O81919 (CALR_BETVU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Calreticulin
Organism	Beta vulgaris (Sugar beet)
Taxonomic identifier	161934 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › Caryophyllales › Amaranthaceae › Beta

Protein attributes

Sequence length	416 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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.
Subcellular location	Endoplasmic reticulum lumen By similarity.
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. The interaction with glycans occurs through a binding site in the globular lectin domain By similarity. The zinc binding sites are localized to the N-domain By similarity.
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 Glycoprotein
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 – 25	25	Potential
	Chain	26 – 416	391	Calreticulin		PRO_0000004188
Regions
	Repeat	197 – 208	12	1-1
	Repeat	216 – 227	12	1-2
	Repeat	233 – 244	12	1-3
	Repeat	251 – 262	12	1-4
	Repeat	266 – 276	11	2-1
	Repeat	280 – 290	11	2-2
	Repeat	294 – 304	11	2-3
	Region	197 – 262	66	4 X approximate repeats
	Region	266 – 304	39	3 X approximate repeats
	Motif	413 – 416	4	Prevents secretion from ER Potential
	Compositional bias	358 – 411	54	Asp/Glu/Lys-rich
Sites
	Binding site	115	1	Carbohydrate By similarity
	Binding site	117	1	Carbohydrate By similarity
	Binding site	134	1	Carbohydrate By similarity
	Binding site	141	1	Carbohydrate By similarity
	Binding site	324	1	Carbohydrate By similarity
Amino acid modifications
	Glycosylation	57	1	N-linked (GlcNAc...) Potential
	Glycosylation	157	1	N-linked (GlcNAc...) Potential
	Disulfide bond	111 ↔ 143		By similarity

Sequences

	Sequence		Length	Mass (Da)
	O81919 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 565FEC3489F77CA7	FASTA	416	48,136
	10 20 30 40 50 60 MENRGRNPSF LSLLLLLSLF AIASAKVFFE ERFEDGWEKR WVKSEWKKDE SMAGEWNYTS 70 80 90 100 110 120 GKWNGDANDK GIQTSEDYRF YAISAEFPEF SNKDNTLVFQ FSVKHEQKLD CGGGYMKLLS 130 140 150 160 170 180 GEVDQKKFGG DTPYSIMFGP DICGYSTKKV HAIFNYNDTN HLIKKDVPCE TDQLTHVYTF 190 200 210 220 230 240 ILRPDATYSI LIDNQEKQTG SLYTDWDLLP AKKIKDPEAK KPEDWDDKEF IPDPEDKKPE 250 260 270 280 290 300 GYDDIPAEIT DPEAKKPEDW DDEEDGEWTA PTIPNPEYKG PWKAKKIKNP NYKGKWKAPM 310 320 330 340 350 360 IDNPEFKDDP ELYVYPKLRY VGVELWQVKS GTLFDNVLVC DDPEYAKQLA EETWGKQKDA 370 380 390 400 410 EKAAFEELEK KREEEETKDD PVESDAEDED EAEADDSDKD DADKSDDKDD DQHDEL

References

[1]	"Nucleotide sequence from sugar beet calreticulin." Viereck R. Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: VV-D/ZR5. Tissue: Leaf.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ002057 mRNA. Translation: CAA05161.1.
PIR	T14554.
3D structure databases
ProteinModelPortal	O81919.
SMR	O81919. Positions 211-312.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
Gene3D	2.10.250.10. 1 hit. 2.60.120.200. 1 hit.
InterPro	IPR001580. Calret/calnex. IPR018124. Calret/calnex_CS. IPR009169. Calreticulin. IPR009033. Calreticulin/calnexin_P_dom. 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	SSF63887. Calret_calnex_P. 1 hit. SSF49899. ConA_like_lec_gl. 1 hit.
PROSITE	PS00803. CALRETICULIN_1. 1 hit. PS00804. CALRETICULIN_2. 1 hit. PS00805. CALRETICULIN_REPEAT. 2 hits. PS00014. ER_TARGET. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CALR_BETVU

Accession

Primary (citable) accession number: O81919

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 1, 1998
Last modified:	March 6, 2013
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program