VSM5_TRYBB
ID VSM5_TRYBB Reviewed; 474 AA.
AC P26333;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Variant surface glycoprotein MITAT 1.5;
DE AltName: Full=VSG 118;
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 118;
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; X56763; CAA40082.1; -; mRNA.
DR PIR; S18452; S18452.
DR AlphaFoldDB; P26333; -.
DR SMR; P26333; -.
DR ABCD; P26333; 5 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..22
FT CHAIN 23..451
FT /note="Variant surface glycoprotein MITAT 1.5"
FT /id="PRO_0000036437"
FT PROPEP 452..474
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000036438"
FT REGION 388..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..419
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..449
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 451
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 37..161
FT /evidence="ECO:0000250"
FT DISULFID 144..214
FT /evidence="ECO:0000250"
SQ SEQUENCE 474 AA; 49754 MW; 5DD75808A01BB6BB CRC64;
MIHSNKVATV VLALISSWPA DGTNNHGLKL QKAQAICKMS KELKATAMRA ANDAKLKITE
ILELENVFAA MIPNATKGTE ADGCTDYNAV FLEANNTAAE TVSKIATLAE SATKAAGAAG
RAAGVLDEFI AALAQAQGAT GLYCIQGSGT GAATHTELAD CFNGDLKPRN MLSIRDPKVS
AAATGSTDLT TLAKAMAASG TDTTFHGDQQ SKGCGLMKGT SDGIMIGQAL TGTFAWAQGL
LRFGALGANG IASTGVTGYA HTATASGNGV HWASDPEKIP VIAEAIALVS NYNTLADSIG
TRAKDAIEKV KKCMKATNKE IKREHIFLNV SHLNRELQKA VTELDKALNK QDAKAEAKQQ
PNCDDKKQIE CGDTPGCGWH KAEGKCEAKD GEGQKNQATG EKDANKNRCT QHGTNKEACE
KENTPGQSAV CGFRKGKDGE TDEPDKEKCR NGSFLTSKQF AFSVVSAAFM ALLF
