ID   TCNA_TRYCR              Reviewed;        1162 AA.
AC   P23253;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   04-NOV-2026, entry version 122.
DE   RecName: Full=Sialidase;
DE            EC=3.2.1.18;
DE   AltName: Full=Major surface antigen;
DE   AltName: Full=Neuraminidase;
DE            Short=NA;
GN   Name=TCNA;
OS   Trypanosoma cruzi.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX   NCBI_TaxID=5693;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Silvio X-10/4;
RX   PubMed=1711561; DOI=10.1084/jem.174.1.179;
RA   Pereira M.E.A., Mejia J.S., Ortega-Barria E., Matzilevich D., Prioli R.P.;
RT   "The Trypanosoma cruzi neuraminidase contains sequences similar to
RT   bacterial neuraminidases, YWTD repeats of the low density lipoprotein
RT   receptor, and type III modules of fibronectin.";
RL   J. Exp. Med. 174:179-191(1991).
RN   [2]
RP   SUBCELLULAR LOCATION.
RX   PubMed=1896773;
RA   Prioli R.P., Mejia J.S., Aji T., Aikawa M., Pereira M.E.A.;
RT   "Trypanosoma cruzi: localization of neuraminidase on the surface of
RT   trypomastigotes.";
RL   Trop. Med. Parasitol. 42:146-150(1991).
CC   -!- FUNCTION: Developmentally regulated neuraminidase implicated in
CC       parasite invasion of cells.
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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC       anchor {ECO:0000305}.
CC   -!- DEVELOPMENTAL STAGE: Maximal activity in trypomastigotes, minimum in
CC       epimastigotes and not detectable in amastigotes.
CC   -!- MISCELLANEOUS: The variable lengths of the long tandem repeat domain
CC       could account in part for the polymorphism of the TCNA protein.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 33 family. {ECO:0000305}.
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DR   EMBL; M61732; AAA30255.1; -; Genomic_DNA.
DR   PIR; JH0557; JH0557.
DR   AlphaFoldDB; P23253; -.
DR   SMR; P23253; -.
DR   GlyCosmos; P23253; 3 sites, No reported glycans.
DR   VEuPathDB; TriTrypDB:BCY84_01981; -.
DR   VEuPathDB; TriTrypDB:C3747_24g366; -.
DR   VEuPathDB; TriTrypDB:C3747_34g136; -.
DR   VEuPathDB; TriTrypDB:C4B63_136g6; -.
DR   VEuPathDB; TriTrypDB:C4B63_69g34; -.
DR   VEuPathDB; TriTrypDB:C4B63_69g50; -.
DR   VEuPathDB; TriTrypDB:ECC02_001599; -.
DR   VEuPathDB; TriTrypDB:ECC02_006627; -.
DR   VEuPathDB; TriTrypDB:Tc_MARK_7083; -.
DR   VEuPathDB; TriTrypDB:Tc_MARK_7565; -.
DR   VEuPathDB; TriTrypDB:Tc_MARK_7746; -.
DR   VEuPathDB; TriTrypDB:TcBrA4_0148830; -.
DR   VEuPathDB; TriTrypDB:TcBrA4_0148920; -.
DR   VEuPathDB; TriTrypDB:TcBrA4_0148930; -.
DR   VEuPathDB; TriTrypDB:TcCL_NonESM05117; -.
DR   VEuPathDB; TriTrypDB:TcCL_NonESM13817; -.
DR   VEuPathDB; TriTrypDB:TcCL_Unassigned02121; -.
DR   VEuPathDB; TriTrypDB:TcCLB.401569.10; -.
DR   VEuPathDB; TriTrypDB:TcCLB.507979.30; -.
DR   VEuPathDB; TriTrypDB:TcCLB.509481.10; -.
DR   VEuPathDB; TriTrypDB:TcCLB.510095.20; -.
DR   VEuPathDB; TriTrypDB:TcCLB.510787.10; -.
DR   VEuPathDB; TriTrypDB:TCDM_09295; -.
DR   VEuPathDB; TriTrypDB:TcG_05563; -.
DR   VEuPathDB; TriTrypDB:TcG_07787; -.
DR   VEuPathDB; TriTrypDB:TCSYLVIO_000115; -.
DR   VEuPathDB; TriTrypDB:TCSYLVIO_003468; -.
DR   VEuPathDB; TriTrypDB:TCSYLVIO_003553; -.
DR   VEuPathDB; TriTrypDB:TcYC6_0130920; -.
