Calreticulin precursor - Rattus norvegicus (Rat)

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Reviewed, UniProtKB/Swiss-Prot P18418 (CALR_RAT)

Last modified November 4, 2008. Version 96. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Calreticulin
Alternative name(s):
    CRP55
    Calregulin
    HACBP
    ERp60
    CALBP
    Calcium-binding protein 3
      Short name=CABP3

Gene names

Name:

Calr

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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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 protein level.

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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 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 By similarity.
Subunit structure	Monomer. Component of an EIF2 complex at least composed of CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5. Interacts with PDIA3/ERp57 and with NR3C1 By similarity.
Subcellular location	Endoplasmic reticulum lumen.
Tissue specificity	Predentin and odontoblast.
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.
Sequence similarities	Belongs to the calreticulin family.
Caution	Was originally (Ref.9) thought to be D-beta-hydroxybutyrate dehydrogenase.

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Ontologies

Keywords
Cellular component	Endoplasmic reticulum
Domain	Repeat Signal
Ligand	Calcium Lectin Metal-binding Zinc
Molecular function	Chaperone
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	negative regulation of translation Inferred from direct assay. Source: UniProtKB
Molecular function	mRNA binding Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 17

Chain

18 – 416

399

Calreticulin

PRO_0000004177

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 – 416

108

C-domain

Motif

413 – 416

Prevents secretion from ER

Compositional bias

351 – 407

Asp/Glu/Lys-rich

Amino acid modifications

Disulfide bond

105 ↔ 137

By similarity

Experimental info

Sequence conflict

269

P → R in CAA31987. Ref.9

Sequence conflict

359 – 361

DKQ → AAG in CAA31987. Ref.9

Secondary structure

416

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P18418-1 [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: 2E6713CED31A2970
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FASTA

416

47,995

        10         20         30         40         50         60 
MLLSVPLLLG LLGLAAADPA IYFKEQFLDG DAWTNRWVES KHKSDFGKFV LSSGKFYGDQ 

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

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

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

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

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

       370        380        390        400        410 
QDEEQRLKEE EEDKKRKEEE EAEDKEDEDD RDEDEDEEDE KEEDEEDATG QAKDEL

« Hide

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structural homology between the rat calreticulin gene product and the Onchocerca volvulus antigen Ral-1." Murthy K.K., Banville D., Srikant C.B., Carrier F., Bell A., Holmes C., Patel Y.C. Nucleic Acids Res. 18:4933-4933(1990) [PubMed: 2395661] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. Tissue: Brain cortex.
[2]	"An endoplasmic reticulum protein, calreticulin, is transported into the acrosome of rat sperm." Nakamura M., Moriya M., Baba T., Michikawa Y., Yamanobe T., Arai K., Okinaga S., Kobayashi T. Exp. Cell Res. 205:101-110(1993) [PubMed: 8453984] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley.
[3]	"Retention and retrieval: both mechanisms cooperate to maintain calreticulin in the endoplasmic reticulum." Soennichsen B., Fuellekrug J., van Nguyen P., Diekmann W., Robinson D.G., Mieskes G. J. Cell Sci. 107:2705-2717(1994) [PubMed: 7876339] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. Tissue: Liver.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Prostate.
[5]	"Calreticulin is present in the acrosome of spermatids of rat testis." Nakamura M., Michikawa Y., Baba T., Okinaga S., Arai K. Biochem. Biophys. Res. Commun. 186:668-673(1992) [PubMed: 1497655] [Abstract] Cited for: PROTEIN SEQUENCE OF 18-32. Strain: Sprague-Dawley. Tissue: Testis.
[6]	"Identification of protein disulfide isomerase and calreticulin as autoimmune antigens in LEC strain of rats." Yokoi T., Nagayama S., Kajiwara R., Kawaguchi Y., Horiuchi R., Kamataki T. Biochim. Biophys. Acta 1158:339-344(1993) [PubMed: 8251535] [Abstract] Cited for: PROTEIN SEQUENCE OF 18-32. Strain: LEC. Tissue: Liver.
[7]	"Calreticulin is a candidate for a calsequestrin-like function in Ca2(+)-storage compartments (calciosomes) of liver and brain." Treves S., de Mattei M., Lanfredi M., Villa A., Green N.M., Maclennan D.H., Meldolesi J., Pozzan T. Biochem. J. 271:473-480(1990) [PubMed: 2241926] [Abstract] Cited for: PROTEIN SEQUENCE OF 18-29.
[8]	Lubec G., Afjehi-Sadat L., Diao W. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 25-36; 88-98 AND 163-185, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Hippocampus and Spinal cord.
[9]	Lone Y.-C., Bailly A., Latruffe N. Submitted (DEC-1988) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 269-361. Strain: Sprague-Dawley.
[10]	"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: 12782144] [Abstract] Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[11]	"TROSY-NMR reveals interaction between ERp57 and the tip of the calreticulin P-domain." Frickel E.M., Riek R., Jelesarov I., Helenius A., Wuethrich K., Ellgaard L. Proc. Natl. Acad. Sci. U.S.A. 99:1954-1959(2002) [PubMed: 11842220] [Abstract] Cited for: INTERACTION WITH PDIA3.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

X53363 mRNA. Translation: CAA37446.1.
D78308 mRNA. Translation: BAA11345.1.
X79327 mRNA. Translation: CAA55890.1.
BC062395 mRNA. Translation: AAH62395.1.
X13702 mRNA. Translation: CAA31987.1.

PIR

JH0819.

RefSeq

NP_071794.1.

UniGene

Rn.974

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1HHN	NMR	-	A	206-305	[»]
1K91	NMR	-	A	238-273	[»]
1K9C	NMR	-	A	206-278	[»]

ModBase

Search...

Genome annotation databases

Ensembl

ENSRNOG00000003029. Rattus norvegicus. [Contig view]

GeneID

64202.

KEGG

rno:64202.

Organism-specific databases

RGD

620288. Calr.

Phylogenomic databases

HOVERGEN

P18418.

Gene expression databases

ArrayExpress

P18418.

GermOnline

ENSRNOG00000003029. Rattus norvegicus.

Family and domain databases

InterPro

IPR001580. Calret/calnex.
IPR009169. Calreticulin.
IPR009033. Calreticulin/calnexin_P.
IPR013320. ConA_like_subgrp.
IPR000886. ER_targeting_sequence.
[Graphical view]

Gene3D

G3DSA:2.10.250.10. Calreticulin/calnexin_P. 1 hit.
G3DSA:2.60.120.200. ConA_like_subgrp. 1 hit.

PANTHER

PTHR11073. Calret/calnex. 1 hit.
PTHR11073:SF2. Calreticulin. 1 hit.

Pfam

PF00262. Calreticulin. 1 hit.
[Graphical view]

PIRSF

PIRSF002356. Calreticulin. 1 hit.

PRINTS

PR00626. CALRETICULIN.

ProDom

PD001866. Calret/calnex. 1 hit.
[Graphical view] [Entries sharing at least one domain]

PROSITE

PS00803. CALRETICULIN_1. 1 hit.
PS00804. CALRETICULIN_2. 1 hit.
PS00805. CALRETICULIN_REPEAT. 3 hits.
PS00014. ER_TARGET. 1 hit.
[Graphical view]

BLOCKS

Search...

ProtoNet

Search...

Other Resources

NextBio

612898.

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Entry information

Entry name

CALR_RAT

Accession

Primary (citable) accession number: P18418
Secondary accession number(s): P10452

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	November 1, 1990
Last modified:	November 4, 2008
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents