ID   D3ZWB7_RAT              Unreviewed;       478 AA.
AC   D3ZWB7;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   RecName: Full=exo-alpha-sialidase {ECO:0000256|ARBA:ARBA00012733};
DE            EC=3.2.1.18 {ECO:0000256|ARBA:ARBA00012733};
GN   Name=Neu4 {ECO:0000313|Ensembl:ENSRNOP00000063883.1,
GN   ECO:0000313|RGD:1308624};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000063883.1, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000063883.1, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000063883.1,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0000313|Ensembl:ENSRNOP00000063883.1}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000063883.1};
RG   Ensembl;
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   RefSeq; NP_001101704.1; NM_001108234.1.
DR   RefSeq; XP_008765616.1; XM_008767394.2.
DR   AlphaFoldDB; D3ZWB7; -.
DR   SMR; D3ZWB7; -.
DR   STRING; 10116.ENSRNOP00000063883; -.
DR   PaxDb; 10116-ENSRNOP00000063883; -.
DR   Ensembl; ENSRNOT00000065533.3; ENSRNOP00000063883.1; ENSRNOG00000019031.7.
DR   GeneID; 316642; -.
DR   KEGG; rno:316642; -.
DR   UCSC; RGD:1308624; rat.
DR   AGR; RGD:1308624; -.
DR   CTD; 129807; -.
DR   RGD; 1308624; Neu4.
DR   eggNOG; ENOG502QSFT; Eukaryota.
DR   GeneTree; ENSGT00950000182944; -.
DR   HOGENOM; CLU_024620_2_1_1; -.
DR   OMA; NKPQGHC; -.
DR   OrthoDB; 5482010at2759; -.
DR   Reactome; R-RNO-4085001; Sialic acid metabolism.
DR   Reactome; R-RNO-9840310; Glycosphingolipid catabolism.
DR   Proteomes; UP000002494; Chromosome 9.
DR   Bgee; ENSRNOG00000019031; Expressed in brain and 3 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005764; C:lysosome; ISO:RGD.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0043005; C:neuron projection; ISO:RGD.
DR   GO; GO:0019866; C:organelle inner membrane; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0052794; F:exo-alpha-(2->3)-sialidase activity; ISO:RGD.
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; ISO:RGD.
DR   GO; GO:0004308; F:exo-alpha-sialidase activity; ISO:RGD.
DR   GO; GO:0006689; P:ganglioside catabolic process; ISO:RGD.
DR   GO; GO:0006516; P:glycoprotein catabolic process; ISO:RGD.
DR   GO; GO:0010977; P:negative regulation of neuron projection development; ISO:RGD.
DR   GO; GO:0009313; P:oligosaccharide catabolic process; ISO:RGD.
DR   CDD; cd15482; Sialidase_non-viral; 1.
DR   Gene3D; 2.120.10.10; -; 2.
DR   InterPro; IPR011040; Sialidase.
DR   InterPro; IPR026856; Sialidase_fam.
DR   InterPro; IPR036278; Sialidase_sf.
DR   PANTHER; PTHR10628; SIALIDASE; 1.
DR   PANTHER; PTHR10628:SF22; SIALIDASE-4; 1.
DR   Pfam; PF13088; BNR_2; 1.
DR   SUPFAM; SSF50939; Sialidases; 1.
PE   3: Inferred from homology;
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00022963};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          36..259
FT                   /note="Sialidase"
FT                   /evidence="ECO:0000259|Pfam:PF13088"
SQ   SEQUENCE   478 AA;  52045 MW;  E59549DCEDE1C69B CRC64;
     MGPAHVPKRT VLFQRERTGL TYRVPALLCV PPRPTLLAFA EQRLSPDDSH AHRLVLRRGT
     LTRGSVRWGV LSVLETAVLE EHRSMNPCPV LDEHSGTIFL FFIAVRGHTP EAVQIATGKN
     AARLCCVTSC DAGLTWGSVR DLTEEAIGAA LQDWATFAVG PGHGVQLRSG RLLVPAYTYH
     VDRRECFGRI CWTSPHSLAF YSDDHGISWH CGGLVPNLRS GECQLAAVDG DFLYCNARSP
     LGNRVQALSA DEGTSFLPGE LVPTLAETAR GCQGSIVGFP APPSIGPQDD RWLASPGNTP
     HSPCFDLRVR ESLAEGARGF VEGWASRLLL CYPQSRGPEN HGLEPGPDGE KTSWSPELPM
     SSASVRQSST WLLYSHPAGR RARLHMGIYL SRSPLDPHSW TEPWIIYEGP SGYSDLAFLG
     PVPGASLAFA CLFESGTRAS YEDISFCLFS LADVLENVPT GLEISSLRNK PQGHCWPS
//