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P52193

- CALR_BOVIN

UniProt

P52193 - CALR_BOVIN

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Protein

Calreticulin

Gene

CALR

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi26 – 261Calcium; via carbonyl oxygenBy similarity
Metal bindingi62 – 621Calcium; via carbonyl oxygenBy similarity
Metal bindingi64 – 641Calcium; via carbonyl oxygenBy similarity
Binding sitei109 – 1091CarbohydrateBy similarity
Binding sitei111 – 1111CarbohydrateBy similarity
Binding sitei128 – 1281CarbohydrateBy similarity
Binding sitei135 – 1351CarbohydrateBy similarity
Binding sitei317 – 3171CarbohydrateBy similarity
Metal bindingi328 – 3281CalciumBy similarity

GO - Molecular functioni

  1. calcium ion binding Source: UniProtKB
  2. carbohydrate binding Source: UniProtKB-KW

GO - Biological processi

  1. protein folding Source: InterPro
  2. protein stabilization Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

Calcium, Lectin, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Calreticulin
Alternative name(s):
CRP55
Calregulin
HACBP
Gene namesi
Name:CALR
Synonyms:CRT
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Unplaced

Subcellular locationi

Endoplasmic reticulum lumen 1 PublicationPROSITE-ProRule annotation. Sarcoplasmic reticulum lumen By similarity

GO - Cellular componenti

  1. sarcoplasmic reticulum Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Sarcoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 17172 PublicationsAdd
BLAST
Chaini18 – 417400CalreticulinPRO_0000004170Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei48 – 481N6-acetyllysineBy similarity
Disulfide bondi137 ↔ 163
Modified residuei159 – 1591N6-acetyllysineBy similarity
Glycosylationi179 – 1791N-linked (GlcNAc...)
Modified residuei209 – 2091N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP52193.
PRIDEiP52193.

Interactioni

Subunit structurei

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. Interacts with PPIB (By similarity).By similarity

Protein-protein interaction databases

IntActiP52193. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP52193.
SMRiP52193. Positions 206-305.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati191 – 202121-1Add
BLAST
Repeati210 – 221121-2Add
BLAST
Repeati227 – 238121-3Add
BLAST
Repeati244 – 255121-4Add
BLAST
Repeati259 – 269112-1Add
BLAST
Repeati273 – 283112-2Add
BLAST
Repeati287 – 297112-3Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni18 – 197180N-domainAdd
BLAST
Regioni191 – 255654 X approximate repeatsAdd
BLAST
Regioni198 – 308111P-domainAdd
BLAST
Regioni237 – 27034Interaction with PPIBBy similarityAdd
BLAST
Regioni259 – 297393 X approximate repeatsAdd
BLAST
Regioni309 – 417109C-domainAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi414 – 4174Prevents secretion from ERPROSITE-ProRule annotation

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi351 – 40757Asp/Glu/Lys-richAdd
BLAST

Domaini

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).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 similaritiesi

Belongs to the calreticulin family.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG305105.
HOGENOMiHOG000192435.
HOVERGENiHBG005407.
InParanoidiP52193.
KOiK08057.

