TCNA_TRYCR
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 25-MAY-2022, entry version 108.
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 CAZy; GH33; Glycoside Hydrolase Family 33.
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: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 GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 PANTHER; PTHR10628; PTHR10628; 1.
DR Pfam; PF13859; BNR_3; 1.
DR PRINTS; PR01803; TCSIALIDASE.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF50939; SSF50939; 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 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
