Q23858

PR
Gene name
crtA (DDB_G0283539)
Protein name
Calreticulin
Names
Species
Dictyostelium discoideum (Slime mold)
KEGG Pathway
ddi:DDB_G0283539
EC number
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

328-424 (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 Q23858

Entry ID Method Resolution Chain Position Source
AF-Q23858-F1 Predicted AlphaFoldDB

No variants for Q23858

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q23858

No associated diseases with Q23858

14 regional properties for Q23858

Type Name Position InterPro Accession
repeat HAT (Half-A-TPR) repeat 55 - 87 IPR003107-1
repeat HAT (Half-A-TPR) repeat 89 - 121 IPR003107-2
repeat HAT (Half-A-TPR) repeat 123 - 155 IPR003107-3
repeat HAT (Half-A-TPR) repeat 157 - 188 IPR003107-4
repeat HAT (Half-A-TPR) repeat 190 - 221 IPR003107-5
repeat HAT (Half-A-TPR) repeat 223 - 258 IPR003107-6
repeat HAT (Half-A-TPR) repeat 260 - 294 IPR003107-7
repeat HAT (Half-A-TPR) repeat 304 - 336 IPR003107-8
repeat HAT (Half-A-TPR) repeat 338 - 372 IPR003107-9
repeat HAT (Half-A-TPR) repeat 382 - 418 IPR003107-10
repeat HAT (Half-A-TPR) repeat 420 - 451 IPR003107-11
repeat HAT (Half-A-TPR) repeat 453 - 485 IPR003107-12
repeat HAT (Half-A-TPR) repeat 487 - 521 IPR003107-13
repeat HAT (Half-A-TPR) repeat 523 - 554 IPR003107-14

Functions

Description
EC Number
Subcellular Localization
  • Endoplasmic reticulum lumen
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 lumen The volume enclosed by the membranes of the endoplasmic reticulum.
endoplasmic reticulum membrane The lipid bilayer surrounding the endoplasmic reticulum.
phagocytic vesicle A membrane-bounded intracellular vesicle that arises from the ingestion of particulate material by phagocytosis.

3 GO annotations of molecular function

Name Definition
calcium ion binding Binding to a calcium ion (Ca2+).
carbohydrate binding Binding to a carbohydrate, which includes monosaccharides, oligosaccharides and polysaccharides as well as substances derived from monosaccharides by reduction of the carbonyl group (alditols), by oxidation of one or more hydroxy groups to afford the corresponding aldehydes, ketones, or carboxylic acids, or by replacement of one or more hydroxy group(s) by a hydrogen atom. Cyclitols are generally not regarded as carbohydrates.
unfolded protein binding Binding to an unfolded protein.

4 GO annotations of biological process

Name Definition
phagocytosis, engulfment The internalization of bacteria, immune complexes and other particulate matter or of an apoptotic cell by phagocytosis, including the membrane and cytoskeletal processes required, which involves one of three mechanisms: zippering of pseudopods around a target via repeated receptor-ligand interactions, sinking of the target directly into plasma membrane of the phagocytosing cell, or induced uptake via an enhanced membrane ruffling of the phagocytosing cell similar to macropinocytosis.
protein folding The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure.
response to other organism 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 a stimulus from another living organism.
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.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MRLLLCLIFL VFVFNFALST VHFKDTFDND WESRWVVSDW HKEDGKSGKL VHTAGKWFGD
70 80 90 100 110 120
ENQKGIQTSE DARFYAVSAK FPSFSNKGKD LVLQYTVKNE QKVDCGGSYI KLLPSKLDQS
130 140 150 160 170 180
AFDGESEYSI MFGPDVCGAS KRVHVILNYK GKNHLIKKEI NKVETDQLTH QYTLVISPDN
190 200 210 220 230 240
TYKVLVDNKE IQAGNLADDW ELLPSKQIKD PKQSKPVDWV DVKEIDDPED VKPAGHDDIP
250 260 270 280 290 300
ASIVDPEAVK PEDWNEEDDG EWEAPTIANP EYKGEWKAKK IPNPEYKGEW VHPLIDNPEY
310 320 330 340 350 360
AEDNELYLFN DLGAIGFELW QVKSGSIFNN MIVTDSVEEA KDFSEKTFVA NQEAEKKMFD
370 380 390 400 410 420
DLEAAKAEER KKADEKLAAE KAAEKEAEEA DEEEEEVAEE DLVKTDDKKE EVKKSTKKVD
HDEL