Family and domain databases

Gene3Di2.60.120.200. 2 hits.
InterProiIPR001580. Calret/calnex.
IPR018124. Calret/calnex_CS.
IPR009169. Calreticulin.
IPR009033. Calreticulin/calnexin_P_dom.
IPR013320. ConA-like_dom.
[Graphical view]
PANTHERiPTHR11073. PTHR11073. 1 hit.
PfamiPF00262. Calreticulin. 1 hit.
[Graphical view]
PIRSFiPIRSF002356. Calreticulin. 1 hit.
PRINTSiPR00626. CALRETICULIN.
SUPFAMiSSF49899. SSF49899. 2 hits.
SSF63887. SSF63887. 1 hit.
PROSITEiPS00803. CALRETICULIN_1. 1 hit.
PS00804. CALRETICULIN_2. 1 hit.
PS00805. CALRETICULIN_REPEAT. 3 hits.
PS00014. ER_TARGET. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P52193 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLLPVPLLLG LLGLAAADPT VYFKEQFLDG DGWTERWIES KHKPDFGKFV
60 70 80 90 100
LSSGKFYGDQ EKDKGLQTSQ DARFYALSAR FEPFSNKGQT LVVQFTVKHE
110 120 130 140 150
QNIDCGGGYV KLFPAGLDQT DMHGDSEYNI MFGPDICGPG TKKVHVIFNY
160 170 180 190 200
KGKNVLINKD IRCKDDEFTH LYTLIVRPNN TYEVKIDNSQ VESGSLEDDW
210 220 230 240 250
DFLPPKKIKD PDAAKPEDWD DRAKIDDPTD SKPEDWDKPE HIPDPDAKKP
260 270 280 290 300
EDWDEEMDGE WEPPVIQNPE YKGEWKPRQI DNPEYKGIWI HPEIDNPEYS
310 320 330 340 350
PDSNIYAYEN FAVLGLDLWQ VKSGTIFDNF LITNDEAYAE EFGNETWGVT
360 370 380 390 400
KAAEKQMKDK QDEEQRLHEE EEEKKGKEEE EADKDDDEDK DEDEEDEDEK
410
EEEEEEDAAA GQAKDEL
Length:417
Mass (Da):48,039
Last modified:February 22, 2003 - v2
Checksum:i7BF812C7B5417BE9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 9999MLLPV…FTVKH → MCLNHFLLSLVLSIVLLFHF VFYICLHHIVTFLREETVFF SEQFLTLDLKYKASKLSSIR EALSMSKVGIIENFCFSEIS FLQESIKSHGRRTLVGCSPW GHE in AAC37307. (PubMed:8373827)CuratedAdd
BLAST
Sequence conflicti18 – 214DPTV → EPAI AA sequence (PubMed:2016321)Curated
Sequence conflicti111 – 1122KL → NV in AAC37307. (PubMed:8373827)Curated
Sequence conflicti265 – 2651V → L in AAC37307. (PubMed:8373827)Curated
Sequence conflicti383 – 3831D → E in AAC37307. (PubMed:8373827)Curated
Sequence conflicti411 – 4111G → A in AAC37307. (PubMed:8373827)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L13462 mRNA. Translation: AAC37307.1.
AB067687 mRNA. Translation: BAB86913.1.
PIRiA33208.
S36799.
S43376.
RefSeqiNP_776425.1. NM_174000.2.
UniGeneiBt.30105.

Genome annotation databases

GeneIDi281036.
KEGGibta:281036.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L13462 mRNA. Translation: AAC37307.1 .
AB067687 mRNA. Translation: BAB86913.1 .
PIRi A33208.
S36799.
S43376.
RefSeqi NP_776425.1. NM_174000.2.
UniGenei Bt.30105.

3D structure databases

ProteinModelPortali P52193.
SMRi P52193. Positions 206-305.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P52193. 1 interaction.

Proteomic databases

PaxDbi P52193.
PRIDEi P52193.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 281036.
KEGGi bta:281036.

Organism-specific databases

CTDi 811.

Phylogenomic databases

eggNOGi NOG305105.
HOGENOMi HOG000192435.
HOVERGENi HBG005407.
InParanoidi P52193.
KOi K08057.

Miscellaneous databases

NextBioi 20805123.

Family and domain databases

Gene3Di 2.60.120.200. 2 hits.
InterProi IPR001580. Calret/calnex.
IPR018124. Calret/calnex_CS.
IPR009169. Calreticulin.
IPR009033. Calreticulin/calnexin_P_dom.
IPR013320. ConA-like_dom.
[Graphical view ]
PANTHERi PTHR11073. PTHR11073. 1 hit.
Pfami PF00262. Calreticulin. 1 hit.
[Graphical view ]
PIRSFi PIRSF002356. Calreticulin. 1 hit.
PRINTSi PR00626. CALRETICULIN.
SUPFAMi SSF49899. SSF49899. 2 hits.
SSF63887. SSF63887. 1 hit.
PROSITEi PS00803. CALRETICULIN_1. 1 hit.
PS00804. CALRETICULIN_2. 1 hit.
PS00805. CALRETICULIN_REPEAT. 3 hits.
PS00014. ER_TARGET. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiCALR_BOVIN
AccessioniPrimary (citable) accession number: P52193
Secondary accession number(s): P28489, P42918, Q8SQ53
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: February 22, 2003
Last modified: October 29, 2014
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3