ID H3A6I4_LATCH Unreviewed; 339 AA.
AC H3A6I4;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=exo-alpha-sialidase {ECO:0000256|ARBA:ARBA00012733};
DE EC=3.2.1.18 {ECO:0000256|ARBA:ARBA00012733};
GN Name=NEU3 {ECO:0000313|Ensembl:ENSLACP00000005255.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000005255.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000005255.1}
RP IDENTIFICATION.
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 EMBL; AFYH01238929; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H3A6I4; -.
DR STRING; 7897.ENSLACP00000005255; -.
DR Ensembl; ENSLACT00000005302.1; ENSLACP00000005255.1; ENSLACG00000004669.1.
DR eggNOG; ENOG502QSFT; Eukaryota.
DR GeneTree; ENSGT00950000182944; -.
DR HOGENOM; CLU_024620_2_1_1; -.
DR InParanoid; H3A6I4; -.
DR OMA; IEMQPAK; -.
DR TreeFam; TF331063; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
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:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022963};
KW Reference proteome {ECO:0000313|Proteomes:UP000008672}.
FT DOMAIN 1..288
FT /note="Sialidase"
FT /evidence="ECO:0000259|Pfam:PF13088"
SQ SEQUENCE 339 AA; 37522 MW; FB81B8AA23356619 CRC64;
MNPCPVYEQG KGILFLFFIC VRGKTSECWQ IFTGRNVARL CCVSSQDGGE TWSELTDLTE
GVIGEQVRRW ATFAVGPGHG IQLQSGRLII PAYAYFVRCR LCCLPLPWLT KPHAFTFYSD
DRGESWHVGK IIRKLKTVEC EVAEIEGQGS ERILYCNART SQGHRAEAIS KDAGLDFEKA
NLCQQLVEPP HGCQGSVVSF AAPKRSLQLE GGSTRDGKEA LLLPDWTNCS SVDGSVNRVW
LVYSHPTSRK ERVDLGTFLN QSPGGASGWS RPWVIHRGPS GYSDLACCES EHLFGCLFEC
GVHSECEEIA FCWFTMADLL KNVNCTEENP TGYSGGDTE
//
