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 O04153

Entry ID Method Resolution Chain Position Source
AF-O04153-F1 Predicted AlphaFoldDB

18 variants for O04153

Variant ID(s) Position Change Description Diseaes Association Provenance
tmp_1_2671737_G_C 22 L>V No 1000Genomes
tmp_1_2671353_G_T 52 N>K No 1000Genomes
tmp_1_2671300_G_T 70 P>H No 1000Genomes
ENSVATH04539387 156 I>L No 1000Genomes
tmp_1_2670358_G_A 158 S>L No 1000Genomes
tmp_1_2670176_C_T 219 V>I No 1000Genomes
tmp_1_2669841_G_A 237 P>L No 1000Genomes
tmp_1_2669827_G_A 242 P>S No 1000Genomes
tmp_1_2669254_T_G 298 K>N No 1000Genomes
tmp_1_2669228_G_A 307 P>L No 1000Genomes
ENSVATH10787970 310 E>V No 1000Genomes
ENSVATH13865169 322 K>N No 1000Genomes
tmp_1_2668727_A_G 352 I>T No 1000Genomes
tmp_1_2668495_C_A 372 E>D No 1000Genomes
ENSVATH01024802 400 R>Q No 1000Genomes
ENSVATH00011788 408 Y>D No 1000Genomes
ENSVATH00011787 408 Y>S No 1000Genomes
ENSVATH04539373 412 N>Y No 1000Genomes

No associated diseases with O04153

2 regional properties for O04153

Type Name Position InterPro Accession
conserved_site Calreticulin/calnexin, conserved site 107 - 122 IPR018124-1
conserved_site Calreticulin/calnexin, conserved site 139 - 147 IPR018124-2

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.
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.

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.

5 GO annotations of biological process

Name Definition
anthocyanin-containing compound metabolic process The chemical reactions and pathways involving anthocyanins, any member of a group of intensely colored soluble glycosides of anthocyanidins that occur in plants. They are responsible from most of the scarlet, purple, mauve and blue coloring in higher plants, especially of flowers.
defense response to bacterium Reactions triggered in response to the presence of a bacterium that act to protect the cell or organism.
plant-type hypersensitive response The rapid, localized death of plant cells in response to invasion by a pathogen.
protein folding The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure.
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
Q38858 CRT2 Calreticulin-2 Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MGLPQNKLSF FCFFFLVSVL TLAPLAFSEI FLEEHFEGGW KSRWVLSDWK RNEGKAGTFK
70 80 90 100 110 120
HTAGKWPGDP DNKGIQTYND AKHYAISAKI PEFSNKNRTL VVQYSVKIEQ DIECGGAYIK
130 140 150 160 170 180
LLSGYVNQKQ FGGDTPYSLM FGPDICGTQT KKLHVIVSYQ GQNYPIKKDL QCETDKLNHF
190 200 210 220 230 240
YTFILRPDAS YSVLVDNKER EFGSMYTDWD ILPPRKIKVK NAKKPEDWDD REYIDDPNDV
250 260 270 280 290 300
KPEGFDSIPR EIPDRKAKEP EDWDEEENGL WEPPKIPNSA YKGPWKAKRI KNPNYKGKWK
310 320 330 340 350 360
NPWIDNPEFE DDPDLYVLKS IKYAGIEVWQ VKAGSIFDNI LICDDPAYAR SIVDDYFAQH
370 380 390 400 410 420
RESEKELFAE AEKERKARED EEARIAREEG ERRRKERDHR YGDRRRRYKR PNPRDYMDDY
HDEL