Q0DJC5

PR
Gene name
OST1A (RPN1A)
Protein name
Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1A
Names
Ribophorin IA, RPN-IA, Ribophorin-1A
Species
Oryza sativa subsp japonica (Rice)
KEGG Pathway
osa:4338348
EC number
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1-46 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q0DJC5

Entry ID Method Resolution Chain Position Source
AF-Q0DJC5-F1 Predicted AlphaFoldDB

No variants for Q0DJC5

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q0DJC5

No associated diseases with Q0DJC5

No regional properties for Q0DJC5

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q0DJC5

Functions

Description
EC Number
Subcellular Localization
  • Endoplasmic reticulum membrane ; Single-pass type I membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
integral component of membrane The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
oligosaccharyltransferase complex A protein complex that is found in the endoplasmic reticulum membrane of eukaryotes and transfers lipid-linked oligosaccharide precursor to asparagine residues on nascent proteins. In yeast, the complex includes at least nine different subunits, whereas in mammalian cells at least three different forms of the complex have been detected.

No GO annotations of molecular function

Name Definition
No GO annotations for molecular function

1 GO annotations of biological process

Name Definition
protein N-linked glycosylation via asparagine The glycosylation of protein via the N4 atom of peptidyl-asparagine forming N4-glycosyl-L-asparagine; the most common form is N-acetylglucosaminyl asparagine; N-acetylgalactosaminyl asparagine and N4 glucosyl asparagine also occur. This modification typically occurs in extracellular peptides with an N-X-(ST) motif. Partial modification has been observed to occur with cysteine, rather than serine or threonine, in the third position; secondary structure features are important, and proline in the second or fourth positions inhibits modification.

4 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P04843 RPN1 Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1 Homo sapiens (Human) PR
Q91YQ5 Rpn1 Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1 Mus musculus (Mouse) PR
Q9GMB0 RPN1 Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1 Sus scrofa (Pig) PR
P07153 Rpn1 Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1 Rattus norvegicus (Rat) PR
10 20 30 40 50 60
MATPPPLRRV AALLLLLVAA ASTPTARADL VVTRADRKVD LTSHIVRVLT SLKVENSGPE
70 80 90 100 110 120
AVSQFLLAFP NVQAKNLAAI RAFGTEEKVK GPSMVLPIEV VQPSGVPPEL TFFSASLSKP
130 140 150 160 170 180
LEKGKTLHLD VLTVFTHSVQ PFPEEITQAE SQLVVYQDSA QYLSPYPVKV QTLSIRLPGG
190 200 210 220 230 240
RVESYTKYPN TKLAESELKY GPYEDLPPFS YSPMVVHYEN NNPFAVAKEV IREIEISHWG
250 260 270 280 290 300
NVQITEHYNI AHGGAKLKGE FSRIDYQSRP YIRGVSSFRH LIARLPPRAH SIYYRDEIGN
310 320 330 340 350 360
ISTSHLWSDS KKTQLEVEPR FPLFGGWQTT FTIGYGLPLQ DFVFNSDGKR FLNITFGSPV
370 380 390 400 410 420
EEILIEKLIV KVVLPEGSKD IDISVPFPTK QEQEVKYSHL DISGRPVVVL EKLDVIPEHN
430 440 450 460 470 480
LYFQVYYRFN NISLLREPMM LITGFFLLFM ACIVYMRTDM SISKNSPSYL AKVQWDEVQS
490 500 510 520 530 540
IIQQIQAIFN QCLAAHDKLE TSLHELSRSG DVKSCKVARK TADAQFKELA KELKPLLTSL
550 560 570 580 590 600
QSSSQSYQIW PKVEELVAKE RELQDKLMTR HSTVVDSFEK KLRGQDVENR IAAQQQKVAA
610
LRQEVESLLE YISEI