VSI4_TRYBB
ID VSI4_TRYBB Reviewed; 514 AA.
AC P26329;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Variant surface glycoprotein ILTAT 1.24;
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 209;
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).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 24-381.
RX PubMed=8464512; DOI=10.1038/362603a0;
RA Blum M.L., Down J.A., Gurnett A.M., Carrington M., Turner M.J., Wiley D.C.;
RT "A structural motif in the variant surface glycoproteins of Trypanosoma
RT brucei.";
RL Nature 362:603-609(1993).
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; X56767; CAA40086.1; -; mRNA.
DR PIR; S18449; S18449.
DR PDB; 2JWG; NMR; -; A=405-450.
DR PDB; 2JWH; NMR; -; A=445-491.
DR PDB; 2VSG; X-ray; 2.70 A; A/B=24-381.
DR PDBsum; 2JWG; -.
DR PDBsum; 2JWH; -.
DR PDBsum; 2VSG; -.
DR AlphaFoldDB; P26329; -.
DR BMRB; P26329; -.
DR SMR; P26329; -.
DR EvolutionaryTrace; P26329; -.
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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor;
KW Lipoprotein; Membrane; Signal; Trypanosomiasis.
FT SIGNAL 1..23
FT CHAIN 24..491
FT /note="Variant surface glycoprotein ILTAT 1.24"
FT /id="PRO_0000036423"
FT PROPEP 492..514
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036424"
FT REGION 451..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 491
FT /note="GPI-anchor amidated aspartate"
FT /evidence="ECO:0000250"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 37..162
FT DISULFID 143..204
FT HELIX 30..43
FT /evidence="ECO:0007829|PDB:2VSG"
FT HELIX 46..77
FT /evidence="ECO:0007829|PDB:2VSG"
FT HELIX 82..135
FT /evidence="ECO:0007829|PDB:2VSG"
FT STRAND 139..144
FT /evidence="ECO:0007829|PDB:2VSG"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:2VSG"
FT TURN 154..157
FT /evidence="ECO:0007829|PDB:2VSG"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:2VSG"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:2VSG"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:2VSG"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:2VSG"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:2VSG"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:2VSG"
FT TURN 214..216
FT /evidence="ECO:0007829|PDB:2VSG"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:2VSG"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:2VSG"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:2VSG"
FT STRAND 235..239
FT /evidence="ECO:0007829|PDB:2VSG"
FT STRAND 242..245
FT /evidence="ECO:0007829|PDB:2VSG"
FT TURN 251..255
FT /evidence="ECO:0007829|PDB:2VSG"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:2VSG"
FT HELIX 262..274
FT /evidence="ECO:0007829|PDB:2VSG"
FT HELIX 286..294
FT /evidence="ECO:0007829|PDB:2VSG"
FT HELIX 297..310
FT /evidence="ECO:0007829|PDB:2VSG"
FT HELIX 315..317
FT /evidence="ECO:0007829|PDB:2VSG"
FT HELIX 321..328
FT /evidence="ECO:0007829|PDB:2VSG"
FT HELIX 335..343
FT /evidence="ECO:0007829|PDB:2VSG"
FT STRAND 347..349
FT /evidence="ECO:0007829|PDB:2VSG"
FT STRAND 352..354
FT /evidence="ECO:0007829|PDB:2VSG"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:2VSG"
FT HELIX 362..364
FT /evidence="ECO:0007829|PDB:2VSG"
FT HELIX 368..380
FT /evidence="ECO:0007829|PDB:2VSG"
FT HELIX 408..413
FT /evidence="ECO:0007829|PDB:2JWG"
FT HELIX 418..423
FT /evidence="ECO:0007829|PDB:2JWG"
FT STRAND 427..429
FT /evidence="ECO:0007829|PDB:2JWG"
FT STRAND 439..442
FT /evidence="ECO:0007829|PDB:2JWG"
FT HELIX 444..446
FT /evidence="ECO:0007829|PDB:2JWG"
FT TURN 460..463
FT /evidence="ECO:0007829|PDB:2JWH"
FT TURN 467..471
FT /evidence="ECO:0007829|PDB:2JWH"
FT TURN 474..476
FT /evidence="ECO:0007829|PDB:2JWH"
FT TURN 479..481
FT /evidence="ECO:0007829|PDB:2JWH"
FT STRAND 482..484
FT /evidence="ECO:0007829|PDB:2JWH"
SQ SEQUENCE 514 AA; 55169 MW; E77395A9E9CFDC8E CRC64;
MVYRNILQLS VLKVLLIVLI VEATHFGVKY ELWQPECELT AELRKTAGVA KMKVNSDLNS
FKTLELTKMK LLTFAAKFPE SKEALTLRAL EAALNTDLRA LRDNIANGID RAVRATAYAS
EAAGALFSGI QTLHDATDGT TYCLSASGQG SNGNAAMASQ GCKPLALPEL LTEDSYNTDV
ISDKGFPKIS PLTNAQGQGK SGECGLFQAA SGAQATNTGV QFSGGSRINL GLGAIVASAA
QQPTRPDLSD FSGTARNQAD TLYGKAHASI TELLQLAQGP KPGQTEVETM KLLAQKTAAL
DSIKFQLAAS TGKKTSDYKE DENLKTEYFG KTESNIEALW NKVKEEKVKG ADPEDPSKES
KISDLNTEEQ LQRVLDYYAV ATMLKLAKQA EDIAKLETEI ADQRGKSPEA ECNKITEEPK
CSEEKICSWH KEVKAGEKNC QFNSTKASKS GVPVTQTQTA GADTTAEKCK GKGEKDCKSP
DCKWEGGTCK DSSILANKQF ALSVASAAFV ALLF
