ID   VSI5_TRYBB              Reviewed;         507 AA.
AC   P26330;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   02-JUN-2021, entry version 72.
DE   RecName: Full=Variant surface glycoprotein ILTAT 1.25;
DE            Short=VSG;
DE   Flags: Precursor;
OS   Trypanosoma brucei brucei.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=5702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Isolate MIAG 211;
RX   PubMed=1942032; DOI=10.1016/0022-2836(91)80178-w;
RA   Carrington M., Miller N., Blum M.L., Roditi I., Wiley D.C., Turner M.J.;
RT   "Variant specific glycoprotein of Trypanosoma brucei consists of two
RT   domains each having an independently conserved pattern of cysteine
RT   residues.";
RL   J. Mol. Biol. 221:823-835(1991).
CC   -!- FUNCTION: VSG forms a coat on the surface of the parasite. The
CC       trypanosome evades the immune response of the host by expressing a
CC       series of antigenically distinct VSGs from an estimated 1000 VSG genes.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. Note=A
CC       soluble form is released from ruptured cells by the action of a PI-PLC.
CC       {ECO:0000250}.
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DR   EMBL; X56769; CAA40088.1; -; mRNA.
DR   PIR; S18450; S18450.
DR   PRIDE; P26330; -.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR025932; Trypano_VSG_B_N_dom.
DR   InterPro; IPR019609; Variant_surf_glycoprt_trypan_C.
DR   Pfam; PF10659; Trypan_glycop_C; 1.
DR   Pfam; PF13206; VSG_B; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Glycoprotein; GPI-anchor; Lipoprotein; Membrane; Signal;
KW   Trypanosomiasis.
FT   SIGNAL          1..21
FT   CHAIN           22..484
FT                   /note="Variant surface glycoprotein ILTAT 1.25"
FT                   /id="PRO_0000036425"
FT   PROPEP          485..507
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000036426"
FT   REGION          379..409
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          432..458
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           484
FT                   /note="GPI-anchor amidated aspartate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        141
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        371
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   507 AA;  53044 MW;  BB9770F05AB3A716 CRC64;
     MQSQQQPVFI SIILLAINTD AAAPTTAVNA REFGLLCTLV RAEDNLEDRR SAGQAAKEVV
     ALAAKIELIL ANLKHIERLA AAEPEAAPKE SRSDETPEAC KASKATVCSQ AAQTYKTIRP
     DEKLALAFLA ETTGDLRSTF NVTLKQITAA AASHARYFGE NTESRPALDK IKKALYGSPE
     AKGDAIIESG DGTRSAACGN TDGNAANSAA KRATAALICL CGGDNTNTGN DACFTQTTAD
     INYAKKGGEV ERAWTEIRQK CKAGAAANKV TAAQLKAAAA ELAALIHQKR GEKAVAGLLG
     AAQINNGAVD CDGSEANGKG SCVILSTSAS KYKVETPDWL NALEAAIADL EQEQIELDNG
     RKAEAQILAL NSSXTTLLAQ AVEPTKQPPA KAAAAPEKKS NPQKDCNKNT KKRDCKEGDG
     CKWSSTEATE GAFCKPKDGE GQTSAAGAGD AGASDTEAKK CSDKKKEEEC KSPNCKWDGK
     ECKDSSILAN KQFALSVASA AFVALLF