ID   H3HXK0_STRPU            Unreviewed;       380 AA.
AC   H3HXK0;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=Sialidase-1 {ECO:0000256|ARBA:ARBA00040509};
DE   AltName: Full=Lysosomal sialidase {ECO:0000256|ARBA:ARBA00041413};
DE   AltName: Full=N-acetyl-alpha-neuraminidase 1 {ECO:0000256|ARBA:ARBA00041332};
DE   Flags: Fragment;
OS   Strongylocentrotus purpuratus (Purple sea urchin).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC   Euechinoidea; Echinacea; Camarodonta; Echinidea; Strongylocentrotidae;
OC   Strongylocentrotus.
OX   NCBI_TaxID=7668 {ECO:0000313|EMBL:DAA35227.1};
RN   [1] {ECO:0000313|EMBL:DAA35227.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=10191093; DOI=10.1006/geno.1999.5749;
RA   Monti E., Preti A., Rossi E., Ballabio A., Borsani G.;
RT   "Cloning and characterization of NEU2, a human gene homologous to rodent
RT   soluble sialidases.";
RL   Genomics 57:137-143(1999).
RN   [2] {ECO:0000313|EMBL:DAA35227.1}
RP   NUCLEOTIDE SEQUENCE.
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 associated
RT   to the plasma membrane.";
RL   Biochem. J. 349:343-351(2000).
RN   [3] {ECO:0000313|EMBL:DAA35227.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=14962670; DOI=10.1016/j.ygeno.2003.08.019;
RA   Monti E., Bassi M.T., Bresciani R., Civini S., Croci G.L., Papini N.,
RA   Riboni M., Zanchetti G., Ballabio A., Preti A., Tettamanti G.,
RA   Venerando B., Borsani G.;
RT   "Molecular cloning and characterization of NEU4, the fourth member of the
RT   human sialidase gene family.";
RL   Genomics 83:445-453(2004).
RN   [4] {ECO:0000313|EMBL:DAA35227.1}
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   [5] {ECO:0000313|EMBL:DAA35227.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=21861893; DOI=10.1186/1471-2091-12-45;
RA   Giacopuzzi E., Barlati S., Preti A., Venerando B., Monti E., Borsani G.,
RA   Bresciani R.;
RT   "Gallus gallus NEU3 sialidase as model to study protein evolution mechanism
RT   based on rapid evolving loops.";
RL   BMC Biochem. 12:45-45(2011).
RN   [6] {ECO:0000313|EMBL:DAA35227.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=22952925; DOI=10.1371/journal.pone.0044193;
RA   Giacopuzzi E., Bresciani R., Schauer R., Monti E., Borsani G.;
RT   "New insights on the sialidase protein family revealed by a phylogenetic
RT   analysis in metazoa.";
RL   PLoS ONE 7:E44193-E44193(2012).
CC   -!- FUNCTION: Catalyzes the removal of sialic acid (N-acetylneuraminic
CC       acid) moieties from glycoproteins and glycolipids. To be active, it is
CC       strictly dependent on its presence in the multienzyme complex. Appears
CC       to have a preference for alpha 2-3 and alpha 2-6 sialyl linkage.
CC       {ECO:0000256|ARBA:ARBA00037235}.
CC   -!- SUBUNIT: Interacts with cathepsin A (protective protein), beta-
CC       galactosidase and N-acetylgalactosamine-6-sulfate sulfatase in a
CC       multienzyme complex. {ECO:0000256|ARBA:ARBA00038519}.
CC   -!- SUBCELLULAR LOCATION: Lysosome membrane
CC       {ECO:0000256|ARBA:ARBA00004207}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004207}; Lumenal side
CC       {ECO:0000256|ARBA:ARBA00004207}.
CC   -!- MISCELLANEOUS: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ third party annotation (TPA) entry.
CC       {ECO:0000313|EMBL:DAA35227.1}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 33 family.
CC       {ECO:0000256|ARBA:ARBA00009348}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BK008540; DAA35227.1; -; mRNA.
DR   RefSeq; XP_003724953.2; XM_003724905.2.
DR   AlphaFoldDB; H3HXK0; -.
DR   STRING; 7668.H3HXK0; -.
DR   GeneID; 100890097; -.
DR   KEGG; spu:100890097; -.
DR   eggNOG; ENOG502QSIT; Eukaryota.
DR   HOGENOM; CLU_024620_3_0_1; -.
DR   OrthoDB; 5388454at2759; -.
DR   PhylomeDB; H3HXK0; -.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004308; F:exo-alpha-sialidase activity; IEA:InterPro.
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:SF25; SIALIDASE-1; 1.
DR   Pfam; PF13088; BNR_2; 1.
DR   SUPFAM; SSF50939; Sialidases; 1.
PE   2: Evidence at transcript level;
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          58..352
FT                   /note="Sialidase"
FT                   /evidence="ECO:0000259|Pfam:PF13088"
FT   NON_TER         380
FT                   /evidence="ECO:0000313|EMBL:DAA35227.1"
SQ   SEQUENCE   380 AA;  41869 MW;  97E76FDB6B6A905C CRC64;
     MAKLTVQQSL LLTISSILVS VTYSINPFVL EEQLIWESSD EGEVSTYRIP IIIQVPNGDL
     LAFSEARKYS AADAGAKFIA MRRSSNGGQS WGENTFILND YKIPDGLNLG TVLVDSVTNS
     TILIHTFCVH SVCNGTGEKP SGVFMVTSSN FGYTWSDPVN LAEKNPELMD LHFDPGPGYG
     IQKKHPPHKG RLVTCGHGPD AEVRSMYCLH SDDGGITWHL SLGLAGLPFA ETKKTGDFVP
     GEVQIVELKN GTILANVRNT YSFHCNCRIQ ALSFDGGSTF PMTSMRMKQE LIDPNVCGSL
     LNFNDNQILF FSNPFNAGSR VNLTLHWSLD AGNTYPNLMN IYEKGSAYSC LTYIDENHIG
     LVYEKDNISS ISYVRIQLNL
//