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 Q38858

Entry ID Method Resolution Chain Position Source
AF-Q38858-F1 Predicted AlphaFoldDB

21 variants for Q38858

Variant ID(s) Position Change Description Diseaes Association Provenance
tmp_1_2976645_A_T 4 M>K No 1000Genomes
tmp_1_2976639_G_A,T 6 P>H No 1000Genomes
tmp_1_2976639_G_A,T 6 P>L No 1000Genomes
tmp_1_2976613_C_G 15 G>R No 1000Genomes
ENSVATH04543595 23 A>T No 1000Genomes
tmp_1_2975710_C_T 83 E>K No 1000Genomes
ENSVATH10830341 116 L>I No 1000Genomes
tmp_1_2975574_T_C 128 D>G No 1000Genomes
tmp_1_2975562_C_A 132 S>I No 1000Genomes
ENSVATH13868836 157 N>Y No 1000Genomes
ENSVATH01027167 184 T>S No 1000Genomes
tmp_1_2975303_C_G 186 S>T No 1000Genomes
tmp_1_2975013_T_C 225 Q>R No 1000Genomes
tmp_1_2974969_C_T 240 D>N No 1000Genomes
tmp_1_2974637_C_G 294 E>D No 1000Genomes
ENSVATH00013219 309 L>I No 1000Genomes
ENSVATH13868810 360 A>S No 1000Genomes
ENSVATH04543564 361 A>G No 1000Genomes
ENSVATH00013215 408 V>E No 1000Genomes
tmp_1_2973361_T_C 410 S>G No 1000Genomes
ENSVATH01027145 413 T>N No 1000Genomes

No associated diseases with Q38858

3 regional properties for Q38858

Type Name Position InterPro Accession
domain Immunoglobulin subtype 568 - 652 IPR003599
domain Immunoglobulin-like domain 562 - 650 IPR007110
domain Immunoglobulin I-set 563 - 651 IPR013098

Functions

Description
EC Number
Subcellular Localization
  • Endoplasmic reticulum lumen
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

7 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.
extracellular region The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite.
mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
plant-type vacuole A closed structure that is completely surrounded by a unit membrane, contains liquid, and retains the same shape regardless of cell cycle phase. An example of this structure is found in Arabidopsis thaliana.
secretory vesicle A cytoplasmic, membrane bound vesicle that is capable of fusing to the plasma membrane to release its contents into the extracellular space.

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.

3 GO annotations of biological process

Name Definition
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 endoplasmic reticulum stress Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stress acting at the endoplasmic reticulum. ER stress usually results from the accumulation of unfolded or misfolded proteins in the ER lumen.
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.

14 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q2TBR8 CALR3 Calreticulin-3 Bos taurus (Bovine) PR
P52193 CALR Calreticulin Bos taurus (Bovine) PR
P29413 Calr Calreticulin Drosophila melanogaster (Fruit fly) PR
P27797 CALR Calreticulin Homo sapiens (Human) PR
Q96L12 CALR3 Calreticulin-3 Homo sapiens (Human) PR
P14211 Calr Calreticulin Mus musculus (Mouse) PR
Q9D9Q6 Calr3 Calreticulin-3 Mus musculus (Mouse) PR
P28491 CALR Calreticulin Sus scrofa (Pig) PR
P18418 Calr Calreticulin Rattus norvegicus (Rat) PR
Q9SLY8 CRO1 Calreticulin Oryza sativa subsp japonica (Rice) PR
P27798 crt-1 Calreticulin Caenorhabditis elegans PR
Q7Z1E6 crt Calreticulin Bombyx mori (Silk moth) PR
O04151 CRT1 Calreticulin-1 Arabidopsis thaliana (Mouse-ear cress) PR
O04153 CRT3 Calreticulin-3 Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MAKMIPSLVS LILIGLVAIA SAAVIFEERF DDGWENRWVK SEWKKDDNTA GEWKHTAGNW
70 80 90 100 110 120
SGDANDKGIQ TSEDYRFYAI SAEFPEFSNK DKTLVFQFSV KHEQKLDCGG GYMKLLSGDV
130 140 150 160 170 180
DQKKFGGDTP YSIMFGPDIC GYSTKKVHAI LTYNEANHLI KKDVPCETDQ LTHVYTFILR
190 200 210 220 230 240
PDATYSILID NVEKQTGSLY SDWDLLPPKK IKDPSAKKPE DWDEQEYISD PEDKKPDGYD
250 260 270 280 290 300
DIPKEIPDTD SKKPEDWDDE EDGEWTAPTI PNPEYMGEWK PKQIKNPNYK GKWEAPLIDN
310 320 330 340 350 360
PDFKDDPELY VFPKLKYVGL ELWQVKSGSL FDNVLICDDP DYAKKLADET WGKLKDAEKA
370 380 390 400 410 420
AFDEAEKKNE EEESKDAPAE SDAEDEPEDD EGGDDSDSES KAEETKSVDS EETSEKDATA
HDEL