3a and neu3b, from medaka (Oryzias latipes).";
RL Biochimie 95:280-289(2013).
RN [5] {ECO:0000313|Ensembl:ENSDARP00000075627, ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000075627};
RX PubMed=23594743; DOI=10.1038/nature12111;
RG Genome Reference Consortium Zebrafish;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [6] {ECO:0000313|RefSeq:NP_001071006.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=27189481;
RA Pasquier J., Cabau C., Nguyen T., Jouanno E., Severac D., Braasch I.,
RA Journot L., Pontarotti P., Klopp C., Postlethwait J.H., Guiguen Y.,
RA Bobe J.;
RT "Gene evolution and gene expression after whole genome duplication in fish:
RT the PhyloFish database.";
RL BMC Genomics 17:368-368(2016).
RN [7] {ECO:0000313|RefSeq:NP_001071006.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=29175743;
RA Teng M., Zhu W., Wang D., Qi S., Wang Y., Yan J., Dong K., Zheng M.,
RA Wang C.;
RT "Metabolomics and transcriptomics reveal the toxicity of difenoconazole to
RT the early life stages of zebrafish (Danio rerio).";
RL Aquat. Toxicol. 194:112-120(2018).
RN [8] {ECO:0000313|RefSeq:NP_001071006.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=30405127;
RA Yamakawa N., Vanbeselaere J., Chang L.Y., Yu S.Y., Ducrocq L.,
RA Harduin-Lepers A., Kurata J., Aoki-Kinoshita K.F., Sato C., Khoo K.H.,
RA Kitajima K., Guerardel Y.;
RT "Systems glycomics of adult zebrafish identifies organ-specific sialylation
RT and glycosylation patterns.";
RL Nat. Commun. 9:4647-4647(2018).
RN [9] {ECO:0000313|Ensembl:ENSDARP00000148301}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000148301};
RG Ensembl;
RL Submitted (APR-2018) to UniProtKB.
RN [10] {ECO:0000313|RefSeq:NP_001071006.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-
CC (2->8)- glycosidic linkages of terminal sialic acid residues in
CC oligosaccharides, glycoproteins, glycolipids, colominic acid and
CC synthetic substrates.; EC=3.2.1.18;
CC Evidence={ECO:0000256|ARBA:ARBA00000427};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 33 family.
CC {ECO:0000256|ARBA:ARBA00009348}.
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DR EMBL; CU928016; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC125931; AAI25932.1; -; mRNA.
DR EMBL; BC164496; AAI64496.1; -; mRNA.
DR EMBL; EF107698; ABO30989.1; -; mRNA.
DR RefSeq; NP_001071006.1; NM_001077538.1.
DR RefSeq; XP_017208270.1; XM_017352781.1.
DR STRING; 7955.ENSDARP00000075627; -.
DR CAZy; GH33; Glycoside Hydrolase Family 33.
DR PaxDb; 7955-ENSDARP00000075627; -.
DR Ensembl; ENSDART00000081184.6; ENSDARP00000075627.5; ENSDARG00000058327.7.
DR Ensembl; ENSDART00000084600.6; ENSDARP00000079035.4; ENSDARG00000058327.7.
DR Ensembl; ENSDART00000180444.1; ENSDARP00000148301.1; ENSDARG00000114607.1.
DR Ensembl; ENSDART00000184899.1; ENSDARP00000155965.1; ENSDARG00000058327.7.
DR GeneID; 555206; -.
DR KEGG; dre:555206; -.
DR AGR; ZFIN:ZDB-GENE-061103-511; -.
DR CTD; 555206; -.
DR ZFIN; ZDB-GENE-061103-511; neu3.3.
DR eggNOG; ENOG502QSFT; Eukaryota.
DR HOGENOM; CLU_024620_2_1_1; -.
DR OMA; SEASIEC; -.
DR OrthoDB; 5482010at2759; -.
DR TreeFam; TF331063; -.
DR Proteomes; UP000000437; Alternate scaffold 21.
DR Proteomes; UP000000437; Chromosome 21.
DR Bgee; ENSDARG00000058327; Expressed in intestine and 13 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:ZFIN.
DR GO; GO:0052794; F:exo-alpha-(2->3)-sialidase activity; IEA:UniProtKB-EC.
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; IEA:UniProtKB-EC.
DR GO; GO:0004308; F:exo-alpha-sialidase activity; IDA:ZFIN.
DR GO; GO:0006689; P:ganglioside catabolic process; IBA:GO_Central.
DR GO; GO:0001573; P:ganglioside metabolic process; IDA:ZFIN.
DR GO; GO:0009313; P:oligosaccharide catabolic process; IBA:GO_Central.
DR CDD; cd15482; Sialidase_non-viral; 1.
DR Gene3D; 2.120.10.10; -; 1.
DR InterPro; IPR011040; Sialidase.
DR InterPro; IPR026856; Sialidase_fam.
DR InterPro; IPR036278; Sialidase_sf.
DR PANTHER; PTHR10628; SIALIDASE; 1.
DR PANTHER; PTHR10628:SF23; SIALIDASE-3; 1.
DR Pfam; PF13088; BNR_2; 1.
DR SUPFAM; SSF50939; Sialidases; 1.
PE 1: Evidence at protein level;
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022963};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0JMM3};
KW Reference proteome {ECO:0000313|Proteomes:UP000000437}.
FT DOMAIN 54..375
FT /note="Sialidase"
FT /evidence="ECO:0000259|Pfam:PF13088"
SQ SEQUENCE 402 AA; 45094 MW; AF2867F30357419E CRC64;
MGNKTPSKSK SGYPKEMNTT TVFKQEQPQT WCCCFKKQVS YRIPALVYVS DEQTFLAFAE
KRKTLNDTNA EVLVMRRGTW VDAKTKEVEW ICGHQVLSSA SLPNHRSMNP CPVYERDSKT
LFLFFVCVPT QVSEFDQIRT NKSQGRLCYV TSKDAGKTWS QTIDLTADVI GEQVNEWAPF
AVGPGHGVQT KNGRLIIPAY AYRYTGKTDC TSCCCLSFCC FTPYALAFYS DDQGITWKAG
QQMDVESCEC QMAEIVGEKG DSTLYCNART RLGYRTEALS NNAGEDFDTV LSSSKLIETG
KGCQGSVLSF VEQSSPPQTW LLYSHPSHPK KRVDLGLYLN KSPLDSSGWS DEPLMILHHG
PSAYSDLVEF EPGHFACLME CGKEHENEEI AFLLFKLPEK KL
//
