ID   VSWA_TRYBR              Reviewed;         471 AA.
AC   P20946;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Variant surface glycoprotein WRATAT A;
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; M33823; AAA30316.1; -; mRNA.
DR   PIR; A35480; A35480.
DR   AlphaFoldDB; P20946; -.
DR   SMR; P20946; -.
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; IPR027446; VSG_C_dom_sf.
DR   Pfam; PF13206; VSG_B; 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..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..454
FT                   /note="Variant surface glycoprotein WRATAT A"
FT                   /id="PRO_0000036447"
FT   PROPEP          455..471
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000036448"
FT   REGION          373..457
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        373..398
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        399..445
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           454
FT                   /note="GPI-anchor amidated serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        61
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        133
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        449
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        401..414
FT                   /evidence="ECO:0000250"
FT   DISULFID        410..427
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   471 AA;  50537 MW;  57ECC0821042376D CRC64;
     MSVLFLLLAI TRTASVKAAE GDQAADFLPL CEAWQATKAL ANAAYKLPPF PPDLTDILNF
     NITVAPEEWK AIFTDGGSDN TWERFAEGHK NTLNGGNWKT RWEHIKQARQ DTKEASSPWN
     ALNSKLINTA TVNTTRAYIA SIADEAFDLY QGTQTPLQTP KALEAASLAE AAKAILCSDP
     LKPTADGQAC TDITATPSKA ATCPTGRSSK GGAPIGLDTV CLCSTNKPSM HSRRRKAAAV
     MTDGQLKDGI LKKLLAACPK KPTLNEPAAA ARHAVTVLAT RLAQKVARAE EGQIILGTRA
     ETDCASSGSA CVEYTNFFKD GDGLAAVPWV KKLLAAADFY DTIEKRKESD KNAATAIAAL
     KSALIREFRR PGQEQTLATT GTKSSSPQST QQKASEAEAN CNDKAKETEC NSPCKWDKEE
     KDEKKRCKLS EEGKQAEKEN QEGKDGKANT TGSSNSFVIK TSPLLLAVLL L