Q9GMB0

PR
Gene name
RPN1
Protein name
Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
Names
Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 67 kDa subunit, Ribophorin I, RPN-I, Ribophorin-1
Species
Sus scrofa (Pig)
KEGG Pathway
ssc:397606
EC number
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

1-133 (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 Q9GMB0

Entry ID Method Resolution Chain Position Source
AF-Q9GMB0-F1 Predicted AlphaFoldDB

No variants for Q9GMB0

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9GMB0

No associated diseases with Q9GMB0

No regional properties for Q9GMB0

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q9GMB0

Functions

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

3 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.
melanosome A tissue-specific, membrane-bounded cytoplasmic organelle within which melanin pigments are synthesized and stored. Melanosomes are synthesized in melanocyte cells.
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
P07153 Rpn1 Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1 Rattus norvegicus (Rat) PR
Q0DJC5 OST1A Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1A Oryza sativa subsp japonica (Rice) PR
10 20 30 40 50 60
MEAPAVCLLP LLLLLWAWAP APGRASPEAL PLVNEDVKRT VDLSSHLAKV TAEVVLAHAG
70 80 90 100 110 120
SSSSPRAASF LLALEPELEA RLAHLGVQVK GEDEEENNLE VRETKIKGKR GRFFTVTLPV
130 140 150 160 170 180
ALDPGAKISV TVETVYTHVL QPYPTQITQS EKQFVVFEGN HYFYSPYPTK SQSMRVKLAS
190 200 210 220 230 240
RNVESYTKLG NPTRSEDLLD YGPFRDVPPY SQDTFKVHSE NNSPFLTITS MTRVIEVSHW
250 260 270 280 290 300
GNIAVEENVD LKHTGAVLKG PFSRYDYQRQ PDSGISSIRS FKTILPAAAQ DVYYRDEIGN
310 320 330 340 350 360
VSTSHLLILD DSVEMEIRPR FPLFGGWKTH YIVGYNLPSY EYLYNLGDQY ALKMRLVDHV
370 380 390 400 410 420
FDEQVIDSLT VKIILPEGAK NIQVDSPYEI SRAPDELHYT YLDTFGRPVI VAHKKNLVEQ
430 440 450 460 470 480
HIQDIVVHYT FNKVLMLQEP LLVVAAFYIL FFTVIVYVRL DFSITKDPAA EARMKVACIT
490 500 510 520 530 540
EQVLTLVNKR IGLYRHFDET INRYKQSRDV STLNSGKKSL ELEHKALTSE VALLQSRLKT
550 560 570 580 590 600
EGSDLCDKVS EMQKLDAQVK ELVLKSAVEA ERLVAGKLKK DTYIENEKLI SGKRQELVTK
IDHILDAL