ID   VSA1_TRYBB              Reviewed;         503 AA.
AC   P06015; Q26722;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Variant surface glycoprotein AnTaT 1.1;
DE            Short=VSG;
DE   AltName: Full=Expression-linked copy;
DE            Short=ELC;
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 [GENOMIC DNA].
RX   PubMed=6313354; DOI=10.1002/j.1460-2075.1983.tb01565.x;
RA   Michiels F., Matthyssens G., Kronenberger P., Pays E., Dero B.,
RA   van Assel S., Darrille M., Cravador A., Steinert M., Hamers R.;
RT   "Gene activation and re-expression of a Trypanosoma brucei variant surface
RT   glycoprotein.";
RL   EMBO J. 2:1185-1192(1983).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-416.
RC   STRAIN=EATRO 1125;
RX   PubMed=2323332;
RA   van der Werf A., van Assel S., Aerts D., Steinert M., Pays E.;
RT   "Telomere interactions may condition the programming of antigen expression
RT   in Trypanosoma brucei.";
RL   EMBO J. 9:1035-1040(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 391-503.
RX   PubMed=7278981; DOI=10.1038/293230a0;
RA   Matthyssens G., Michiels F., Hamers R., Pays E., Steinert M.;
RT   "Two variant surface glycoproteins of Trypanosoma brucei have a conserved
RT   C-terminus.";
RL   Nature 293:230-233(1981).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 270-344.
RX   PubMed=4053185; DOI=10.1016/0092-8674(85)90278-8;
RA   Pays E., Houard S., Pays A., van Assel S., Dupont F., Aerts D.,
RA   Huet-Duviller G., Gomes V., Richet C., Degand P., van Meirvenne N.,
RA   Steinert M.;
RT   "Trypanosoma brucei: the extent of conversion in antigen genes may be
RT   related to the DNA coding specificity.";
RL   Cell 42:821-829(1985).
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; X01843; CAA25971.1; -; Genomic_DNA.
DR   EMBL; X15817; CAA33809.1; -; Genomic_DNA.
DR   EMBL; M12005; AAA30162.1; -; Genomic_DNA.
DR   EMBL; J01213; AAA30280.1; -; mRNA.
DR   PIR; S07174; VMUT1B.
DR   AlphaFoldDB; P06015; -.
DR   SMR; P06015; -.
DR   ABCD; P06015; 17 sequenced antibodies.
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 AnTaT 1.1"
FT                   /id="PRO_0000036409"
FT   PROPEP          481..503
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000036410"
FT   LIPID           480
FT                   /note="GPI-anchor amidated aspartate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        113
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
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        45..172
FT                   /evidence="ECO:0000250"
FT   DISULFID        154..209
FT                   /evidence="ECO:0000250"
FT   CONFLICT        334
FT                   /note="A -> P (in Ref. 2; CAA33809)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        346
FT                   /note="A -> V (in Ref. 2; CAA33809)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        419
FT                   /note="N -> K (in Ref. 3)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   503 AA;  52814 MW;  38541B93F6DF46C6 CRC64;
     MVTKERNAAL KIVMLVASAL TLHPQQALAQ TAGRPLADVV GKTLCTYSKT AKRQAANLAQ
     TLQRASSAAK QSRQAQQLAA LALAKLPDYK EAAATLLIYA THKIQDAQAS IENWTGENTK
     LVGQAMYSSG RIDELMLLLE GHREDGANGQ DKTCLGAAAG GNTVNEFVKT ECDTESGHNI
     EADNSNIGQA ATTLSQESTD PEASGGASCK ITANLATDYD SHANELPLLG GLLTIHNAGG
     FKTGQSLQTA APTNKLISAL KNKGAGVAAK LATVTSAAPT SKQELKTLLA SKGERAKLQA
     ANDEYNNWKP GAKPEDFDAH IKKVFGAEDG KDSAYAIALE GISIEAPLGG GQTQNKQLYS
     MQPKDLMAAL IGTIAELQTA AATKPACPGH KQTTTESDAL CSKIKDANEC NSKHFCSYNG
     TETDSAKKCK YNATKASASD APVTQAQTTS RSETPAEKCT GKKKDDCKDG CKWEAETCKD
     SSILLTKNFA LSVVSAALVA LLF