NEUR4_MOUSE
ID NEUR4_MOUSE Reviewed; 478 AA.
AC Q8BZL1; Q6NS66;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 3.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Sialidase-4;
DE EC=3.2.1.18 {ECO:0000269|PubMed:19506080, ECO:0000269|PubMed:22393058};
DE AltName: Full=N-acetyl-alpha-neuraminidase 4;
DE AltName: Full=Neuraminidase 4;
GN Name=Neu4;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=14637003; DOI=10.1016/j.gene.2003.08.005;
RA Comelli E.M., Amado M., Lustig S.R., Paulson J.C.;
RT "Identification and expression of Neu4, a novel murine sialidase.";
RL Gene 321:155-161(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Diencephalon;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [4]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=19506080; DOI=10.1074/jbc.m109.012708;
RA Shiozaki K., Koseki K., Yamaguchi K., Shiozaki M., Narimatsu H., Miyagi T.;
RT "Developmental change of sialidase neu4 expression in murine brain and its
RT involvement in the regulation of neuronal cell differentiation.";
RL J. Biol. Chem. 284:21157-21164(2009).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=22393058; DOI=10.1074/jbc.m111.324186;
RA Takahashi K., Mitoma J., Hosono M., Shiozaki K., Sato C., Yamaguchi K.,
RA Kitajima K., Higashi H., Nitta K., Shima H., Miyagi T.;
RT "Sialidase NEU4 hydrolyzes polysialic acids of neural cell adhesion
RT molecules and negatively regulates neurite formation by hippocampal
RT neurons.";
RL J. Biol. Chem. 287:14816-14826(2012).
CC -!- FUNCTION: Exo-alpha-sialidase that catalyzes the hydrolytic cleavage of
CC the terminal sialic acid (N-acetylneuraminic acid, Neu5Ac) of a glycan
CC moiety in the catabolism of glycolipids, glycoproteins and
CC oligosacharides. Efficiently hydrolyzes gangliosides including alpha-
CC (2->3)-sialylated GD1a and GM3 and alpha-(2->8)-sialylated GD3
CC (PubMed:19506080, PubMed:22393058). Hydrolyzes poly-alpha-(2->8)-
CC sialylated neural cell adhesion molecule NCAM1 likely at growth cones,
CC suppressing neurite outgrowth in hippocampal neurons (PubMed:19506080,
CC PubMed:22393058). May desialylate sialyl Lewis A and X antigens at the
CC cell surface, down-regulating these glycan epitopes recognized by
CC SELE/E selectin in the initiation of cell adhesion and extravasation
CC (By similarity). Has sialidase activity toward mucin, fetuin and
CC sialyllactose (PubMed:19506080, PubMed:22393058).
CC {ECO:0000250|UniProtKB:Q8WWR8, ECO:0000269|PubMed:19506080,
CC ECO:0000269|PubMed:22393058}.
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:0000269|PubMed:19506080, ECO:0000269|PubMed:22393058};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ganglioside GM3 + H2O = beta-D-galactosyl-(1->4)-beta-D-
CC glucosyl-(1<->1)-ceramide + N-acetylneuraminate;
CC Xref=Rhea:RHEA:48136, ChEBI:CHEBI:15377, ChEBI:CHEBI:35418,
CC ChEBI:CHEBI:79208, ChEBI:CHEBI:79210;
CC Evidence={ECO:0000269|PubMed:19506080};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48137;
CC Evidence={ECO:0000305|PubMed:19506080};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ganglioside GM3 (d18:1(4E)) + H2O = a beta-D-Gal-(1->4)-beta-
CC D-Glc-(1<->1)-Cer(d18:1(4E)) + N-acetylneuraminate;
CC Xref=Rhea:RHEA:47900, ChEBI:CHEBI:15377, ChEBI:CHEBI:17950,
CC ChEBI:CHEBI:35418, ChEBI:CHEBI:60065;
CC Evidence={ECO:0000250|UniProtKB:Q8WWR8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47901;
CC Evidence={ECO:0000250|UniProtKB:Q8WWR8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ganglioside GM2 + H2O = N-acetyl-beta-D-galactosaminyl-(1->4)-
CC beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide + N-
CC acetylneuraminate; Xref=Rhea:RHEA:48172, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:35418, ChEBI:CHEBI:79218, ChEBI:CHEBI:90085;
CC Evidence={ECO:0000250|UniProtKB:Q8WWR8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48173;
CC Evidence={ECO:0000250|UniProtKB:Q8WWR8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ganglioside GM2 (d18:1(4E)) + H2O = ganglioside GA2
CC (d18:1(4E)) + N-acetylneuraminate; Xref=Rhea:RHEA:48068,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:27731, ChEBI:CHEBI:35418,
