ID   8511_TRYCR              Reviewed;         752 AA.
AC   P18269;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=Sialidase 85-1.1;
DE            EC=3.2.1.18;
DE   AltName: Full=Major 85 kDa surface antigen;
DE   AltName: Full=Neuraminidase;
DE            Short=NA;
DE   AltName: Full=SA85-1.1 protein;
DE   Flags: Precursor;
GN   Name=SA85-1.1;
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=2034687; DOI=10.1073/pnas.88.10.4481;
RA   Kahn S., Colbert T.G., Wallace J.C., Hoagland N.A., Eisen H.;
RT   "The major 85-kDa surface antigen of the mammalian-stage forms of
RT   Trypanosoma cruzi is a family of sialidases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:4481-4485(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 520-752.
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; M62735; AAA30245.1; -; mRNA.
DR   EMBL; X53545; CAA37617.1; -; mRNA.
DR   PIR; A39378; A39378.
DR   PIR; S11292; S11292.
DR   AlphaFoldDB; P18269; -.
DR   SMR; P18269; -.
DR   CAZy; GH33; Glycoside Hydrolase Family 33.
DR   VEuPathDB; TriTrypDB:BCY84_06519; -.
DR   VEuPathDB; TriTrypDB:C3747_244g28; -.
DR   VEuPathDB; TriTrypDB:C4B63_62g100; -.
DR   VEuPathDB; TriTrypDB:Tc_MARK_4947; -.
DR   VEuPathDB; TriTrypDB:TcBrA4_0141070; -.
DR   VEuPathDB; TriTrypDB:TcCL_ESM07364; -.
DR   VEuPathDB; TriTrypDB:TcCLB.508061.20; -.
DR   VEuPathDB; TriTrypDB:TcCLB.508285.60; -.
DR   VEuPathDB; TriTrypDB:TcCLB.509411.10; -.
DR   VEuPathDB; TriTrypDB:TCDM_12170; -.
DR   VEuPathDB; TriTrypDB:TcG_10912; -.
DR   VEuPathDB; TriTrypDB:TCSYLVIO_007680; -.
DR   VEuPathDB; TriTrypDB:TcYC6_0130090; -.
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; IPR011040; Sialidase.
DR   InterPro; IPR026856; Sialidase_fam.
DR   InterPro; IPR036278; Sialidase_sf.
DR   InterPro; IPR008377; Sialidase_trypan.
DR   InterPro; IPR021287; Trans-sialidase_CS.
DR   PANTHER; PTHR10628; PTHR10628; 1.
DR   Pfam; PF13859; BNR_3; 1.
DR   Pfam; PF11052; Tr-sialidase_C; 1.
DR   PRINTS; PR01803; TCSIALIDASE.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   SUPFAM; SSF50939; SSF50939; 1.
PE   2: Evidence at transcript level;
KW   Glycosidase; Hydrolase; Repeat; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..752
FT                   /note="Sialidase 85-1.1"
FT                   /id="PRO_0000012039"
FT   REPEAT          274..285
FT                   /note="BNR 1"
FT   REPEAT          319..330
FT                   /note="BNR 2"
FT   REGION          693..725
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   752 AA;  80847 MW;  BDC33F3EF2DC6859 CRC64;
     MSRRVFASAV LLLIVVTMCC GGAATAQVGS NADASTPGSA LTGAIAGEGS SSGGVEGLQR
     VDLFVPQKTQ VLPKKGPDSS RRDSFFSPSL VSAGGVIAAF AEGHINTKNP HNESAKPFSD
     VVAGYIDSAW EWPTLVEKVS ESTWQAHTVL GKAEGKKSLD VVLRPTTTTK GNKVFLLAGS
     TDLSYVNWSW REGSLELKLV VGDVTKPTSS EPTERIKWGE IKSLLNESTI AAQKGKLTEF
     LASGGSGVVM EDGTIVFSLM AVNEKKDGVF SLIIYSKDNG STWSLSEGIS PAKCGAPRIT
     EWEGSLLMIV DCENDQRVYV SRDMGTTWTE AIGTLSGVGS THNWETIGRR LAVEALITVT
     IEGRKVMLYT QRGYALGETE TTSPLYLWVT DNNRSFFVGP VGMDNAVKGE LAGALLYSDG
     GLHLLQRRDS GEDSVMSLSR LTEELKEIKS VLSTWSQKDV FFSSLSIPTV GLVAVLSDAA
     GDGRWYDEYL CLNATVTNAT KVKDGFQLTE PDSRAVWSVN IPDGNVRHIS LSHNFTLVAS
     VIIEEAPSGN TPLLTAVLVD AGPEYFMRLS YTADNKWMTM LKDEKKPTTE SRPWEAGKEH
     QVALMLQGNK ASVYVDGELL GEEEVPLTGE KPLEIFAFCF GACKIDGDEE ESSPKEIGKK
     PRVTVTNVFL YNRPLNSTEM RAIKDRIPVP TRAPEPQVKI APKPAAPAAP AGNEETARET
     GDGGANGDAV SAYGRVLLPL LFLLGLWGLA TA