ID   VSM5_TRYBR              Reviewed;         517 AA.
AC   P21840;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Variant surface glycoprotein MVAT5;
DE            Short=VSG;
DE   Flags: Precursor;
OS   Trypanosoma brucei rhodesiense.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=31286;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=WRATat 1;
RX   PubMed=2357229; DOI=10.1016/0006-291x(90)90392-z;
RA   Reddy L.V., Hall T., Donelson J.E.;
RT   "Sequences of three VSG mRNAs expressed in a mixed population of
RT   Trypanosoma brucei rhodesiense.";
RL   Biochem. Biophys. Res. Commun. 169:730-736(1990).
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; M33825; AAA30216.1; -; mRNA.
DR   PIR; C35480; C35480.
DR   AlphaFoldDB; P21840; -.
DR   SMR; P21840; -.
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   InterPro; IPR027446; VSG_C_dom_sf.
DR   Pfam; PF00913; Trypan_glycop; 1.
DR   Pfam; PF10659; Trypan_glycop_C; 1.
DR   SUPFAM; SSF118251; SSF118251; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; Lipoprotein;
KW   Membrane; Signal; Trypanosomiasis.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..495
FT                   /note="Variant surface glycoprotein MVAT5"
FT                   /id="PRO_0000036451"
FT   PROPEP          496..517
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000036452"
FT   REGION          454..487
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        469..487
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           495
FT                   /note="GPI-anchor amidated aspartate"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        435
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        417..430
FT                   /evidence="ECO:0000250"
FT   DISULFID        426..443
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   517 AA;  54191 MW;  521A1FE353887482 CRC64;
     MIGKAFIILS LLNELPTPTA AQAAQGGALG KDVWLPLAKF TATAAKIPGR AAKLLQDRSA
     QIVNLMKLQV QADICLNKAA SEVSALGWQA LAVAIAADIG SLQSLQQQRS EEAIAAAAAA
     EFARGHAAEF FKVAAAVQSA ANSGCLTTNN KGGAAGSVIN GFSTLGTAEQ PAIGATSTAH
     VGDDITAITT TGFSDLAATD GIRTDSLTAD TNCVLFKGGS DGPLTTANFG QSIPFAGGYL
     TRNPTANTAS SADGTDFVSN PEDSKIAGIK VYRDAHAAAA KIRTAATFGS TFTDFKKLDQ
     AKKSVHLRAA VKNIILGKPD GSVDDLSGEI DTKINQVFGE DQETFHSRFW DQLTKVKVEK
     AASGQEETTL DAITSFAALS RARTYYSTKV IKGLRDKISS LEIKNSKTEV KVTDADCNKH
     QSKDKCAAPC KWNENTTDIN KKCSLDPVKA TEQQAAQTAG AGEGAAGTTT DKCKDKKKDD
     CKSPDCKWEG ETCKDSSILL NKQFALMVSA AFVALLF