CC ChEBI:CHEBI:71502; Evidence={ECO:0000250|UniProtKB:Q8WWR8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48069;
CC Evidence={ECO:0000250|UniProtKB:Q8WWR8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ganglioside GD1a + H2O = ganglioside GM1 + N-
CC acetylneuraminate; Xref=Rhea:RHEA:47832, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:35418, ChEBI:CHEBI:82637, ChEBI:CHEBI:82639;
CC Evidence={ECO:0000250|UniProtKB:Q8WWR8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47833;
CC Evidence={ECO:0000250|UniProtKB:Q8WWR8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ganglioside GD1a (d18:1(4E)) + H2O = ganglioside GM1
CC (d18:1(4E)) + N-acetylneuraminate; Xref=Rhea:RHEA:47856,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:35418, ChEBI:CHEBI:77709,
CC ChEBI:CHEBI:78445; Evidence={ECO:0000250|UniProtKB:Q8WWR8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47857;
CC Evidence={ECO:0000250|UniProtKB:Q8WWR8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ganglioside GD3 + H2O = ganglioside GM3 + N-acetylneuraminate;
CC Xref=Rhea:RHEA:48120, ChEBI:CHEBI:15377, ChEBI:CHEBI:35418,
CC ChEBI:CHEBI:79210, ChEBI:CHEBI:79214;
CC Evidence={ECO:0000269|PubMed:19506080};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48121;
CC Evidence={ECO:0000305|PubMed:19506080};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ganglioside GD3 (d18:1(4E)) + H2O = ganglioside GM3
CC (d18:1(4E)) + N-acetylneuraminate; Xref=Rhea:RHEA:48124,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:35418, ChEBI:CHEBI:60065,
CC ChEBI:CHEBI:78436; Evidence={ECO:0000250|UniProtKB:Q8WWR8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48125;
CC Evidence={ECO:0000250|UniProtKB:Q8WWR8};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 4.4-6.5. {ECO:0000269|PubMed:22393058};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22393058};
CC Peripheral membrane protein. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q8WWR8}; Peripheral membrane protein. Microsome
CC membrane {ECO:0000250|UniProtKB:Q8WWR8}; Peripheral membrane protein.
CC Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q8WWR8}; Peripheral
CC membrane protein. Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:Q8WWR8}; Peripheral membrane protein. Cell
CC projection, neuron projection {ECO:0000269|PubMed:22393058}. Lysosome
CC lumen {ECO:0000250|UniProtKB:Q8WWR8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BZL1-2; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BZL1-1; Sequence=VSP_037492;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain, particularly in
CC hippocampus, and at lower levels in liver and spleen. Expressed in
CC hippocampal neurons (at protein level). {ECO:0000269|PubMed:14637003,
CC ECO:0000269|PubMed:19506080, ECO:0000269|PubMed:22393058}.
CC -!- DEVELOPMENTAL STAGE: Expressed at low levels in embryonic brain, then
CC rapidly up-regulated after birth reaching a maximum at postnatal day
CC 14, followed by a decrease. {ECO:0000269|PubMed:19506080}.
CC -!- INDUCTION: Down-regulated upon neuron differentiation.
CC {ECO:0000269|PubMed:22393058}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 33 family. {ECO:0000305}.
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DR EMBL; AY258421; AAP81169.1; -; mRNA.
DR EMBL; AK034236; BAC28641.1; -; mRNA.
DR EMBL; BC070438; AAH70438.1; -; mRNA.
DR CCDS; CCDS15199.1; -. [Q8BZL1-2]
DR CCDS; CCDS78660.1; -. [Q8BZL1-1]
DR RefSeq; NP_001297698.1; NM_001310769.1. [Q8BZL1-1]
DR RefSeq; NP_776133.1; NM_173772.3. [Q8BZL1-2]
DR AlphaFoldDB; Q8BZL1; -.
DR SMR; Q8BZL1; -.
DR STRING; 10090.ENSMUSP00000051151; -.
DR ChEMBL; CHEMBL4106170; -.
DR ChEMBL; CHEMBL4106181; -.
DR ChEMBL; CHEMBL4296071; -.
DR CAZy; GH33; Glycoside Hydrolase Family 33.
DR iPTMnet; Q8BZL1; -.
DR PhosphoSitePlus; Q8BZL1; -.
DR SwissPalm; Q8BZL1; -.
DR PaxDb; Q8BZL1; -.
DR PRIDE; Q8BZL1; -.
DR ProteomicsDB; 287391; -. [Q8BZL1-2]
DR ProteomicsDB; 287392; -. [Q8BZL1-1]
DR Antibodypedia; 34580; 172 antibodies from 25 providers.
DR DNASU; 241159; -.
