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Reviewed, UniProtKB/Swiss-Prot P12244 (GSBP_CHICK)

Last modified February 9, 2010. Version 85. 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:
    Dolichyl-diphosphooligosaccharide--protein glycotransferase
    EC=2.4.1.119
Alternative name(s):
    Glycosylation site-binding chain
      Short name=GSBP
OrganismGallus gallus (Chicken)
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

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Protein attributes

Sequence length508 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

Transfers the polysaccharide side-chains of glycoproteins to an asparagine residue of Asn-X-Ser/Thr sites in nascent proteins.

Catalytic activity

Dolichyl diphosphooligosaccharide + protein L-asparagine = dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-glycosyl linkage to protein L-asparagine.

Subcellular location

Endoplasmic reticulum lumen.

Sequence similarities

Belongs to the protein disulfide isomerase family.

Contains 2 thioredoxin domains.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Chain18 – 508491Dolichyl-diphosphooligosaccharide--protein glycotransferase
PRO_0000034201

Regions

Domain18 – 133116Thioredoxin 1
Domain333 – 496164Thioredoxin 2
Motif505 – 5084Prevents secretion from ER

Sites

Active site521Nucleophile By similarity
Active site551Nucleophile By similarity
Active site3981Nucleophile By similarity
Active site4011Nucleophile By similarity
Site531Contributes to redox potential value By similarity
Site541Contributes to redox potential value By similarity
Site1191Lowers pKa of C-terminal Cys of first active site By similarity
Site3991Contributes to redox potential value By similarity
Site4001Contributes to redox potential value By similarity
Site4621Lowers pKa of C-terminal Cys of second active site By similarity

Amino acid modifications

Disulfide bond52 ↔ 55Redox-active By similarity
Disulfide bond398 ↔ 401Redox-active By similarity

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Sequences

Sequence LengthMass (Da)Tools
P12244-1 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: D2BA0E5872BE58BE

FASTA50856,892
        10         20         30         40         50         60 
MLRALCALAW RVARVGADAE EQDNVLVAKK SNFLEPLAAH SYLAVEFYAP LCGHCKALAP 

        70         80         90        100        110        120 
DYAKAGGKLK AEGSEIKAAK VEATEESDLA QQYGVRAYPT IKFFKNGDTA SPKEYTAGRE 

       130        140        150        160        170        180 
ADDIVNWLKK RTGPAATTLS DTAAAESLVD SSEITVIIGF FKDPGSDSAR QFLLAADAVD 

       190        200        210        220        230        240 
DVPFGINSNS DVYSKYQMDK DAVVLFKKFA EGRNNFEGEI TKEKLLDFIK HNNLPLVIEF 

       250        260        270        280        290        300 
TEQTAPKIFG GEIKTHILLF LPKSVSDYDG KLSNLKKAAD GFKGKILFVF IDSDHTDNQR 

       310        320        330        340        350        360 
ILEFFGLKKE ECPAVRLITL DEELTKYKPE TEELTAEKLT QFCHHFLEGK IKPHLMSNEP 

       370        380        390        400        410        420 
LPEDWDKQPV KVLVGKNYEE VAFDEKKNVF IEFYAPWCGH CKQLAPMWDR LGEAYKDDEN 

       430        440        450        460        470        480 
IVIAKMESTA NEVEAIKVHS FPTLKFFPAS AERTVIDYNG ERTLDGYKKF LESGGQDGYG 

       490        500 
NNDDDDLEEA LESDMEEDED QKAMKDEL

« Hide

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References

[1]"Glycosylation site binding protein, a component of oligosaccharyl transferase, is highly similar to three other 57 kd luminal proteins of the ER."
Geetha-Habib M., Noiva R., Kaplan H.A., Lennarz W.J.
Cell 54:1053-1060(1988) [PubMed: 2458190] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M22594 mRNA. Translation: AAA64295.1.
IPIIPI00597613.
PIRA30007.
RefSeqNP_990739.1.
UniGeneGga.785

3D structure databases

SMRP12244. Positions 17-474, 370-501.
ModBaseSearch...

Proteomic databases

PRIDEP12244.

Genome annotation databases

GeneID396376.
KEGGgga:396376.

Organism-specific databases

CTD396376.

Phylogenomic databases

HOVERGENP12244.
PhylomeDBP12244.

Enzyme and pathway databases

BRENDA2.4.1.119. 4.

Family and domain databases

InterProIPR005788. Disulphide_isomerase.
IPR005792. Prot_disulphide_isomerase.
IPR017936. Thioredoxin-like.
IPR012336. Thioredoxin-like_fold.
IPR006662. Thioredoxin-like_subdom.
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]
PRINTSPR00421. THIOREDOXIN.
TIGRFAMsTIGR01130. ER_PDI_fam. 1 hit.
TIGR01126. pdi_dom. 2 hits.
PROSITEPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameGSBP_CHICK
AccessionPrimary (citable) accession number: P12244
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: February 1, 1996
Last modified: February 9, 2010
This is version 85 of the entry and version 2 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