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P12244

- GSBP_CHICK

UniProt

P12244 - GSBP_CHICK

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Protein
Dolichyl-diphosphooligosaccharide--protein glycotransferase
Gene
N/A
Organism
Gallus gallus (Chicken)
Status
Reviewed - 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 – 521Nucleophile By similarity
Sitei53 – 531Contributes to redox potential value By similarity
Sitei54 – 541Contributes to redox potential value By similarity
Active sitei55 – 551Nucleophile By similarity
Sitei119 – 1191Lowers pKa of C-terminal Cys of first active site By similarity
Active sitei398 – 3981Nucleophile By similarity
Sitei399 – 3991Contributes to redox potential value By similarity
Sitei400 – 4001Contributes to redox potential value By similarity
Active sitei401 – 4011Nucleophile By similarity
Sitei462 – 4621Lowers pKa of C-terminal Cys of second active site By 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539: 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 – 1717 Reviewed prediction
Add
BLAST
Chaini18 – 508491Dolichyl-diphosphooligosaccharide--protein glycotransferase
PRO_0000034201Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi52 ↔ 55Redox-active By similarity
Disulfide bondi398 ↔ 401Redox-active By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP12244.

Structurei

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini18 – 133116Thioredoxin 1
Add
BLAST
Domaini333 – 496164Thioredoxin 2
Add
BLAST

Motif

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

Sequence similaritiesi

Contains 2 thioredoxin domains.

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

MLRALCALAW RVARVGADAE EQDNVLVAKK SNFLEPLAAH SYLAVEFYAP    50
LCGHCKALAP DYAKAGGKLK AEGSEIKAAK VEATEESDLA QQYGVRAYPT 100
IKFFKNGDTA SPKEYTAGRE ADDIVNWLKK RTGPAATTLS DTAAAESLVD 150
SSEITVIIGF FKDPGSDSAR QFLLAADAVD DVPFGINSNS DVYSKYQMDK 200
DAVVLFKKFA EGRNNFEGEI TKEKLLDFIK HNNLPLVIEF TEQTAPKIFG 250
GEIKTHILLF LPKSVSDYDG KLSNLKKAAD GFKGKILFVF IDSDHTDNQR 300
ILEFFGLKKE ECPAVRLITL DEELTKYKPE TEELTAEKLT QFCHHFLEGK 350
IKPHLMSNEP LPEDWDKQPV KVLVGKNYEE VAFDEKKNVF IEFYAPWCGH 400
CKQLAPMWDR LGEAYKDDEN IVIAKMESTA NEVEAIKVHS FPTLKFFPAS 450
AERTVIDYNG ERTLDGYKKF LESGGQDGYG NNDDDDLEEA LESDMEEDED 500
QKAMKDEL 508
Length:508
Mass (Da):56,892
Last modified:February 1, 1996 - v2
Checksum:iD2BA0E5872BE58BE
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
M22594 mRNA. Translation: AAA64295.1 .
PIRi A30007.
RefSeqi NP_990739.1. NM_205408.1.
UniGenei Gga.785.

3D structure databases

ProteinModelPortali P12244.
SMRi P12244. Positions 20-136, 369-472.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P12244.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 396376.
KEGGi gga:396376.

Organism-specific databases

CTDi 396376.

Phylogenomic databases

HOVERGENi HBG005920.
KOi K09580.
PhylomeDBi P12244.

Miscellaneous databases

NextBioi 20816418.

Family and domain databases

Gene3Di 3.40.30.10. 4 hits.
InterProi IPR005792. Prot_disulphide_isomerase.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view ]
Pfami PF00085. Thioredoxin. 2 hits.
[Graphical view ]
SUPFAMi SSF52833. SSF52833. 4 hits.
TIGRFAMsi TIGR01130. ER_PDI_fam. 1 hit.
PROSITEi PS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

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(1988) [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: September 3, 2014
This is version 112 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

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