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Protein

Dolichyl-diphosphooligosaccharide--protein glycotransferase

Gene
N/A
Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

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

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei52 – 521NucleophileBy similarity
Sitei53 – 531Contributes to redox potential valueBy similarity
Sitei54 – 541Contributes to redox potential valueBy similarity
Active sitei55 – 551NucleophileBy similarity
Sitei119 – 1191Lowers pKa of C-terminal Cys of first active siteBy similarity
Active sitei398 – 3981NucleophileBy similarity
Sitei399 – 3991Contributes to redox potential valueBy similarity
Sitei400 – 4001Contributes to redox potential valueBy similarity
Active sitei401 – 4011NucleophileBy similarity
Sitei462 – 4621Lowers pKa of C-terminal Cys of second active siteBy similarity

GO - Molecular functioni

  1. isomerase activity Source: InterPro
  2. transferase activity Source: UniProtKB-KW

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Names & Taxonomyi

Protein namesi
Recommended name:
Dolichyl-diphosphooligosaccharide--protein glycotransferase (EC:2.4.99.18)
Alternative name(s):
Glycosylation site-binding chain
Short name:
GSBP
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum lumen Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence AnalysisAdd
BLAST
Chaini18 – 508491Dolichyl-diphosphooligosaccharide--protein glycotransferasePRO_0000034201Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi52 ↔ 55Redox-activePROSITE-ProRule annotation
Disulfide bondi398 ↔ 401Redox-activePROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP12244.

Structurei

3D structure databases

ProteinModelPortaliP12244.
SMRiP12244. Positions 20-136, 369-472.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini18 – 133116Thioredoxin 1PROSITE-ProRule annotationAdd
BLAST
Domaini333 – 496164Thioredoxin 2PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi505 – 5084Prevents secretion from ER

Sequence similaritiesi

Belongs to the protein disulfide isomerase family.Curated
Contains 2 thioredoxin domains.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center, Repeat, Signal

Phylogenomic databases

HOVERGENiHBG005920.
KOiK09580.
PhylomeDBiP12244.

Family and domain databases

Gene3Di3.40.30.10. 4 hits.
InterProiIPR005792. Prot_disulphide_isomerase.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00085. Thioredoxin. 2 hits.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 4 hits.
TIGRFAMsiTIGR01130. ER_PDI_fam. 1 hit.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P12244-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRALCALAW RVARVGADAE EQDNVLVAKK SNFLEPLAAH SYLAVEFYAP
60 70 80 90 100
LCGHCKALAP DYAKAGGKLK AEGSEIKAAK VEATEESDLA QQYGVRAYPT
110 120 130 140 150
IKFFKNGDTA SPKEYTAGRE ADDIVNWLKK RTGPAATTLS DTAAAESLVD
160 170 180 190 200
SSEITVIIGF FKDPGSDSAR QFLLAADAVD DVPFGINSNS DVYSKYQMDK
210 220 230 240 250
DAVVLFKKFA EGRNNFEGEI TKEKLLDFIK HNNLPLVIEF TEQTAPKIFG
260 270 280 290 300
GEIKTHILLF LPKSVSDYDG KLSNLKKAAD GFKGKILFVF IDSDHTDNQR
310 320 330 340 350
ILEFFGLKKE ECPAVRLITL DEELTKYKPE TEELTAEKLT QFCHHFLEGK
360 370 380 390 400
IKPHLMSNEP LPEDWDKQPV KVLVGKNYEE VAFDEKKNVF IEFYAPWCGH
410 420 430 440 450
CKQLAPMWDR LGEAYKDDEN IVIAKMESTA NEVEAIKVHS FPTLKFFPAS
460 470 480 490 500
AERTVIDYNG ERTLDGYKKF LESGGQDGYG NNDDDDLEEA LESDMEEDED

QKAMKDEL
Length:508
Mass (Da):56,892
Last modified:February 1, 1996 - v2
Checksum:iD2BA0E5872BE58BE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22594 mRNA. Translation: AAA64295.1.
PIRiA30007.
RefSeqiNP_990739.1. NM_205408.1.
UniGeneiGga.785.

Genome annotation databases

GeneIDi396376.
KEGGigga:396376.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22594 mRNA. Translation: AAA64295.1.
PIRiA30007.
RefSeqiNP_990739.1. NM_205408.1.
UniGeneiGga.785.

3D structure databases

ProteinModelPortaliP12244.
SMRiP12244. Positions 20-136, 369-472.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP12244.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi396376.
KEGGigga:396376.

Organism-specific databases

CTDi396376.

Phylogenomic databases

HOVERGENiHBG005920.
KOiK09580.
PhylomeDBiP12244.

Miscellaneous databases

NextBioi20816418.

Family and domain databases

Gene3Di3.40.30.10. 4 hits.
InterProiIPR005792. Prot_disulphide_isomerase.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00085. Thioredoxin. 2 hits.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 4 hits.
TIGRFAMsiTIGR01130. ER_PDI_fam. 1 hit.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiGSBP_CHICK
AccessioniPrimary (citable) accession number: P12244
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: February 1, 1996
Last modified: February 4, 2015
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.