ID   BS2_TRYBB               Reviewed;         497 AA.
AC   P12865;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   09-APR-2025, entry version 114.
DE   RecName: Full=Bloodstream-specific protein 2;
DE   Flags: Precursor;
GN   Name=BS2;
OS   Trypanosoma brucei brucei.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=5702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2551375; DOI=10.1021/bi00441a042;
RA   Hsu M.P., Muhich M.L., Boothroyd J.C.;
RT   "A developmentally regulated gene of trypanosomes encodes a homologue of
RT   rat protein-disulfide isomerase and phosphoinositol-phospholipase C.";
RL   Biochemistry 28:6440-6446(1989).
CC   -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC       {ECO:0000305}.
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DR   EMBL; J02865; AAA30168.1; -; Genomic_DNA.
DR   PIR; A32820; A32820.
DR   AlphaFoldDB; P12865; -.
DR   SMR; P12865; -.
DR   GlyCosmos; P12865; 13 sites, No reported glycans.
DR   BRENDA; 5.3.4.1; 6519.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:TreeGrafter.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:TreeGrafter.
DR   GO; GO:0034976; P:response to endoplasmic reticulum stress; IEA:TreeGrafter.
DR   CDD; cd02961; PDI_a_family; 1.
DR   CDD; cd02995; PDI_a_PDI_a'_C; 1.
DR   CDD; cd02982; PDI_b'_family; 1.
DR   CDD; cd02981; PDI_b_family; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 4.
DR   InterPro; IPR005788; PDI_thioredoxin-like_dom.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   NCBIfam; TIGR01126; pdi_dom; 1.
DR   PANTHER; PTHR18929; PROTEIN DISULFIDE ISOMERASE; 1.
DR   PANTHER; PTHR18929:SF246; PROTEIN DISULFIDE ISOMERASE-LIKE 1-4; 1.
DR   Pfam; PF00085; Thioredoxin; 2.
DR   Pfam; PF13848; Thioredoxin_6; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 4.
DR   PROSITE; PS00194; THIOREDOXIN_1; 2.
DR   PROSITE; PS51352; THIOREDOXIN_2; 2.
PE   3: Inferred from homology;
KW   Disulfide bond; Glycoprotein; Isomerase; Redox-active center; Repeat;
KW   Signal.
FT   SIGNAL          1..14
FT                   /evidence="ECO:0000255"
FT   CHAIN           15..497
FT                   /note="Bloodstream-specific protein 2"
FT                   /id="PRO_0000034246"
FT   DOMAIN          15..124
FT                   /note="Thioredoxin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DOMAIN          334..455
FT                   /note="Thioredoxin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   REGION          461..497
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        467..480
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        481..490
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        378
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        381
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   SITE            379
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            380
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            441
FT                   /note="Lowers pKa of C-terminal Cys of second active site"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        30
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        63
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        85
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        153
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        154
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        250
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        278
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        413
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        465
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        476
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        482
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        485
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        488
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        48..51
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        378..381
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   497 AA;  55579 MW;  8AE6C44D762B67EB CRC64;
     MRAIFLVALA LATMRESTAE SLKLTKENFN ETIAKSEIFL VKFYVDTCGY CQMLAPEWEK
     AANETIDNAL MGEVDCHSQP ELAANFSIRG YPTIILFRNG KEAEHYGGAR TKDDIIKYIK
     ANVGPAVTPA SNAEEVTRAK EEHDVVCVGL TANNSTSLST TLAEAAQSFR VSLKFFEAEP
     KLFPDEKPET IVVYRKGGEK EVYDGPMEVE KLTEFLQISR VAFGGEITPE NYQYYSVIKR
     PVGWAMVKPN ETASIELKES LTEVGKKMRS HMVVLWVNIS KHPVWRDFGV PEDAKYPAFL
     AIHWGANYLH STAEVVTRES LEKFILEFAA GRVEPTIKSL PVPEVETVDG KTTIVAKTMQ
     KHLTSGKDML ILFFAPWCGH CKNFAPTFDK IAKEFDATDL IVAELDATAN YVNSSTFTVT
     AFPTVFFVPN GGKPVVFEGE RSFENVYEFV RKHVTTFKVS EKPANVTEEK KSEEENKSSK
     SNESNDSNES NVDKQDL
//