Q7Z1E6 (CALR_BOMMO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Calreticulin

Gene names

Name:

crt

Organism

Bombyx mori (Silk moth) [Reference proteome]

Taxonomic identifier

7091 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Amphiesmenoptera › Lepidoptera › Glossata › Neolepidoptera › Heteroneura › Ditrysia › Obtectomera › Bombycoidea › Bombyciformes › Bombycidae › Bombycinae › Bombyx

Protein attributes

Sequence length	398 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER By similarity.
Subunit structure	Monomer By similarity. UniProtKB P27797
Subcellular location	Endoplasmic reticulum lumen.
Tissue specificity	Expressed in fat bodies. Not expressed in midgut, silk gland, ovary or testis. Ref.1 Ref.2
Induction	Induced by disturbances in intracellular calcium levels caused by the chelators BAPTA-AM and EDTA, the endoplasmic reticulum calcium-ATPase inhibitor thapsigargin and by calcium. Not induced by the endoplasmic reticulum stress-inducing drugs brefeldin A, DTT and tunicamycin, or by heat stress and hydrogen peroxide. Ref.2
Domain	Can be divided into a N-terminal globular domain, a proline-rich P-domain forming an elongated arm-like structure and a C-terminal acidic domain. The P-domain binds one molecule of calcium with high affinity, whereas the acidic C-domain binds multiple calcium ions with low affinity By similarity. UniProtKB P27797 The interaction with glycans occurs through a binding site in the globular lectin domain By similarity. UniProtKB P27797 The zinc binding sites are localized to the N-domain By similarity. UniProtKB P27797
Sequence similarities	Belongs to the calreticulin family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum
Domain	Repeat Signal
Ligand	Calcium Lectin Metal-binding Zinc
Molecular function	Chaperone
PTM	Disulfide bond
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	protein folding Inferred from electronic annotation. Source: InterPro
Cellular_component	endoplasmic reticulum lumen Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19	Potential
	Chain	20 – 398	379	Calreticulin		PRO_0000279696
Regions
	Repeat	191 – 202	12	1-1
	Repeat	210 – 221	12	1-2
	Repeat	227 – 238	12	1-3
	Repeat	244 – 255	12	1-4
	Repeat	259 – 269	11	2-1
	Repeat	273 – 283	11	2-2
	Repeat	287 – 297	11	2-3
	Region	20 – 197	178	N-domain
	Region	191 – 255	65	4 X approximate repeats
	Region	198 – 308	111	P-domain
	Region	259 – 297	39	3 X approximate repeats
	Region	309 – 398	90	C-domain
	Motif	395 – 398	4	Prevents secretion from ER
Sites
	Binding site	109	1	Carbohydrate By similarity
	Binding site	111	1	Carbohydrate By similarity
	Binding site	128	1	Carbohydrate By similarity
	Binding site	135	1	Carbohydrate By similarity
	Binding site	317	1	Carbohydrate By similarity
Amino acid modifications
	Disulfide bond	105 ↔ 137		By similarity UniProtKB P27797
Experimental info
	Sequence conflict	36	1	W → K AA sequence Ref.4
	Sequence conflict	41	1	H → A AA sequence Ref.4
	Sequence conflict	45	1	E → D AA sequence Ref.4
	Sequence conflict	47	1	G → E AA sequence Ref.4
	Sequence conflict	49	1	F → K AA sequence Ref.4
	Sequence conflict	205	1	N → P in BAC57964. Ref.3
	Sequence conflict	285	1	Y → F in BAC57964. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q7Z1E6 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: 0BC049839F5950EA	FASTA	398	45,802
	10 20 30 40 50 60 MKAVVLVVVS LLALSSINCD VFFEEKFPDD SWESNWVYSE HPGKEFGKFK LTAGKFFSDP 70 80 90 100 110 120 EDDKGLKTSE DARFYALSRK FKPFSNEGKP LVVQFTVKHE QDIDCGGGYL KVFDCKLEQK 130 140 150 160 170 180 DMHGETPYEI MFGPDICGPG TKKVHVIFSY KGKNHLIKKD IRCKDDVYTH LYTLIVKPDN 190 200 210 220 230 240 TYEVLIDNEK VESGDLEADW DFLPNKKIKD PEAKKPEDWD DKPTIPDPED KKPEDWDKPE 250 260 270 280 290 300 HIPDPDATKP EDWDDEMDGE WEPPMIDNPD YKGVWAPKQI DNPAYKGPWV HPEIDNPEYT 310 320 330 340 350 360 PDSNLYKRDE ICAVGLDLWQ VKSGTIFDDF LITDDPAAAK ERGEVIKKRQ EGEKKMKSEQ 370 380 390 DEAEREKEKA EKPDDEEDDE DLDDETGDAA PVEEHDEL

References

[1]	"Molecular cloning of a cDNA encoding putative calreticulin from the silkworm, Bombyx mori." Kim S.R., Lee K.S., Kim I., Kang S.W., Nho S.K., Sohn H.D., Jin B.R. Int. J. Ind. Entomol. 6:93-97(2003) Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[2]	"Endoplasmic reticulum stress response of Bombyx mori calreticulin." Goo T.W., Park S., Jin B.R., Yun E.Y., Kim I., Nho S.-K., Kang S.-W., Kwon O.-Y. Mol. Biol. Rep. 32:133-139(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION.
[3]	Takahashi T., Yamashita T. Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: p50T. Tissue: Fat body.
[4]	"Protein database for several tissues derived from five instar of silkworm." Zhong B.-X. Yi Chuan Xue Bao 28:217-224(2001) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-49. Strain: Xinhang X Keming. Tissue: Body wall and Fat body.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY297158 mRNA. Translation: AAP50845.1. AB090887 mRNA. Translation: BAC57964.1.
RefSeq	NP_001037075.1. NM_001043610.1.
UniGene	Bmo.1394.
3D structure databases
HSSP	HSSP built from PDB template 1K91 based on UniProtKB P18418.
ProteinModelPortal	Q7Z1E6.
SMR	Q7Z1E6. Positions 205-305.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	692629.
Organism-specific databases
CTD	45841.
Family and domain databases
Gene3D	2.60.120.200. 2 hits.
InterPro	IPR001580. Calret/calnex. IPR018124. Calret/calnex_CS. IPR009169. Calreticulin. IPR008985. ConA-like_lec_gl_sf. IPR013320. ConA-like_subgrp. [Graphical view]
PANTHER	PTHR11073. PTHR11073. 1 hit.
Pfam	PF00262. Calreticulin. 1 hit. [Graphical view]
PIRSF	PIRSF002356. Calreticulin. 1 hit.
PRINTS	PR00626. CALRETICULIN.
SUPFAM	SSF49899. ConA_like_lec_gl. 1 hit.
PROSITE	PS00803. CALRETICULIN_1. 1 hit. PS00804. CALRETICULIN_2. 1 hit. PS00805. CALRETICULIN_REPEAT. 3 hits. PS00014. ER_TARGET. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CALR_BOMMO

Accession

Primary (citable) accession number: Q7Z1E6
Secondary accession number(s): P82199, Q869E0

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 6, 2007
Last sequence update:	October 1, 2003
Last modified:	April 3, 2013
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)