VSIB_TRYBB
ID VSIB_TRYBB Reviewed; 471 AA.
AC P07208;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Variant surface glycoprotein ILTAT 1.1BC;
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 [GENOMIC DNA].
RX PubMed=6927851; DOI=10.1038/298676a0;
RA Rice-Ficht A.C., Chen K.K., Donelson J.E.;
RT "Point mutations during generation of expression-linked extra copy of
RT trypanosome surface glycoprotein gene.";
RL Nature 298:676-679(1982).
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; V01384; CAA24674.1; -; Genomic_DNA.
DR PIR; S07329; S07329.
DR AlphaFoldDB; P07208; -.
DR SMR; P07208; -.
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 3: Inferred from homology;
KW Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; Lipoprotein;
KW Membrane; Signal; Trypanosomiasis.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..454
FT /note="Variant surface glycoprotein ILTAT 1.1BC"
FT /id="PRO_0000036415"
FT PROPEP 455..471
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000036416"
FT REGION 158..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..454
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 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 450
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 397..410
FT /evidence="ECO:0000250"
FT DISULFID 406..421
FT /evidence="ECO:0000250"
SQ SEQUENCE 471 AA; 50521 MW; 3F31B229E295B6D1 CRC64;
MVKAIASLML LHIWAIEEIK AERQAPSVSR TECTTPCRCA QRLEKLKKHC QMRVQTAVRK
QKENGKLAQK LLIGTITSTA GGGEQTSTTS FLLSNSSPTR RETLETNQAE IMSQLEHIIA
MEAQYYAILN VSATSTDTTL DGDGTQYNTG SITSGGFTVS KTTECNTESP EDTKEPDQTT
LSKKQGLKDL KLALRVKVAC KNGGGACSAA SSSDKIHITN ETDSKNKGTT ASTMNSQNTA
VAFATDLQIV NWKSDHIDSN ITALANALTA LDSIPDLTDP AAYTADAAFK QLVATVTLNK
PPTTELTGEV LDAVNRACAD NYGTSASELT TKIWDPLNEQ AASYYSDKTI KTDQLKLLTS
NQQLTTALGV ALAKAINVKE ASKKECNLHG HETDATCEAK GVGDNCKPPC KEVEEGGKKK
CKLDKEEAKR VAEQAATNQE TEGKDGKTTN TTGSNSFLIN KAPVLLAFLL L