ID   VSI6_TRYBB              Reviewed;         503 AA.
AC   P06014;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Variant surface glycoprotein ILTAT 1.3;
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].
RA   Rice-Ficht A.C., Chen K.K., Donelson J.E.;
RT   "Sequence homologies near the C-termini of the variable surface
RT   glycoproteins of Trypanosoma brucei.";
RL   Nature 294:53-57(1981).
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; J01221; AAA30288.1; -; mRNA.
DR   PIR; S09640; S09640.
DR   AlphaFoldDB; P06014; -.
DR   SMR; P06014; -.
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:0042783; P:evasion of host immune response; IEA:InterPro.
DR   InterPro; IPR001812; Trypano_VSG_A_N_dom.
DR   InterPro; IPR019609; Variant_surf_glycoprt_trypan_C.
DR   Pfam; PF00913; Trypan_glycop; 1.
DR   Pfam; PF10659; Trypan_glycop_C; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; Lipoprotein;
KW   Membrane; Signal; Trypanosomiasis.
FT   SIGNAL          1..29
FT   CHAIN           30..480
FT                   /note="Variant surface glycoprotein ILTAT 1.3"
FT                   /id="PRO_0000036427"
FT   PROPEP          481..503
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000036428"
FT   LIPID           480
FT                   /note="GPI-anchor amidated aspartate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        419
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        432
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        42..168
FT                   /evidence="ECO:0000250"
FT   DISULFID        150..206
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   503 AA;  54618 MW;  70144D8B0408AA9A CRC64;
     MTKAYENRML LQALVLAAVL CTTHAEGTAK APLKHSVATG FCSFSKAAKQ AANKLAQTLD
     AVKATLNQNR KAHLQNLLVA VKRPTEQIAA LILGQYANTQ AASGLSDLGK WAPDETKTIG
     QALYTSGRLD GFIDVLDGHR SENSGQNKNC IANDGDGTTK AFDFDALCGP TEVAKAGNEP
     GDLKSSDRNG FWWHRRAAAS GGNNHCVIFD DLNTAYSTKT AATDFLAGLI KVHQTTGLTA
     ATAIAAQKST NKILKDIDAN WPKVQQAYTT AAGRSPTTEQ EYKDLLKDES SRQKLRAAAQ
     TVNNWKPADK PANMDDYLKQ VFKIDANVNS AYVTAMKEIS MDVPTKDGET QKKELFEMSE
     EDLEAALAVE IRRLSSENAK LTTEVKQLRR NQGKQATEDT CNKMKGETAC NNKPFCTYNA
     TETDENKKCK FNETKASKSG VSVAQAQTGG TQTTTDKCKD KKKDDCKSPD CKWEGETCKD
     SSFILNKQFA LSVVSAAFAA LLF