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 27-MAR-2024, entry version 109.
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:0003756; F:protein disulfide isomerase activity; IEA:InterPro.
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; 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 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
//
