Descriptions

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

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q5RCE2

Entry ID Method Resolution Chain Position Source
AF-Q5RCE2-F1 Predicted AlphaFoldDB

No variants for Q5RCE2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q5RCE2

No associated diseases with Q5RCE2

No regional properties for Q5RCE2

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q5RCE2

Functions

Description
EC Number 2.4.99.18 Transferring other glycosyl groups
Subcellular Localization
  • Endoplasmic reticulum membrane ; Multi-pass 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 III complex An oligosaccharyltransferase (OST) complex that contains the seven polypeptides found in OST complex I, plus heterotrimeric Sec61alpha-beta-gamma and the tetrameric TRAP complex. Of the three forms of mammalian OST complexes identified, the OSTIII complex has the strongest affinity for ribosomes.

2 GO annotations of molecular function

Name Definition
dolichyl-diphosphooligosaccharide-protein glycotransferase activity Catalysis of the reaction: dolichyl diphosphooligosaccharide + protein L-asparagine = dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by glycosylamine linkage to protein L-asparagine.
metal ion binding Binding to a metal ion.

2 GO annotations of biological process

Name Definition
co-translational protein modification The process of covalently altering one or more amino acids in a protein after translation has begun but before the protein has been released from the ribosome.
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.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MTKFGFLRLS YEKQDTLLKL LILSMAAVLS FSTRLFAVLR FESVIHEFDP YFNYRTTRFL
70 80 90 100 110 120
AEEGFYKFHN WFDDRAWYPL GRIIGGTIYP GLMITSAAIY HVLHFFHITI DIRNVCVFLA
130 140 150 160 170 180
PLFSSFTTIV TYHLTKELKD AGAGLLAAAM IAVVPGYISR SVAGSYDNEG IAIFCMLLTY
190 200 210 220 230 240
YMWIKAVKTG SICWAAKCAL AYFYMVSSWG GYVFLINLIP LHVLVLMLTG RFSHRIYVAY
250 260 270 280 290 300
CTVYCLGTIL SMQISFVGFQ PVLSSEHMAA FGVFGLCQIH AFVDYLRSKL NPQQFEVLFR
310 320 330 340 350 360
SVISLVGFVL LTVGALLMLT GKISPWTGRF YSLLDPSYAK NNIPIIASVS EHQPTTWSSY
370 380 390 400 410 420
YFDLQLLVFM FPVGLYYCFS NLSDARIFII MYGVTSMYFS AVMVRLMLVL APVMCILSGI
430 440 450 460 470 480
GVSQVLSTYM KNLDISRPDK KSKKQQDSTY PIKNEVASGM ILVMAFFLIT YTFHSTWVTS
490 500 510 520 530 540
EAYSSPSIVL SARGGDGSRI IFDDFREAYY WLRHNTPEDA KVMSWWDYGY QITAMANRTI
550 560 570 580 590 600
LVDNNTWNNT HISRVGQAMA STEEKAYEIM RELDVSYVLV IFGGLTGYSS DDINKFLWMV
610 620 630 640 650 660
RIGGSTDTGK HIKENDYYTP TGEFRVDREG SPVLLNCLMY KMCYYRFGQV YTEAKRPPGF
670 680 690 700
DRVRNAEIGN KDFELDVLEE AYTTEHWLVR IYKVKDLDNR GLSRT