ID   Q95PJ2_TRYBB            Unreviewed;       127 AA.
AC   Q95PJ2;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   SubName: Full=Surface protein EP2-1 procyclin {ECO:0000313|EMBL:AAK62890.1};
GN   Name=EP2-1 {ECO:0000313|EMBL:AAK62890.1};
OS   Trypanosoma brucei brucei.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=5702 {ECO:0000313|EMBL:AAK62890.1};
RN   [1] {ECO:0000313|EMBL:AAK62890.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=AnTat 1.1 {ECO:0000313|EMBL:AAK62890.1};
RX   PubMed=11575917; DOI=10.1006/jmbi.2001.5004;
RA   Vassella E., Acosta-Serrano A., Studer E., Lee S.H., Englund P.T.,
RA   Roditi I.;
RT   "Multiple procyclin isoforms are expressed differentially during the
RT   development of insect forms of Trypanosoma brucei.";
RL   J. Mol. Biol. 312:597-607(2001).
RN   [2] {ECO:0000313|EMBL:AAK62890.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=AnTat 1.1 {ECO:0000313|EMBL:AAK62890.1};
RX   PubMed=11171982; DOI=10.1073/pnas.041611698;
RA   Acosta-Serrano A., Vassella E., Liniger M., Kunz Renggli C., Brun R.,
RA   Roditi I., Englund P.T.;
RT   "The surface coat of procyclic Trypanosoma brucei: programmed expression
RT   and proteolytic cleavage of procyclin in the tsetse fly.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:1513-1518(2001).
CC   -!- FUNCTION: Major surface antigen of procyclic forms.
CC       {ECO:0000256|ARBA:ARBA00003078}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609};
CC       Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor
CC       {ECO:0000256|ARBA:ARBA00004589}.
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DR   EMBL; AF353627; AAK62890.1; -; Genomic_DNA.
DR   PIR; S09372; S09372.
DR   AlphaFoldDB; Q95PJ2; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR008882; Trypano_PARP.
DR   Pfam; PF05887; Trypan_PARP; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Cyclin {ECO:0000313|EMBL:AAK62890.1};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00022622};
KW   GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Membrane {ECO:0000256|ARBA:ARBA00022622};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..127
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004321251"
FT   REGION          27..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..55
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        56..100
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   127 AA;  13378 MW;  F96879394C4ED3F1 CRC64;
     MAPRSLYLLA VLLFSANLFA GVGFAAAAEG PEDKGLTKGG KGKGEKETKV QDEVEPEPEP
     EPEPEPEPEP EPEPEPEPEP EPEPEPEPEP EPEPEPEPEP EPEPGAATLK SVALPFAIAA
     VGLVAAF
//