VSI3_TRYBB
ID VSI3_TRYBB Reviewed; 532 AA.
AC P26328;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=Variant surface glycoprotein ILTAT 1.23;
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 206;
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; X56768; CAA40087.1; -; mRNA.
DR PIR; S18448; S18448.
DR AlphaFoldDB; P26328; -.
DR SMR; P26328; -.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR025932; Trypano_VSG_B_N_dom.
DR InterPro; IPR019609; Variant_surf_glycoprt_trypan_C.
DR InterPro; IPR027446; VSG_C_dom_sf.
DR Pfam; PF10659; Trypan_glycop_C; 1.
DR Pfam; PF13206; VSG_B; 1.
DR SUPFAM; SSF118251; SSF118251; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; GPI-anchor; Lipoprotein; Membrane; Signal;
KW Trypanosomiasis.
FT SIGNAL 1..23
FT CHAIN 24..509
FT /note="Variant surface glycoprotein ILTAT 1.23"
FT /id="PRO_0000036421"
FT PROPEP 510..532
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000036422"
FT REGION 79..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..442
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..504
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 509
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 66
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 509
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 532 AA; 56779 MW; EED0D72C919396E6 CRC64;
MFKNINAAVL LLILSTRNDY ANAAAGDNEN LFLDLCNLLE LGKRAVSKLA PTNLGELAYS
EIQKLNMSLS DDAWKAKFAP KKGKQENSNN ADGAPRSQEK THARNHAWRQ AATDLAGDEG
DKPTLRLAGL EAVTQVEKLQ YLSALQPLAE RAAAILEQLK TLHSGSAGLT DTNIRQEIQT
ALYGTGATAP EKTTLQLLKG KGNVGSTRKD ICGQDNTAAK ADTVLAYLFC ICAGHATDSG
GAIKVCSQTQ PANNKADADV SDAHTHAAAL AGQCHGSDTT NDIKAAEIDS AILEFTSKLK
AANQKPYFGK YSATGCTGSD AEGICVMFKT TAKGEGKAVK QIPWVLTLHN AAEMIRKQQA
VNGKIDSLNQ ELQAIQTAAY ALKPQLEMYK RLQQTTEKAR PGKQLTEMQA GECNTHKSNS
TCPKNNCKWE EKDGKDGKCV ADDSKVTTQG NAPAGAGDGT AGTTTTPNCA SHTDKTKCEE
ENKGKTTPVC GWRKGKEGES DQDKEMCRNG SFLAKKKFAL SVVSAAFTAL LF