DR Ensembl; ENSMUST00000050890; ENSMUSP00000051151; ENSMUSG00000034000. [Q8BZL1-2]
DR Ensembl; ENSMUST00000190212; ENSMUSP00000140127; ENSMUSG00000034000. [Q8BZL1-1]
DR GeneID; 241159; -.
DR KEGG; mmu:241159; -.
DR UCSC; uc007ceu.1; mouse. [Q8BZL1-2]
DR CTD; 129807; -.
DR MGI; MGI:2661364; Neu4.
DR VEuPathDB; HostDB:ENSMUSG00000034000; -.
DR eggNOG; ENOG502QSFT; Eukaryota.
DR GeneTree; ENSGT00950000182944; -.
DR HOGENOM; CLU_024620_2_1_1; -.
DR InParanoid; Q8BZL1; -.
DR TreeFam; TF331063; -.
DR Reactome; R-MMU-1660662; Glycosphingolipid metabolism.
DR Reactome; R-MMU-4085001; Sialic acid metabolism.
DR BioGRID-ORCS; 241159; 1 hit in 74 CRISPR screens.
DR PRO; PR:Q8BZL1; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8BZL1; protein.
DR Bgee; ENSMUSG00000034000; Expressed in striatum and 8 other tissues.
DR ExpressionAtlas; Q8BZL1; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0043202; C:lysosomal lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISO:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:0019866; C:organelle inner membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0052794; F:exo-alpha-(2->3)-sialidase activity; IDA: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; IDA:UniProtKB.
DR GO; GO:0004308; F:exo-alpha-sialidase activity; IDA:MGI.
DR GO; GO:0006689; P:ganglioside catabolic process; IDA:UniProtKB.
DR GO; GO:0006516; P:glycoprotein catabolic process; IDA:UniProtKB.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IDA:UniProtKB.
DR GO; GO:0009313; P:oligosaccharide catabolic process; ISS:UniProtKB.
DR InterPro; IPR011040; Sialidase.
DR InterPro; IPR026946; Sialidase-4.
DR InterPro; IPR026856; Sialidase_fam.
DR InterPro; IPR036278; Sialidase_sf.
DR PANTHER; PTHR10628; PTHR10628; 1.
DR PANTHER; PTHR10628:SF22; PTHR10628:SF22; 1.
DR Pfam; PF13088; BNR_2; 1.
DR SUPFAM; SSF50939; SSF50939; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Carbohydrate metabolism; Cell membrane;
KW Cell projection; Endoplasmic reticulum; Glycosidase; Hydrolase;
KW Lipid degradation; Lipid metabolism; Lysosome; Membrane; Microsome;
KW Mitochondrion; Mitochondrion inner membrane; Mitochondrion outer membrane;
KW Reference proteome; Repeat.
FT CHAIN 1..478
FT /note="Sialidase-4"
FT /id="PRO_0000208907"
FT REPEAT 127..138
FT /note="BNR 1"
FT REPEAT 200..211
FT /note="BNR 2"
FT REPEAT 247..258
FT /note="BNR 3"
FT REGION 285..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 22..25
FT /note="FRIP motif"
FT COMPBIAS 291..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 47
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 48
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 413
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 434
FT /evidence="ECO:0000255"
FT BINDING 23
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 43
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 179
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 222
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 238
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 383
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1
FT /note="M -> METAGAPFCFHVDSLVPCSYWKVM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14637003"
FT /id="VSP_037492"
SQ SEQUENCE 478 AA; 52426 MW; E1833F5DBFBFD08F CRC64;
MGPTRVPRRT VLFQRERTGL TYRVPALLCV PPRPTLLAFA EQRLSPDDSH AHRLVLRRGT
LTRGSVRWGT LSVLETAVLE EHRSMNPCPV LDEHSGTIFL FFIAVLGHTP EAVQIATGKN
AARLCCVTSC DAGLTWGSVR DLTEEAIGAA LQDWATFAVG PGHGVQLRSG RLLVPAYTYH
VDRRECFGKI CWTSPHSLAF YSDDHGISWH CGGLVPNLRS GECQLAAVDG DFLYCNARSP
LGNRVQALSA DEGTSFLPGE LVPTLAETAR GCQGSIVGFL APPSIEPQDD RWTGSPRNTP
HSPCFNLRVQ ESSGEGARGL LERWMPRLPL CYPQSRSPEN HGLEPGSDGD KTSWTPECPM
SSDSMLQSPT WLLYSHPAGR RARLHMGIYL SRSPLDPHSW TEPWVIYEGP SGYSDLAFLG
PMPGASLVFA CLFESGTRTS YEDISFCLFS LADVLENVPT GLEMLSLRDK AQGHCWPS
