Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
Active sitei52NucleophileBy similarity1
Sitei53Contributes to redox potential valueBy similarity1
Sitei54Contributes to redox potential valueBy similarity1
Active sitei55NucleophileBy similarity1
Sitei119Lowers pKa of C-terminal Cys of first active siteBy similarity1
Active sitei398NucleophileBy similarity1
Sitei399Contributes to redox potential valueBy similarity1
Sitei400Contributes to redox potential valueBy similarity1
Active sitei401NucleophileBy similarity1
Sitei462Lowers pKa of C-terminal Cys of second active siteBy similarity1

GO - Molecular functioni

GO - Biological processi

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
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 17Sequence analysisAdd BLAST17
ChainiPRO_000003420118 – 508Dolichyl-diphosphooligosaccharide--protein glycotransferaseAdd BLAST491

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi52 ↔ 55Redox-activePROSITE-ProRule annotation
Disulfide bondi398 ↔ 401Redox-activePROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP12244.

Structurei

3D structure databases

ProteinModelPortaliP12244.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini18 – 133Thioredoxin 1PROSITE-ProRule annotationAdd BLAST116
Domaini333 – 496Thioredoxin 2PROSITE-ProRule annotationAdd BLAST164

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi505 – 508Prevents secretion from ER4

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.
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

PROiP12244.

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...

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: October 5, 2016
This is version 122 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

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 one 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.