Calreticulin precursor - Bos taurus (Bovine)

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P52193 (CALR_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 106. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Calreticulin

Alternative name(s):
CRP55
Calregulin
HACBP

Gene names

Name:	CALR
Synonyms:	CRT

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	417 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	Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export. Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis By similarity.
Subunit structure	Monomer. Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5. Interacts with GABARAP, NR3C1, PDIA3/ERp57 and TRIM21 By similarity.
Subcellular location	Endoplasmic reticulum lumen. Sarcoplasmic reticulum lumen By similarity Ref.5.
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. Associates with PDIA3 through the tip of the extended arm formed by the P-domain By similarity.
Sequence similarities	Belongs to the calreticulin family.

Ontologies

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 17

Ref.3 Ref.4

Chain

18 – 417

400

Calreticulin

PRO_0000004170

Regions

Repeat

191 – 202

1-1

Repeat

210 – 221

1-2

Repeat

227 – 238

1-3

Repeat

244 – 255

1-4

Repeat

259 – 269

2-1

Repeat

273 – 283

2-2

Repeat

287 – 297

2-3

Region

18 – 197

180

N-domain

Region

191 – 255

4 X approximate repeats

Region

198 – 308

111

P-domain

Region

259 – 297

3 X approximate repeats

Region

309 – 417

109

C-domain

Motif

414 – 417

Prevents secretion from ER Potential

Compositional bias

351 – 407

Asp/Glu/Lys-rich

Sites

Metal binding

Calcium; via carbonyl oxygen By similarity

Metal binding

Calcium; via carbonyl oxygen By similarity

Metal binding

Calcium; via carbonyl oxygen By similarity

Metal binding

328

Calcium By similarity

Binding site

109

Carbohydrate By similarity

Binding site

111

Carbohydrate By similarity

Binding site

128

Carbohydrate By similarity

Binding site

135

Carbohydrate By similarity

Binding site

317

Carbohydrate By similarity

Amino acid modifications

Modified residue

N6-acetyllysine By similarity

Modified residue

159

N6-acetyllysine By similarity

Modified residue

209

N6-acetyllysine By similarity

Glycosylation

179

N-linked (GlcNAc...)

Disulfide bond

137 ↔ 163

Experimental info

Sequence conflict

1 – 99

MLLPV…FTVKH → MCLNHFLLSLVLSIVLLFHF VFYICLHHIVTFLREETVFF SEQFLTLDLKYKASKLSSIR EALSMSKVGIIENFCFSEIS FLQESIKSHGRRTLVGCSPW GHE in AAC37307. Ref.1

Sequence conflict

18 – 21

DPTV → EPAI AA sequence Ref.4

Sequence conflict

111 – 112

KL → NV in AAC37307. Ref.1

Sequence conflict

265

V → L in AAC37307. Ref.1

Sequence conflict

383

D → E in AAC37307. Ref.1

Sequence conflict

411

G → A in AAC37307. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P52193 [UniParc].

Last modified February 22, 2003. Version 2.
Checksum: 7BF812C7B5417BE9
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FASTA

417

48,039

        10         20         30         40         50         60 
MLLPVPLLLG LLGLAAADPT VYFKEQFLDG DGWTERWIES KHKPDFGKFV LSSGKFYGDQ 

        70         80         90        100        110        120 
EKDKGLQTSQ DARFYALSAR FEPFSNKGQT LVVQFTVKHE QNIDCGGGYV KLFPAGLDQT 

       130        140        150        160        170        180 
DMHGDSEYNI MFGPDICGPG TKKVHVIFNY KGKNVLINKD IRCKDDEFTH LYTLIVRPNN 

       190        200        210        220        230        240 
TYEVKIDNSQ VESGSLEDDW DFLPPKKIKD PDAAKPEDWD DRAKIDDPTD SKPEDWDKPE 

       250        260        270        280        290        300 
HIPDPDAKKP EDWDEEMDGE WEPPVIQNPE YKGEWKPRQI DNPEYKGIWI HPEIDNPEYS 

       310        320        330        340        350        360 
PDSNIYAYEN FAVLGLDLWQ VKSGTIFDNF LITNDEAYAE EFGNETWGVT KAAEKQMKDK 

       370        380        390        400        410 
QDEEQRLHEE EEEKKGKEEE EADKDDDEDK DEDEEDEDEK EEEEEEDAAA GQAKDEL

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References

[1]	"Comparison of cDNAs from bovine brain coding for two isoforms of calreticulin." Liu N., Fine R.E., Johnson R.J. Biochim. Biophys. Acta 1202:70-76(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[2]	"Bovine brain calreticulin." Hossain M.A., Takuwa K., Minakata H., Nakajima T. Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[3]	"Covalent structure of bovine brain calreticulin." Matsuoka K., Seta K., Yamakawa Y., Okuyama T., Shinoda T., Isobe T. Biochem. J. 298:435-442(1994) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 18-417. Tissue: Brain.
[4]	"Calreticulin, and not calsequestrin, is the major calcium binding protein of smooth muscle sarcoplasmic reticulum and liver endoplasmic reticulum." Milner R.E., Baksh S., Shemanko C., Carpenter M.R., Smillie L., Vance J.E., Opas M., Michalak M. J. Biol. Chem. 266:7155-7165(1991) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 18-30. Tissue: Liver.
[5]	"Calreticulin -- an endoplasmic reticulum protein with calcium-binding activity is also found in the extracellular matrix." Somogyi E., Petersson U., Hultenby K., Wendel M. Matrix Biol. 22:179-191(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, SUBCELLULAR LOCATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L13462 mRNA. Translation: AAC37307.1. AB067687 mRNA. Translation: BAB86913.1.
IPI	IPI00691963.
PIR	A33208. S36799. S43376.
RefSeq	NP_776425.1. NM_174000.2.
UniGene	Bt.30105.
3D structure databases
ProteinModelPortal	P52193.
SMR	P52193. Positions 206-305.
ModBase	Search...
Protein-protein interaction databases
IntAct	P52193. 1 interaction.
Proteomic databases
PaxDb	P52193.
PRIDE	P52193.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	281036.
KEGG	bta:281036.
Organism-specific databases
CTD	811.
Phylogenomic databases
eggNOG	NOG305105.
HOGENOM	HOG000192435.
HOVERGEN	HBG005407.
InParanoid	P52193.
KO	K08057.
OrthoDB	EOG41JZCD.
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. 2 hits.
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...
Other
NextBio	20805123.

Entry information

Entry name

CALR_BOVIN

Accession

Primary (citable) accession number: P52193
Secondary accession number(s): P28489, P42918, Q8SQ53

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	February 22, 2003
Last modified:	April 3, 2013
This is version 106 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents