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 Q9FG93

Entry ID Method Resolution Chain Position Source
AF-Q9FG93-F1 Predicted AlphaFoldDB

75 variants for Q9FG93

Variant ID(s) Position Change Description Diseaes Association Provenance
tmp_5_17556520_C_A 2 D>Y No 1000Genomes
tmp_5_17556506_C_G,T 6 K>N No 1000Genomes
tmp_5_17556507_T_C 6 K>R No 1000Genomes
ENSVATH12461162 19 S>L No 1000Genomes
tmp_5_17556454_G_A 24 H>Y No 1000Genomes
ENSVATH00702247 33 K>N No 1000Genomes
ENSVATH12461161 39 Q>R No 1000Genomes
ENSVATH03340041 53 D>E No 1000Genomes
ENSVATH14580294 53 D>N No 1000Genomes
tmp_5_17555855_G_A 93 L>F No 1000Genomes
tmp_5_17555840_G_A 98 R>C No 1000Genomes
ENSVATH00702235 100 T>I No 1000Genomes
tmp_5_17555813_C_T 107 G>S No 1000Genomes
tmp_5_17555795_T_G 113 N>H No 1000Genomes
tmp_5_17555650_T_G 115 N>T No 1000Genomes
ENSVATH03340039 120 V>L No 1000Genomes
tmp_5_17555582_C_A 138 A>S No 1000Genomes
tmp_5_17555576_C_T 140 D>N No 1000Genomes
tmp_5_17555298_T_A 147 I>F No 1000Genomes
ENSVATH12461012 157 L>M No 1000Genomes
ENSVATH07321611 159 E>D No 1000Genomes
ENSVATH12461011 163 R>Q No 1000Genomes
tmp_5_17555242_C_A 165 M>I No 1000Genomes
tmp_5_17555226_T_A 171 T>S No 1000Genomes
ENSVATH07321596 229 L>I No 1000Genomes
ENSVATH12460882 231 A>S No 1000Genomes
tmp_5_17554498_C_A 237 D>Y No 1000Genomes
ENSVATH12460876 276 G>E No 1000Genomes
tmp_5_17554061_G_T 285 Q>K No 1000Genomes
ENSVATH07321584 292 M>R No 1000Genomes
ENSVATH07321583 293 Q>R No 1000Genomes
tmp_5_17554022_C_A 298 D>Y No 1000Genomes
ENSVATH12460833 334 D>H No 1000Genomes
ENSVATH12460832 340 H>Y No 1000Genomes
tmp_5_17553646_C_A 363 S>I No 1000Genomes
ENSVATH12460826 371 Y>F No 1000Genomes
tmp_5_17553324_T_A 405 Q>L No 1000Genomes
ENSVATH03340007 427 D>N No 1000Genomes
ENSVATH00702196 470 L>F No 1000Genomes
tmp_5_17552927_G_T 479 L>I No 1000Genomes
tmp_5_17552920_C_T 481 R>Q No 1000Genomes
ENSVATH12460759 481 R>W No 1000Genomes
tmp_5_17552885_T_G 493 S>R No 1000Genomes
ENSVATH03340000 500 Q>H No 1000Genomes
ENSVATH12460758 502 V>G No 1000Genomes
ENSVATH00702195 504 G>E No 1000Genomes
ENSVATH00702194 506 D>N No 1000Genomes
ENSVATH03339999 508 S>N No 1000Genomes
ENSVATH03339998 509 N>I No 1000Genomes
tmp_5_17552831_C_T 511 D>N No 1000Genomes
tmp_5_17552824_C_A 513 S>I No 1000Genomes
ENSVATH00702193 515 D>G No 1000Genomes
tmp_5_17552804_C_T 520 E>K No 1000Genomes
ENSVATH12460756 523 P>S No 1000Genomes
tmp_5_17552781_C_A 527 L>F No 1000Genomes
ENSVATH12460755 527 L>S No 1000Genomes
ENSVATH12460754 528 I>V No 1000Genomes
ENSVATH07321548 536 T>I No 1000Genomes
ENSVATH07321548 536 T>K No 1000Genomes
ENSVATH07321549 536 T>S No 1000Genomes
tmp_5_17552502_C_T 542 G>D No 1000Genomes
tmp_5_17552471_A_T 552 D>E No 1000Genomes
tmp_5_17552446_G_A 561 P>S No 1000Genomes
ENSVATH00702191 563 V>I No 1000Genomes
ENSVATH03339980 577 E>V No 1000Genomes
tmp_5_17552385_T_A 581 Q>L No 1000Genomes
ENSVATH12460688 583 E>K No 1000Genomes
ENSVATH07321546 588 S>F No 1000Genomes
tmp_5_17552337_G_T 597 S>Y No 1000Genomes
ENSVATH07321545 599 G>D No 1000Genomes
ENSVATH07321545 599 G>V No 1000Genomes
tmp_5_17552319_T_G 603 D>A No 1000Genomes
tmp_5_17552307_T_G 607 Q>P No 1000Genomes
ENSVATH07321544 617 D>E No 1000Genomes
ENSVATH12460686 622 Y>C No 1000Genomes

No associated diseases with Q9FG93

No regional properties for Q9FG93

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q9FG93

Functions

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

4 GO annotations of cellular component

Name Definition
endoplasmic reticulum The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
endoplasmic reticulum membrane The lipid bilayer surrounding 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.
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.

3 GO annotations of molecular function

Name Definition
alpha-mannosidase activity Catalysis of the hydrolysis of terminal, non-reducing alpha-D-mannose residues in alpha-D-mannosides.
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.
ubiquitin-dependent ERAD pathway The series of steps necessary to target endoplasmic reticulum (ER)-resident proteins for degradation by the cytoplasmic proteasome. Begins with recognition of the ER-resident protein, includes retrotranslocation (dislocation) of the protein from the ER to the cytosol, protein ubiquitination necessary for correct substrate transfer, transport of the protein to the proteasome, and ends with degradation of the protein by the cytoplasmic proteasome.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q9BZQ6 EDEM3 ER degradation-enhancing alpha-mannosidase-like protein 3 Homo sapiens (Human) PR
Q2HXL6 Edem3 ER degradation-enhancing alpha-mannosidase-like protein 3 Mus musculus (Mouse) PR
10 20 30 40 50 60
MDSNFKWLLF AILISLTFSG FVLHHGVLAE SVKPDEAKQL RDEVRGMFYH AFDGYMNNAF
70 80 90 100 110 120
PLDELRPLSC QGEDTLGGYA LTLIDSLDTL ALLGDRERFT SSVEWIGKNL QFNINKTVSV
130 140 150 160 170 180
FETTIRVLGG LLSAHLIASD YATGMRIPSY NNELLVLAEN LARRMLPAFD TPTGIPFGSV
190 200 210 220 230 240
NLMYGVDKHE SKITSTAGGG TLSLEFGVLS RLTNDPVFEQ VAKNAVRGLW ARRSNLDLVG
250 260 270 280 290 300
AHINVFTGEW TQKDAGIGTS IDSFYEYLLK AYILFGDEEY LYIFQEAYRS AMQYLHKDPW
310 320 330 340 350 360
YVEVNMDSAA IVWPVFNSLQ AFWPGLQVLA GDVDPAIRTH TAFFSVWKRY GFTPEGFNLA
370 380 390 400 410 420
TLSVQYGQKS YPLRPELIES TYWLYKATRD PRYLDAGRDF VASLQYGAKC PCGYCHITDV
430 440 450 460 470 480
ELHKQEDHME SFFLAETVKY LWLLFDLAVD SDNLVDNGPY KYIFSTEGHL LPITPQISLA
490 500 510 520 530 540
REHCSYFGGY CPSNSTKLEQ EVLGEDSSND DHSNDYPYHE SFPVTGLIKG LCPGLTHAQK
550 560 570 580 590 600
YGFSYVLPEK TDREDVNQPK PVVTSSSIVL ISDQTVEKRP QEEEGFTSQS EPIMTISGGS
610 620
SNDQTGQELT LLESETDDQR SYSS