ID   8512_TRYCR              Reviewed;         240 AA.
AC   P18270;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Sialidase 85-1.2;
DE            EC=3.2.1.18;
DE   AltName: Full=Major 85 kDa surface antigen;
DE   AltName: Full=Neuraminidase;
DE            Short=NA;
DE   AltName: Full=SA85-1.2 protein;
DE   Flags: Fragment;
GN   Name=SA85-1.2;
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; X53546; CAA37618.1; -; mRNA.
DR   PIR; S11293; S11293.
DR   AlphaFoldDB; P18270; -.
DR   SMR; P18270; -.
DR   CAZy; GH33; Glycoside Hydrolase Family 33.
DR   VEuPathDB; TriTrypDB:BCY84_13838; -.
DR   VEuPathDB; TriTrypDB:C3747_210g16; -.
DR   VEuPathDB; TriTrypDB:C4B63_94g93; -.
DR   VEuPathDB; TriTrypDB:Tc_MARK_8755; -.
DR   VEuPathDB; TriTrypDB:TcBrA4_0141070; -.
DR   VEuPathDB; TriTrypDB:TcCL_ESM09153; -.
DR   VEuPathDB; TriTrypDB:TcCLB.504491.20; -.
DR   VEuPathDB; TriTrypDB:TcCLB.508061.20; -.
DR   VEuPathDB; TriTrypDB:TcCLB.508563.20; -.
DR   VEuPathDB; TriTrypDB:TCDM_12903; -.
DR   VEuPathDB; TriTrypDB:TcG_10017; -.
DR   VEuPathDB; TriTrypDB:TCSYLVIO_009561; -.
DR   VEuPathDB; TriTrypDB:TcYC6_0130160; -.
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   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR008377; Sialidase_trypan.
DR   PRINTS; PR01803; TCSIALIDASE.
DR   SUPFAM; SSF49899; SSF49899; 1.
PE   2: Evidence at transcript level;
KW   Glycosidase; Hydrolase; Repeat.
FT   CHAIN           <1..240
FT                   /note="Sialidase 85-1.2"
FT                   /id="PRO_0000208911"
FT   REGION          127..158
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          221..240
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        127..143
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
SQ   SEQUENCE   240 AA;  26601 MW;  8B73A9F7EE19ED9C CRC64;
     EHSGDNVRHV FLNHNFTLVA SVTIEEAPSE KTPLLTALLG DAEPPYFMRL SYTADNKWET
     ISKGDKKLTT ESRPWVPKKE HQVALMLQGN KASVYIDGES LGEEAPLTVE TPLEPFGFCF
     GACDFDDDDD GGDDDDEEDS QEESSPKESS PEKIGKKPHV TVTNVFLYNR PLNPTEMRAI
     KDRIPVSTRA PEPQVKIAPK PVAPAAPGSL RCLAHGKYQQ HRGGQLWGEP PIPNMRQRDA