ID   8513_TRYCR              Reviewed;         175 AA.
AC   P18271;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   28-JUN-2023, entry version 83.
DE   RecName: Full=Sialidase 85-1.3;
DE            EC=3.2.1.18;
DE   AltName: Full=Major 85 kDa surface antigen;
DE   AltName: Full=Neuraminidase;
DE            Short=NA;
DE   AltName: Full=SA85-1.3 protein;
DE   Flags: Fragment;
GN   Name=SA85-1.3;
OS   Trypanosoma cruzi.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX   NCBI_TaxID=5693;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=CL;
RX   PubMed=1695668; DOI=10.1084/jem.172.2.589;
RA   Kahn S., van Voorhis W., Eisen H.;
RT   "The major 85-kD surface antigen of the mammalian form of Trypanosoma cruzi
RT   is encoded by a large heterogeneous family of simultaneously expressed
RT   genes.";
RL   J. Exp. Med. 172:589-597(1990).
CC   -!- FUNCTION: Developmentally regulated neuraminidase implicated in
CC       parasite invasion of cells. May contribute to the pathology during
CC       T.cruzi infection by cleaving sialic acid from cells of the immune
CC       system.
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   -!- DEVELOPMENTAL STAGE: Mammalian stage of parasite.
CC   -!- MISCELLANEOUS: The parasite mammalian stage surface antigen exhibits
CC       extensive antigenic diversity.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 33 family. {ECO:0000305}.
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DR   EMBL; X53547; CAA37619.1; -; mRNA.
DR   PIR; S11294; S11294.
DR   AlphaFoldDB; P18271; -.
DR   SMR; P18271; -.
DR   VEuPathDB; TriTrypDB:BCY84_22557; -.
DR   VEuPathDB; TriTrypDB:C3747_88g95; -.
DR   VEuPathDB; TriTrypDB:C4B63_155g14; -.
DR   VEuPathDB; TriTrypDB:ECC02_012905; -.
DR   VEuPathDB; TriTrypDB:Tc_MARK_7633; -.
DR   VEuPathDB; TriTrypDB:TcBrA4_0142060; -.
DR   VEuPathDB; TriTrypDB:TcCL_NonESM11807; -.
DR   VEuPathDB; TriTrypDB:TcCLB.463279.20; -.
DR   VEuPathDB; TriTrypDB:TcCLB.506537.80; -.
DR   VEuPathDB; TriTrypDB:TcCLB.508285.60; -.
DR   VEuPathDB; TriTrypDB:TCDM_12359; -.
DR   VEuPathDB; TriTrypDB:TcG_10017; -.
DR   VEuPathDB; TriTrypDB:TCSYLVIO_008783; -.
DR   VEuPathDB; TriTrypDB:TcYC6_0130460; -.
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:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.200; -; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR008377; Sialidase_trypan.
DR   Pfam; PF13385; Laminin_G_3; 1.
DR   PRINTS; PR01803; TCSIALIDASE.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE   2: Evidence at transcript level;
KW   Glycosidase; Hydrolase; Repeat.
FT   CHAIN           <1..175
FT                   /note="Sialidase 85-1.3"
FT                   /id="PRO_0000208912"
FT   NON_TER         1
SQ   SEQUENCE   175 AA;  19552 MW;  E90DD13274B75B8F CRC64;
     LCLNATVRNA TKVKDGFQLT EPDSGVMWPV NIPDYNKRHV FLNHNFTLVA SVTIEEAPSG
     NTPLLIAVLA NTEPTHTMRI LYTADNKWMT MLKDEKKPTT ESGTWEPKKE HQVALMLQGN
     KASVYVDGEL LGEEEVPLTG EKPLELFAFC FGACGEENPS QESHVTVTNV FLYNR
//