Q6GQB9

PR
Gene name
edem3
Protein name
ER degradation-enhancing alpha-mannosidase-like protein 3
Names
Alpha-1,2-mannosidase EDEM3
Species
Xenopus laevis (African clawed frog)
KEGG Pathway
xla:443907
EC number
3.2.1.113: Glycosidases, ie enzymes hydrolyzing O- and S-glycosyl compounds
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

44-114 (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 Q6GQB9

Entry ID Method Resolution Chain Position Source
AF-Q6GQB9-F1 Predicted AlphaFoldDB

No variants for Q6GQB9

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q6GQB9

No associated diseases with Q6GQB9

4 regional properties for Q6GQB9

Type Name Position InterPro Accession
domain Translation elongation factor P/YeiP, central 68 - 127 IPR001059
domain Translation elongation factor, KOW-like 5 - 60 IPR013185
conserved_site Translation elongation factor P/YeiP, conserved site 151 - 170 IPR013852
domain Elongation factor P, C-terminal 130 - 185 IPR015365

Functions

Description
EC Number 3.2.1.113 Glycosidases, ie enzymes hydrolyzing O- and S-glycosyl compounds
Subcellular Localization
  • Endoplasmic reticulum lumen
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
endoplasmic reticulum lumen The volume enclosed by the membranes of the endoplasmic reticulum.
endoplasmic reticulum quality control compartment A subcompartment of the endoplasmic reticulum in which proteins with improper or incorrect folding accumulate. Enzymes in this compartment direct proteins with major folding problems to translocation to the cytosol and degradation, and proteins with minor folding problems to the ER, to interact with chaperon proteins.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.

2 GO annotations of molecular function

Name Definition
calcium ion binding Binding to a calcium ion (Ca2+).
mannosyl-oligosaccharide 1,2-alpha-mannosidase activity Catalysis of the hydrolysis of the terminal (1->2)-linked alpha-D-mannose residues in an oligo-mannose oligosaccharide.

5 GO annotations of biological process

Name Definition
carbohydrate metabolic process The chemical reactions and pathways involving carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y.
endoplasmic reticulum mannose trimming Any protein alpha-1,2-demannosylation that takes place in the endoplasmic reticulum quality control compartment (ERQC).
mannose trimming involved in glycoprotein ERAD pathway The removal of one or more alpha 1,2-linked mannose residues from a mannosylated protein that occurs as part of glycoprotein ER-associated glycoprotein degradation (gpERAD).
protein glycosylation A protein modification process that results in the addition of a carbohydrate or carbohydrate derivative unit to a protein amino acid, e.g. the addition of glycan chains to proteins.
response to unfolded protein Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an unfolded protein stimulus.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MGCPAVEARR WGDMWLVVAF CLLGHGHAAV TKEEKAHLRS QVLEMFDHAY GNYMQHAYPA
70 80 90 100 110 120
DELMPLTCRG RIRGQEPSRG DVDDALGKFS LTLIDTLDTL VVLNKTKEFE DAVRKVITDV
130 140 150 160 170 180
NLDNDIVVSV FETNIRVLGG LLGGHSVAIM LKENGDGMQW YNDELLHMAK ELGYKLLPAF
190 200 210 220 230 240
NTTSGLPYPR INLKFGIRRP EARTGTETDT CTACAGTMIL EFAALSRFTG ISVFEEHARK
250 260 270 280 290 300
ALDFLWDKRQ RSSNLVGVTI NIHTGDWVRK DSGVGAGIDS YYEYLLKAYV LLGDDSYLER
310 320 330 340 350 360
FNTHYDAIMR YISQPPLLLD VHIHKPMLTA RTWMDSLLAF FPGLQVLKGD IRPAIETHEM
370 380 390 400 410 420
LYQVIKKHNF LPEAFTTDFR VHWAQHPLRP EFAESTYFLY KATGDPYYLE VGKTLIDNLN
430 440 450 460 470 480
KYARVPCGFA AVKDVRTGSH EDRMDSFFLA EMFKYLYLLF SEREDLIFDI EDYIFTTEAH
490 500 510 520 530 540
LLPLSLSTAN PSSTKKNTTT QYTELDDSNF DWSCPNTQIL FRNDPMYAQN IREPLKNVVD
550 560 570 580 590 600
KNCPRSPSRL DEISGSGKMP PLRARDFMAS NSEHLEILKK MGVSLIHLKD GRVQLVQHAN
610 620 630 640 650 660
QAASSIDAED GLRFMQEMIE LSSQQQKEQQ LPPRAVQIVS HPFYGRVVLT AGPAQFGMDL
670 680 690 700 710 720
SKHLAGAQGL VARAEPYSGC SDITNGQAIQ GKIALMQRGQ CMFAEKARNV QKAGAIGGIV
730 740 750 760 770 780
IDDNEGSSSD TAPLFQMAGD GKSTDDVTIP MLFLFSKEGN IILDAIREYQ QVEVLLSDKA
790 800 810 820 830 840
KDRDLESESG EQKPVENDSQ KQALEDLFMT PEEIAELLIV HEEESPVSQP EVPSSDSPSG
850 860 870 880 890 900
GDRTSERDIT PESQEHKTEE TEHSPKDNVQ TPPENSEDST EEKMDNKVQP MESILADWKE
910
DIEAFEMMEK DEL