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P28491

- CALR_PIG

UniProt

P28491 - CALR_PIG

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Protein

Calreticulin

Gene

CALR

Organism
Sus scrofa (Pig)
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 (By similarity). Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis.By similarity1 Publication

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
  3. mRNA binding Source: Ensembl

GO - Biological processi

  1. cell cycle arrest Source: Ensembl
  2. cellular senescence Source: Ensembl
  3. cortical actin cytoskeleton organization Source: Ensembl
  4. negative regulation of intracellular steroid hormone receptor signaling pathway Source: Ensembl
  5. negative regulation of neuron differentiation Source: Ensembl
  6. negative regulation of retinoic acid receptor signaling pathway Source: Ensembl
  7. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  8. peptide antigen assembly with MHC class I protein complex Source: Ensembl
  9. positive regulation of cell cycle Source: Ensembl
  10. positive regulation of cell proliferation Source: Ensembl
  11. positive regulation of dendritic cell chemotaxis Source: Ensembl
  12. positive regulation of DNA replication Source: Ensembl
  13. positive regulation of gene expression Source: Ensembl
  14. positive regulation of phagocytosis Source: Ensembl
  15. positive regulation of substrate adhesion-dependent cell spreading Source: Ensembl
  16. protein export from nucleus Source: Ensembl
  17. protein folding Source: InterPro
  18. protein localization to nucleus Source: Ensembl
  19. protein stabilization Source: UniProtKB
  20. regulation of meiosis Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

Calcium, Lectin, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_201997. Scavenging by Class A Receptors.
REACT_203806. ATF6-alpha activates chaperone genes.
REACT_206877. Scavenging by Class F Receptors.
REACT_209237. Calnexin/calreticulin cycle.

Names & Taxonomyi

Protein namesi
Recommended name:
Calreticulin
Alternative name(s):
CRP55
Calregulin
Endoplasmic reticulum resident protein 60
Short name:
ERp60
HACBP
Gene namesi
Name:CALR
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227: Chromosome 2

Subcellular locationi

Endoplasmic reticulum lumen. Sarcoplasmic reticulum lumen. Cytoplasmperinuclear region. Membrane
Note: During oocyte maturation and after parthenogenetic activation accumulates in the plasma membrane region. In pronuclear and early cleaved embryos localizes weakly to cytoplasm around nucleus and more strongly in the region near the cortex.

GO - Cellular componenti

  1. cytosol Source: Ensembl
  2. endoplasmic reticulum lumen Source: Ensembl
  3. external side of plasma membrane Source: Ensembl
  4. extracellular space Source: Ensembl
  5. extracellular vesicular exosome Source: Ensembl
  6. MHC class I peptide loading complex Source: Ensembl
  7. nucleus Source: Ensembl
  8. perinuclear region of cytoplasm Source: Ensembl
  9. polysome Source: Ensembl
  10. sarcoplasmic reticulum Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Membrane, Sarcoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 17171 PublicationAdd
BLAST
Chaini18 – 417400CalreticulinPRO_0000004175Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi137 ↔ 163By similarity
Modified residuei159 – 1591N6-acetyllysineBy similarity
Modified residuei209 – 2091N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Disulfide bond

Proteomic databases

PaxDbiP28491.

Expressioni

Tissue specificityi

In blastocyst expressed in all blastomeres (at protein level). In embryos, expressed in spleen, kidney, liver, fat, muscle, ovary, granulosa cells and cumulus cells.1 Publication

Developmental stagei

Expressed in immature GV-stage oocytes, mature MII-stage oocytes, parthenogenetically activated MII-stage oocytes and in pronuclear embryos (at protein level). During in vitro oocyte maturation, expression initially increases after 12 hours of culture, followed by a strong decline at 30 hours (MI stage) and 44 hours (MII stage). Expression remains constant in MII-stage oocytes after parthenogenetic activation, increasing in two- and four-cell parthenotes. Not detected in blastocyst stage embryos.1 Publication

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

STRINGi9823.ENSSSCP00000014615.

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

Sequence similaritiesi

Belongs to the calreticulin family.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG305105.
GeneTreeiENSGT00430000030841.
HOGENOMiHOG000192435.
InParanoidiP28491.
KOiK08057.
OMAiVKLFPDG.
OrthoDBiEOG77126Z.
TreeFamiTF338438.

