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Reviewed, UniProtKB/Swiss-Prot P12865 (BS2_TRYBB)

Last modified June 16, 2009. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Bloodstream-specific protein 2
Gene names
Name: BS2
OrganismTrypanosoma brucei brucei
Taxonomic identifier5702 [NCBI]
Taxonomic lineageEukaryota › Euglenozoa › Kinetoplastida › Trypanosomatidae › Trypanosoma

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Protein attributes

Sequence length497 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology.

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General annotation (Comments)

Sequence similarities

Belongs to the protein disulfide isomerase family.

Contains 2 thioredoxin domains.

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Ontologies

Keywords
   DomainRedox-active center
Repeat
Signal
   Molecular functionIsomerase
   PTMDisulfide bond
Glycoprotein
Gene Ontology (GO)
   Biological processcell redox homeostasis

Inferred from electronic annotation. Source: InterPro

   Molecular functionisomerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1414 Potential
Chain15 – 497483Bloodstream-specific protein 2
PRO_0000034246

Regions

Domain15 – 124110Thioredoxin 1
Domain334 – 455122Thioredoxin 2

Sites

Active site3781Nucleophile By similarity
Active site3811Nucleophile By similarity
Site3791Contributes to redox potential value By similarity
Site3801Contributes to redox potential value By similarity
Site4411Lowers pKa of C-terminal Cys of second active site By similarity

Amino acid modifications

Glycosylation301N-linked (GlcNAc...) Potential
Glycosylation631N-linked (GlcNAc...) Potential
Glycosylation851N-linked (GlcNAc...) Potential
Glycosylation1531N-linked (GlcNAc...) Potential
Glycosylation1541N-linked (GlcNAc...) Potential
Glycosylation2501N-linked (GlcNAc...) Potential
Glycosylation2781N-linked (GlcNAc...) Potential
Glycosylation4131N-linked (GlcNAc...) Potential
Glycosylation4651N-linked (GlcNAc...) Potential
Glycosylation4761N-linked (GlcNAc...) Potential
Glycosylation4821N-linked (GlcNAc...) Potential
Glycosylation4851N-linked (GlcNAc...) Potential
Glycosylation4881N-linked (GlcNAc...) Potential
Disulfide bond48 ↔ 51Redox-active By similarity
Disulfide bond378 ↔ 381Redox-active By similarity

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Sequences

Sequence LengthMass (Da)Tools
P12865-1 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: 8AE6C44D762B67EB

FASTA49755,579
        10         20         30         40         50         60 
MRAIFLVALA LATMRESTAE SLKLTKENFN ETIAKSEIFL VKFYVDTCGY CQMLAPEWEK 

        70         80         90        100        110        120 
AANETIDNAL MGEVDCHSQP ELAANFSIRG YPTIILFRNG KEAEHYGGAR TKDDIIKYIK 

       130        140        150        160        170        180 
ANVGPAVTPA SNAEEVTRAK EEHDVVCVGL TANNSTSLST TLAEAAQSFR VSLKFFEAEP 

       190        200        210        220        230        240 
KLFPDEKPET IVVYRKGGEK EVYDGPMEVE KLTEFLQISR VAFGGEITPE NYQYYSVIKR 

       250        260        270        280        290        300 
PVGWAMVKPN ETASIELKES LTEVGKKMRS HMVVLWVNIS KHPVWRDFGV PEDAKYPAFL 

       310        320        330        340        350        360 
AIHWGANYLH STAEVVTRES LEKFILEFAA GRVEPTIKSL PVPEVETVDG KTTIVAKTMQ 

       370        380        390        400        410        420 
KHLTSGKDML ILFFAPWCGH CKNFAPTFDK IAKEFDATDL IVAELDATAN YVNSSTFTVT 

       430        440        450        460        470        480 
AFPTVFFVPN GGKPVVFEGE RSFENVYEFV RKHVTTFKVS EKPANVTEEK KSEEENKSSK 

       490 
SNESNDSNES NVDKQDL

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References

[1]"A developmentally regulated gene of trypanosomes encodes a homologue of rat protein-disulfide isomerase and phosphoinositol-phospholipase C."
Hsu M.P., Muhich M.L., Boothroyd J.C.
Biochemistry 28:6440-6446(1989) [PubMed: 2551375] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

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Cross-references

Sequence databases

J02865 Genomic DNA. Translation: AAA30168.1.
PIRA32820.

3D structure databases

HSSPHSSP built from PDB template 1MEK based on UniProtKB P07237.
ModBaseSearch...

Enzyme and pathway databases

BRENDA5.3.4.1. 409.

Family and domain databases

InterProIPR005788. Disulphide_isomerase.
IPR017936. Thioredoxin-like.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
IPR012335. Thioredoxin_fold.
[Graphical view]
Gene3DG3DSA:3.40.30.10. Thioredoxin_fold. 2 hits.
PfamPF00085. Thioredoxin. 2 hits.
[Graphical view]
TIGRFAMsTIGR01126. pdi_dom. 2 hits.
PROSITEPS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameBS2_TRYBB
AccessionPrimary (citable) accession number: P12865
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: June 16, 2009
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents