ID   VSI2_TRYBB              Reviewed;         479 AA.
AC   P26327;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Variant surface glycoprotein ILTAT 1.22;
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 202B;
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; X56765; CAA40084.1; -; mRNA.
DR   PIR; S18447; S18447.
DR   AlphaFoldDB; P26327; -.
DR   SMR; P26327; -.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR027446; VSG_C_dom_sf.
DR   SUPFAM; SSF118251; SSF118251; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Glycoprotein; GPI-anchor; Lipoprotein; Membrane; Signal;
KW   Trypanosomiasis.
FT   SIGNAL          1..12
FT   CHAIN           13..462
FT                   /note="Variant surface glycoprotein ILTAT 1.22"
FT                   /id="PRO_0000036419"
FT   PROPEP          463..479
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000036420"
FT   LIPID           462
FT                   /note="GPI-anchor amidated asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        120
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        458
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   479 AA;  51458 MW;  FF7205FF0F58435A CRC64;
     MDTAQVFALF YMATVMAAGT KNKASQAVSD PCSEIHFDEQ LANYFENEVS AATTQLDENQ
     NFERSWKLLQ YLQMDHQKSK GAAALAAYAS TINIRTAANV KAASGELLTA ASLLRQRAAN
     VSAAFQLQGQ GVIKLGTPDI DNGAKSITHA DAGCNYAAIS KTVPTQRCTP PQQQADTITA
     ADMQPDKLDE LQLITEAYTT TITIAASAYS KGTPATGHTV YTYGNCQSTG GSASAQLGDT
     HALGIHVKTI GTKAVTEKTT LQPSSSNKCP DEGTTAELTP IKRLARAICL ARKASLAKPK
     ALSRLQYSDL QTDTDFKRIA AIFLSRNGKQ LDPEKDSQEI NELIKETYGP NEEHFHKSYV
     EALDNKKWEF KIKESKIEGT VNALANGVDA GLATAYYASK RQSTCGQAAA DTPIVSSDVE
     KCKGKTQDDC RTADECEMRD GECNAKVAKT AEPDSKTNTT GNNSFAIKTS TLLLAVLLF