ID   VSI1_TRYBB              Reviewed;         471 AA.
AC   P26326;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Variant surface glycoprotein ILTAT 1.21;
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 201;
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; X56766; CAA40085.1; -; mRNA.
DR   PIR; S18446; S18446.
DR   AlphaFoldDB; P26326; -.
DR   SMR; P26326; -.
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   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..454
FT                   /note="Variant surface glycoprotein ILTAT 1.21"
FT                   /id="PRO_0000036417"
FT   PROPEP          455..471
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000036418"
FT   REGION          406..449
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        412..429
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        435..449
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           454
FT                   /note="GPI-anchor amidated serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        64
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        405
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        450
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   471 AA;  50481 MW;  784F48E944EEA37C CRC64;
     MLRALLPSTT LALILAGGGH AAVGDAFPAF AVLCAAWDAA TNKQIKPWSE DRELPELNDI
     YNMNMSIASE EWQTIFDGQA EQQTWSQFAQ ANAGKYKGID WKQNWDRWRK QRQQTKDAGG
     AWQTKNHRPE WAATPRDVRP VILAIAEEAT ELSRKLEPPR TADGKDLIAE INSKLASARC
     SGELKAAAGN IGCTGPEGTP DKTTTCTTAK AGGSIGHDML CLCSVAEATD KCSSTGVGDA
     VPNSGEKLRS NGFQHIVARC PKGPESGTLP QAIDLALAML ATALGTQQPG SNNMILGKSG
     GGTCTATNSA CVDYHEKFSK QQAGITGIPW VALLQQARAL YGTYVDAKLA AQTARQQIVM
     LAGQAKREYR RPAGSLKDPA GVIQEQATNR RRHGADDTNQ CTSNNATADE CPETRCEYDS
     EKNECRPKKG TETTATGPGE RTTPADGKAN NTVSDSLLIK TSPLWLAFLL F