DR   OMA; ADCEHNE; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004308; F:exo-alpha-sialidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006689; P:ganglioside catabolic process; IEA:TreeGrafter.
DR   GO; GO:0009313; P:oligosaccharide catabolic process; IEA:TreeGrafter.
DR   CDD; cd15482; Sialidase_non-viral; 1.
DR   Gene3D; 2.120.10.10; -; 1.
DR   Gene3D; 2.60.120.200; -; 1.
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; IPR055239; TS_C.
DR   PANTHER; PTHR10628:SF30; EXO-ALPHA-SIALIDASE; 1.
DR   PANTHER; PTHR10628; SIALIDASE; 1.
DR   Pfam; PF13859; BNR_3; 1.
DR   Pfam; PF22925; TS_C; 1.
DR   PRINTS; PR01803; TCSIALIDASE.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF50939; Sialidases; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Glycoprotein; Glycosidase; GPI-anchor; Hydrolase;
KW   Lipoprotein; Membrane; Phosphoprotein; Repeat.
FT   CHAIN           1..1162
FT                   /note="Sialidase"
FT                   /id="PRO_0000208910"
FT   REPEAT          23..34
FT                   /note="BNR 1"
FT   REPEAT          163..174
FT                   /note="BNR 2"
FT   REPEAT          209..220
FT                   /note="BNR 3"
FT   REGION          587..1123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          589..1120
FT                   /note="44 X 12 AA tandem repeats, LTR domain"
FT   COMPBIAS        589..615
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        616..689
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        699..1123
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        342
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        394
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1125
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1162 AA;  120033 MW;  07049221897C6A40 CRC64;
     MVAIADARYE TSSENSLIDT VAKYSVDDGE TWETQIAIKN SRVSSVSRVV DPTVIVKGNK
     LYVLVGSYYS SRSYWSSHGD ARDWDILLAV GEVTKSTAGG KITASIKWGS PVSLKKFFPA
     EMEGMHTNQF LGGAGVAIVA SNGNLVYPVQ VTNKRKQVFS KIFYSEDDGK TWKFGKGRSD
     FGCSEPVALE WEGKLIINTR VDWKRRLVYE SSDMEKPWVE AVGTVSRVWG PSPKSNQPGS
     QTSFTAVTIE GMRVMLFTHP LNFKGRCVRD RLNLWLTDNQ RIYNVGQVSI GDENSAYSSV
     LYKDDKLYCL HEINTDEVYS LVFARLVGEL RIIKSVLRSW KNWTATCPAF APLLIQPLRR
     QRVVVVPLSP RLVLLAFCRQ RLPKRMGGSY RCVNASTANA ERVRNGLKFA GVGGGALWPV
     SQQGQNQRYR FANHAFTLVA SVTIHEAPRA ASPLLGASLD SSGGKKLLGL SYDEKHQWQP
     IYGSTPVTPT GSWETGKRYH LVLTMANKIG SVYIDGELLE GSGQTVVPDG RTPDISHFYV
     GGYKRSDMPT ISHVTVNNVL LYNRRQLNTE EIRTLFLSQD LIGTEAHMDS SSDSSAHSTP
     STPADSSAHS TPSTPVDSSA HSTPSTPADS SAHGTPSTPV DSSAHGTPST PADSSAHGTP
     STPVDSSAHS TPSTPVDSSA HSTPSTPVDS SAHGAPSTPA DSSAHGTPST PVDSSAHGTP
     STPADSSAHS TPSTPADSSA HSTPSTPADS SAHSTPSTPV DSSAHGTPST PADSSAHSTP
     STPADSSAHG TPSTPVDSSA HSTPSTPVDS SAHGTPSTPV DSSAHSTPST PVDSSAHGTP
     STPVDSSAHS TPSTPADSSA HSTPSTPADS SAHGTPSTPV DSSAHSTPST PADSSAHSTP
     STPVDSSAHS TPSTPADSSA HGTPSTPVDS SAHGTPSTPA DSSAHSTPST PADSSAHSTP
     STPADSSAHS TPSTPVDSSA HSTPSTPADS SAHSTPSTPA DSSAHSTPST PADSSAHSTP
     STPVDSSAHS TPSTPADSSA HGTPSTPADS SAHSTPSTPV DSSAHSTPST PADSSAHGTP
     STPADSSAHS TPSTPADSSA HGTPSTPADS SAHSTPSTPA GSSANGTVLI LPDGAALSTF
     SGGGLLLCAC ALLLHVFFMA VF
//