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. 1 hit.
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.

P28491-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLLPVPLLLG LVGLAAAEPT IYFKEQFLDG DGWTDRWIES KHKPDFGRFV
60 70 80 90 100
LSSGKFYGDQ EKDKGLQTSQ DARFYALSAR FEPFSNKGQT LVVQFTVKHE
110 120 130 140 150
QNIDCGGGYV KLFPDGLDQT DMHGDSEYNI MFGPDICGPG TKKVHVIFNY
160 170 180 190 200
KGKNVLINKD IRCKDDEFTH LYTLIVRPDN TYEVKIDNSQ VESGSLEDDW
210 220 230 240 250
DFLPPKKIKD PDAVKPEDWD ERAKIDDPTD SKPEDWDKPE HIPDPDAKKP
260 270 280 290 300
EDWDEEMDGE WEPPVIQNPE YKGEWKPRQI DNPDYKGTWI HPEIDNPEYS
310 320 330 340 350
PDSNIYAYEN FAVLGLDLWQ VKSGTIFDNF LITNDEAYAE EFGNETWGVT
360 370 380 390 400
KAAEKQMKDK QDEEQRLKEE EEEKKRKEEE EVDKEDEEDK DEDEEEEDEK
410
EEEEEEDAAA GQAKDEL
Length:417
Mass (Da):48,288
Last modified:May 16, 2012 - v3
Checksum:i31A9E4CC95F2D54F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti15 – 151A → V in CAA23142. (PubMed:8672129)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
GQ984146 mRNA. Translation: ADD52600.1.
CU463133 Genomic DNA. No translation available.
F14591 mRNA. Translation: CAA23142.1.
PIRiB33208.
RefSeqiNP_001167604.1. NM_001174133.1.
UniGeneiSsc.48945.

Genome annotation databases

EnsembliENSSSCT00000015020; ENSSSCP00000014615; ENSSSCG00000013746.
GeneIDi100381266.
KEGGissc:100381266.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
GQ984146 mRNA. Translation: ADD52600.1 .
CU463133 Genomic DNA. No translation available.
F14591 mRNA. Translation: CAA23142.1 .
PIRi B33208.
RefSeqi NP_001167604.1. NM_001174133.1.
UniGenei Ssc.48945.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9823.ENSSSCP00000014615.

Proteomic databases

PaxDbi P28491.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSSSCT00000015020 ; ENSSSCP00000014615 ; ENSSSCG00000013746 .
GeneIDi 100381266.
KEGGi ssc:100381266.

Organism-specific databases

CTDi 811.

Phylogenomic databases

eggNOGi NOG305105.
GeneTreei ENSGT00430000030841.
HOGENOMi HOG000192435.
InParanoidi P28491.
KOi K08057.
OMAi VKLFPDG.
OrthoDBi EOG77126Z.
TreeFami TF338438.

Enzyme and pathway databases

Reactomei REACT_201997. Scavenging by Class A Receptors.
REACT_203806. ATF6-alpha activates chaperone genes.
REACT_206877. Scavenging by Class F Receptors.
REACT_209237. Calnexin/calreticulin cycle.

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. 1 hit.
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

« Hide 'large scale' publications
  1. "Involvement of ER-calreticulin-Ca2+ signaling in the regulation of porcine oocyte meiotic maturation and maternal gene expression."
    Zhang D.X., Li X.P., Sun S.C., Shen X.H., Cui X.S., Kim N.H.
    Mol. Reprod. Dev. 77:462-471(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Tissue: Oocyte.
  2. Porcine genome sequencing project
    Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "Evaluation and characterization of a porcine small intestine cDNA library: analysis of 839 clones."
    Winteroe A.K., Fredholm M., Davies W.
    Mamm. Genome 7:509-517(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-105.
    Tissue: Small intestine.
  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 18-32, SUBCELLULAR LOCATION.
    Tissue: Uterus.

Entry informationi

Entry nameiCALR_PIG
AccessioniPrimary (citable) accession number: P28491
Secondary accession number(s): D4N5N1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: May 16, 2012
Last modified: October 29, 2014
This is version 96 of the entry and version 3 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