VSM2_TRYBB
ID VSM2_TRYBB Reviewed; 476 AA.
AC P26332;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Variant surface glycoprotein MITAT 1.2;
DE AltName: Full=VSG 221;
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 221;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 1-59 AND 452-476.
RX PubMed=6272213; DOI=10.1093/nar/9.18.4735;
RA Boothroyd J.C., Paynter C.A., Cross G.A.M., Bernards A., Borst P.;
RT "Variant surface glycoproteins of Trypanosoma brucei are synthesised with
RT cleavable hydrophobic sequences at the carboxy and amino termini.";
RL Nucleic Acids Res. 9:4735-4743(1981).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
RX PubMed=6692467; DOI=10.1016/0092-8674(84)90085-0;
RA Bernards A., de Lange T., Michels P.A.M., Liu A.Y.C., Huisman M.J.,
RA Borst P.;
RT "Two modes of activation of a single surface antigen gene of Trypanosoma
RT brucei.";
RL Cell 36:163-170(1984).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 27-390.
RX PubMed=2231728; DOI=10.1016/s0022-2836(05)80066-x;
RA Freymann D., Down J., Carrington M., Roditi I., Turner M.J., Wiley D.C.;
RT "2.9-A resolution structure of the N-terminal domain of a variant surface
RT glycoprotein from Trypanosoma brucei.";
RL J. Mol. Biol. 216:141-160(1990).
RN [5]
RP STRUCTURE BY NMR OF 385-459, AND DISULFIDE BONDS.
RX PubMed=15557330; DOI=10.1074/jbc.m410787200;
RA Chattopadhyay A., Jones N.G., Nietlispach D., Nielsen P.R., Voorheis H.P.,
RA Mott H.R., Carrington M.;
RT "Structure of the C-terminal domain from Trypanosoma brucei variant surface
RT glycoprotein MITat1.2.";
RL J. Biol. Chem. 280:7228-7235(2005).
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 -!- SUBUNIT: Homodimer.
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; X56762; CAA40081.1; -; mRNA.
DR EMBL; K00640; AAA30276.1; -; mRNA.
DR EMBL; K01290; AAA30275.1; -; Genomic_DNA.
DR EMBL; K00641; AAA30277.1; -; mRNA.
DR PIR; S18451; S18451.
DR PDB; 1VSG; X-ray; 2.90 A; A/B=27-390.
DR PDB; 1XU6; NMR; -; A=385-459.
DR PDB; 7AQX; X-ray; 1.50 A; A/B=27-390.
DR PDB; 7AQY; X-ray; 1.90 A; A/B=27-390.
DR PDB; 7AQZ; X-ray; 1.30 A; A/B=27-390.
DR PDB; 7AR0; X-ray; 2.14 A; A=27-390.
DR PDBsum; 1VSG; -.
DR PDBsum; 1XU6; -.
DR PDBsum; 7AQX; -.
DR PDBsum; 7AQY; -.
DR PDBsum; 7AQZ; -.
DR PDBsum; 7AR0; -.
DR AlphaFoldDB; P26332; -.
DR SMR; P26332; -.
DR EvolutionaryTrace; P26332; -.
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..26
FT CHAIN 27..459
FT /note="Variant surface glycoprotein MITAT 1.2"
FT /id="PRO_0000036433"
FT PROPEP 460..476
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000036434"
FT REGION 389..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 459
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 454
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 41..171
FT /evidence="ECO:0000269|PubMed:15557330"
FT DISULFID 149..213
FT /evidence="ECO:0000269|PubMed:15557330"
FT DISULFID 407..419
FT /evidence="ECO:0000269|PubMed:15557330"
FT DISULFID 415..430
FT /evidence="ECO:0000269|PubMed:15557330"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:7AQZ"
FT HELIX 34..47
FT /evidence="ECO:0007829|PDB:7AQZ"
FT HELIX 50..82
FT /evidence="ECO:0007829|PDB:7AQZ"
FT HELIX 86..111
FT /evidence="ECO:0007829|PDB:7AQZ"
FT HELIX 113..140
FT /evidence="ECO:0007829|PDB:7AQZ"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:7AQZ"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:7AQZ"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:7AQZ"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:7AQZ"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:7AQZ"
FT HELIX 202..205
FT /evidence="ECO:0007829|PDB:7AQZ"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:7AQZ"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:7AQZ"
FT TURN 220..222
FT /evidence="ECO:0007829|PDB:7AQZ"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:7AQZ"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:7AQZ"
FT TURN 237..240
FT /evidence="ECO:0007829|PDB:7AQZ"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:7AQZ"
FT STRAND 245..248
FT /evidence="ECO:0007829|PDB:7AQZ"
FT HELIX 267..277
FT /evidence="ECO:0007829|PDB:7AQZ"
FT HELIX 285..287
FT /evidence="ECO:0007829|PDB:7AQZ"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:1VSG"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:1VSG"
FT HELIX 300..307
FT /evidence="ECO:0007829|PDB:7AQZ"
FT HELIX 316..327
FT /evidence="ECO:0007829|PDB:7AQZ"
FT STRAND 328..331
FT /evidence="ECO:0007829|PDB:7AQZ"
FT HELIX 332..344
FT /evidence="ECO:0007829|PDB:7AQZ"
FT HELIX 349..351
FT /evidence="ECO:0007829|PDB:7AQZ"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:7AQY"
FT HELIX 360..362
FT /evidence="ECO:0007829|PDB:7AQZ"
FT HELIX 366..387
FT /evidence="ECO:0007829|PDB:7AQZ"
FT HELIX 404..409
FT /evidence="ECO:0007829|PDB:1XU6"
FT TURN 412..414
FT /evidence="ECO:0007829|PDB:1XU6"
FT STRAND 425..427
FT /evidence="ECO:0007829|PDB:1XU6"
FT HELIX 434..441
FT /evidence="ECO:0007829|PDB:1XU6"
FT STRAND 443..447
FT /evidence="ECO:0007829|PDB:1XU6"
FT STRAND 454..457
FT /evidence="ECO:0007829|PDB:1XU6"
SQ SEQUENCE 476 AA; 51042 MW; D8CF719A995B9D5D CRC64;
MPSNQEARLF LAVLVLAQVL PILVDSAAEK GFKQAFWQPL CQVSEELDDQ PKGALFTLQA
AASKIQKMRD AALRASIYAE INHGTNRAKA AVIVANHYAM KADSGLEALK QTLSSQEVTA
TATASYLKGR IDEYLNLLLQ TKESGTSGCM MDTSGTNTVT KAGGTIGGVP CKLQLSPIQP
KRPAATYLGK AGYVGLTRQA DAANNFHDND AECRLASGHN TNGLGKSGQL SAAVTMAAGY
VTVANSQTAV TVQALDALQE ASGAAHQPWI DAWKAKKALT GAETAEFRNE TAGIAGKTGV
TKLVEEALLK KKDSEASEIQ TELKKYFSGH ENEQWTAIEK LISEQPVAQN LVGDNQPTKL
GELEGNAKLT TILAYYRMET AGKFEVLTQK HKPAESQQQA AETEGSCNKK DQNECKSPCK
WHNDAENKKC TLDKEEAKKV ADETAKDGKT GNTNTTGSSN SFVISKTPLW LAVLLF
