VSM1_TRYBB
ID VSM1_TRYBB Reviewed; 492 AA.
AC P26331;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Variant surface glycoprotein MITAT 1.1;
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 060;
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; X56761; CAA40080.1; -; mRNA.
DR PIR; S18445; S18445.
DR PDB; 5LY9; X-ray; 1.65 A; A/B=33-400.
DR PDB; 5M4T; NMR; -; A=404-475.
DR PDBsum; 5LY9; -.
DR PDBsum; 5M4T; -.
DR AlphaFoldDB; P26331; -.
DR BMRB; P26331; -.
DR SMR; P26331; -.
DR ABCD; P26331; 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; IPR027446; VSG_C_dom_sf.
DR Pfam; PF00913; Trypan_glycop; 1.
DR SUPFAM; SSF118251; SSF118251; 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..32
FT CHAIN 33..475
FT /note="Variant surface glycoprotein MITAT 1.1"
FT /id="PRO_0000036431"
FT PROPEP 476..492
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000036432"
FT LIPID 475
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 471
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 47..177
FT /evidence="ECO:0000250"
FT DISULFID 155..222
FT /evidence="ECO:0000250"
FT HELIX 40..53
FT /evidence="ECO:0007829|PDB:5LY9"
FT HELIX 56..87
FT /evidence="ECO:0007829|PDB:5LY9"
FT HELIX 94..117
FT /evidence="ECO:0007829|PDB:5LY9"
FT HELIX 119..146
FT /evidence="ECO:0007829|PDB:5LY9"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:5LY9"
FT STRAND 155..160
FT /evidence="ECO:0007829|PDB:5LY9"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:5LY9"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:5LY9"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:5LY9"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:5LY9"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:5LY9"
FT STRAND 232..237
FT /evidence="ECO:0007829|PDB:5LY9"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:5LY9"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:5LY9"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:5LY9"
FT STRAND 254..257
FT /evidence="ECO:0007829|PDB:5LY9"
FT HELIX 271..274
FT /evidence="ECO:0007829|PDB:5LY9"
FT HELIX 276..286
FT /evidence="ECO:0007829|PDB:5LY9"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:5LY9"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:5LY9"
FT HELIX 307..316
FT /evidence="ECO:0007829|PDB:5LY9"
FT HELIX 327..336
FT /evidence="ECO:0007829|PDB:5LY9"
FT STRAND 337..340
FT /evidence="ECO:0007829|PDB:5LY9"
FT HELIX 341..344
FT /evidence="ECO:0007829|PDB:5LY9"
FT HELIX 345..353
FT /evidence="ECO:0007829|PDB:5LY9"
FT HELIX 360..362
FT /evidence="ECO:0007829|PDB:5LY9"
FT HELIX 369..371
FT /evidence="ECO:0007829|PDB:5LY9"
FT HELIX 375..399
FT /evidence="ECO:0007829|PDB:5LY9"
FT HELIX 409..420
FT /evidence="ECO:0007829|PDB:5M4T"
FT TURN 421..424
FT /evidence="ECO:0007829|PDB:5M4T"
FT HELIX 426..432
FT /evidence="ECO:0007829|PDB:5M4T"
FT HELIX 433..435
FT /evidence="ECO:0007829|PDB:5M4T"
FT STRAND 437..440
FT /evidence="ECO:0007829|PDB:5M4T"
FT TURN 441..444
FT /evidence="ECO:0007829|PDB:5M4T"
FT STRAND 445..448
FT /evidence="ECO:0007829|PDB:5M4T"
FT HELIX 450..457
FT /evidence="ECO:0007829|PDB:5M4T"
FT STRAND 461..464
FT /evidence="ECO:0007829|PDB:5M4T"
SQ SEQUENCE 492 AA; 53272 MW; 05A97474D88DD10D CRC64;
MATGRAKNTK WARWLSTAGL IIVVTLPATT MAAERTGLKA TAWKPLCKLT TELSKVSGEM
LNKGQEVISN IQKIKAAEYK VSIYLAKNPE TQALQQSTLL RGYFARKTNG GLESYKTMGL
ATQIRSARAA AYLKGSIDEF LNLLESLKGG SENKCLVTTN ADTAATRRET KLDDQECALS
MPETKPEAAT RTELTQTGYP NLQHGGGGTA NTFQPTTSTG TCKLLSGHST NGYPTTSALD
TTAKVLAGYM TIPNTQVEAT LANMQAMGNG HKATAPAWHE AWEARNREAK AKDLAYTNET
GNLDTQPTLK ALVKTLLLPK DNTEHNAEAT KLEALFGGLA ADKTKTYLDM VDAEIIPAGI
AGRTTEAPLG KIHDTVELGD ILSNYEMIAA QNVVTLKKNL DAVSKKQQTE SAENKEKICN
AAKDNQKACE NLKEKGCVFN TESNKCELKK DVKEKLEKES KETEGKDEKA NTTGSNSFLI
HKAPLLLAFL LF
