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GP85_TRYCR
ID   GP85_TRYCR              Reviewed;         714 AA.
AC   Q03877;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=85 kDa surface antigen;
DE   Flags: Precursor;
GN   Name=GP85;
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=Y;
RX   PubMed=1762630; DOI=10.1016/0166-6851(91)90114-l;
RA   Takle G.B., Cross G.A.M.;
RT   "An 85-kilodalton surface antigen gene family of Trypanosoma cruzi encodes
RT   polypeptides homologous to bacterial neuraminidases.";
RL   Mol. Biochem. Parasitol. 48:185-198(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE OF 42-461.
RC   STRAIN=Y;
RX   PubMed=2693963; DOI=10.1016/0166-6851(89)90102-3;
RA   Takle G.B., Young A., Snary D., Hudson L., Nicholls S.C.;
RT   "Cloning and expression of a trypomastigote-specific 85-kilodalton surface
RT   antigen gene from Trypanosoma cruzi.";
RL   Mol. Biochem. Parasitol. 37:57-64(1989).
CC   -!- FUNCTION: Implicated in attachment and penetration of host cells,
CC       possibly via a neuraminidase activity.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
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DR   EMBL; M64836; AAA30150.1; -; mRNA.
DR   EMBL; J04667; AAA03205.1; -; Unassigned_DNA.
DR   PIR; S25236; S25236.
DR   AlphaFoldDB; Q03877; -.
DR   SMR; Q03877; -.
DR   CAZy; GH33; Glycoside Hydrolase Family 33.
DR   VEuPathDB; TriTrypDB:BCY84_06519; -.
DR   VEuPathDB; TriTrypDB:C3747_81g99; -.
DR   VEuPathDB; TriTrypDB:C4B63_10g538; -.
DR   VEuPathDB; TriTrypDB:Tc_MARK_4947; -.
DR   VEuPathDB; TriTrypDB:TcBrA4_0143290; -.
DR   VEuPathDB; TriTrypDB:TcCL_ESM05132; -.
DR   VEuPathDB; TriTrypDB:TcCLB.463323.10; -.
DR   VEuPathDB; TriTrypDB:TcCLB.506241.30; -.
DR   VEuPathDB; TriTrypDB:TcCLB.506455.30; -.
DR   VEuPathDB; TriTrypDB:TCDM_12888; -.
DR   VEuPathDB; TriTrypDB:TcG_10912; -.
DR   VEuPathDB; TriTrypDB:TCSYLVIO_007680; -.
DR   VEuPathDB; TriTrypDB:TcYC6_0131230; -.
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:0004308; F:exo-alpha-sialidase activity; IEA:InterPro.
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   Cell membrane; Glycoprotein; GPI-anchor; Lipoprotein; Membrane; Repeat;
KW   Signal.
FT   SIGNAL          1..24
FT   CHAIN           25..691
FT                   /note="85 kDa surface antigen"
FT                   /id="PRO_0000021358"
FT   PROPEP          692..714
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000021359"
FT   REPEAT          258..268
FT                   /note="BNR 1"
FT   REPEAT          302..313
FT                   /note="BNR 2"
FT   LIPID           691
FT                   /note="GPI-anchor amidated alanine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        96
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        124
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        171
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        375
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        475
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        546
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        652
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   714 AA;  77875 MW;  6780D792790DC8AF CRC64;
     MSRRVFTSAA LHLLVVMWMC CGPCEAAAAS TGENSVNARQ PQRFDLFVPQ KTVLLPRGGG
     NSEKKWDSFA SPSLVSAGGV IAAFAEGHLS SKNKDNKSTE PSSDAVAWYI DSAWEWSTLV
     GEVNKSTWQA HTVLGKVDGK ERFDVVLRPT TTTKDNKVFL LAGSSVASNV NGSWSHGGLK
     LKLVVGDVRK PTDSEQSGRI NWGEVQSPLN ENSGAVQERK LTAFVASGGA GVLMEDGTIV
     FSLMARNEEE DVYSMIIYSK DDGSTWALSN SVSSAKCVNP RITEWEGSLL MIVDCEDEQK
     VYVSRDMGTT WTEAVGKLLG VWVNSGSGAS QDSSLHVDAL ITATIEGRRV MLYTQRGNSL
     GENANPLYLW VTDNNRSFHV GPVGMDNAEK EELESALLYS DGKLHLLQRR VSGEGSVISL
     SRLTEELKEI ESVLSTWAQK DIFFSSLSIP TAGLVAVLSD AAGDGRWNDE YLCLNATVKN
     AVKVKDGFQL TESNSRVLWS VNTRDNNLRH VFLSHDFTVV ATVIIQNVPS GKTSLLTATL
     ANTESNYTMG LSYTADNKWE TIFKGDKKPT TESRPWEPKK EYQVALMLQG KKASVYIDGR
     SLGEGEALLT DEKSLEFVHF CFGACVQESS PTAAQKTKVT VTNVFLYNRP LNSTEMRAIK
     DRIPIPKRGP GSQVEGGTER RHIPRIEGVR ANAPVGSGLL PLLLLLGLWV FAAL
 
 
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