Calr | ENSRNOG00000003029 | NCBI 64202

Details for: Calr

Gene ID: 64202

Symbol: Calr

Ensembl ID: ENSRNOG00000003029

Description: calreticulin

Associated with

Adaptive immune system
(R-RNO-1280218)
Antigen presentation: folding, assembly and peptide loading of class i mhc
(R-RNO-983170)
Antigen processing-cross presentation
(R-RNO-1236975)
Asparagine n-linked glycosylation
(R-RNO-446203)
Binding and uptake of ligands by scavenger receptors
(R-RNO-2173782)
Calnexin/calreticulin cycle
(R-RNO-901042)
Class i mhc mediated antigen processing & presentation
(R-RNO-983169)
Er-phagosome pathway
(R-RNO-1236974)
Immune system
(R-RNO-168256)
Metabolism of proteins
(R-RNO-392499)
N-glycan trimming in the er and calnexin/calreticulin cycle
(R-RNO-532668)
Post-translational protein modification
(R-RNO-597592)
Scavenging by class a receptors
(R-RNO-3000480)
Vesicle-mediated transport
(R-RNO-5653656)
Acrosomal vesicle
(GO:0001669)
Calcium ion binding
(GO:0005509)
Carbohydrate binding
(GO:0030246)
Cardiac muscle cell differentiation
(GO:0055007)
Cell surface
(GO:0009986)
Cellular response to electrical stimulus
(GO:0071257)
Cellular response to lithium ion
(GO:0071285)
Cellular response to organic substance
(GO:0071310)
Cellular response to virus
(GO:0098586)
Cellular senescence
(GO:0090398)
Collagen-containing extracellular matrix
(GO:0062023)
Complement component c1q complex binding
(GO:0001849)
Cortical actin cytoskeleton organization
(GO:0030866)
Cortical granule
(GO:0060473)
Cytolytic granule
(GO:0044194)
Cytoplasm
(GO:0005737)
Cytosol
(GO:0005829)
Endoplasmic reticulum
(GO:0005783)
Endoplasmic reticulum lumen
(GO:0005788)
Endoplasmic reticulum membrane
(GO:0005789)
Endoplasmic reticulum quality control compartment
(GO:0044322)
Erad pathway
(GO:0036503)
External side of plasma membrane
(GO:0009897)
Extracellular region
(GO:0005576)
Extracellular space
(GO:0005615)
Hormone binding
(GO:0042562)
Integrin binding
(GO:0005178)
Iron ion binding
(GO:0005506)
Membrane
(GO:0016020)
Mhc class i peptide loading complex
(GO:0042824)
Molecular sequestering activity
(GO:0140313)
Mrna binding
(GO:0003729)
Negative regulation of dna-templated transcription
(GO:0045892)
Negative regulation of intracellular steroid hormone receptor signaling pathway
(GO:0033144)
Negative regulation of neuron differentiation
(GO:0045665)
Negative regulation of retinoic acid receptor signaling pathway
(GO:0048387)
Negative regulation of transcription by rna polymerase ii
(GO:0000122)
Negative regulation of translation
(GO:0017148)
Negative regulation of trophoblast cell migration
(GO:1901164)
Nuclear androgen receptor binding
(GO:0050681)
Nuclear envelope
(GO:0005635)
Nuclear export signal receptor activity
(GO:0005049)
Nucleus
(GO:0005634)
Peptide antigen assembly with mhc class i protein complex
(GO:0002502)
Peptide binding
(GO:0042277)
Perinuclear region of cytoplasm
(GO:0048471)
Positive regulation of cell cycle
(GO:0045787)
Positive regulation of cell population proliferation
(GO:0008284)
Positive regulation of dendritic cell chemotaxis
(GO:2000510)
Positive regulation of endothelial cell migration
(GO:0010595)
Positive regulation of gene expression
(GO:0010628)
Positive regulation of non-canonical nf-kappab signal transduction
(GO:1901224)
Positive regulation of phagocytosis
(GO:0050766)
Positive regulation of substrate adhesion-dependent cell spreading
(GO:1900026)
Protein-containing complex
(GO:0032991)
Protein binding
(GO:0005515)
Protein export from nucleus
(GO:0006611)
Protein folding
(GO:0006457)
Protein localization to nucleus
(GO:0034504)
Protein stabilization
(GO:0050821)
Regulation of meiotic nuclear division
(GO:0040020)
Response to estradiol
(GO:0032355)
Response to glycoside
(GO:1903416)
Response to organic substance
(GO:0010033)
Response to testosterone
(GO:0033574)
Response to xenobiotic stimulus
(GO:0009410)
Ribosome
(GO:0005840)
Sarcoplasmic reticulum
(GO:0016529)
Sarcoplasmic reticulum lumen
(GO:0033018)
Smooth endoplasmic reticulum
(GO:0005790)
Spermatogenesis
(GO:0007283)
Ubiquitin protein ligase binding
(GO:0031625)
Unfolded protein binding
(GO:0051082)

Other Information

Proteins

Calreticulin

Genular Protein ID: 1214620324

Symbol: CALR_RAT

Name: Calreticulin

UniProtKB Accession Codes:

P18418 P10452

Database IDs:

Citations:

PubMed ID: 2395661

Title: Structural homology between the rat calreticulin gene product and the Onchocerca volvulus antigen Ral-1.

PubMed ID: 2395661

DOI: 10.1093/nar/18.16.4933

PubMed ID: 8453984

Title: An endoplasmic reticulum protein, calreticulin, is transported into the acrosome of rat sperm.

PubMed ID: 8453984

DOI: 10.1006/excr.1993.1063

PubMed ID: 7876339

Title: Retention and retrieval: both mechanisms cooperate to maintain calreticulin in the endoplasmic reticulum.

PubMed ID: 7876339

DOI: 10.1242/jcs.107.10.2705

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 1497655

Title: Calreticulin is present in the acrosome of spermatids of rat testis.

PubMed ID: 1497655

DOI: 10.1016/0006-291x(92)90798-p

PubMed ID: 8251535

Title: Identification of protein disulfide isomerase and calreticulin as autoimmune antigens in LEC strain of rats.

PubMed ID: 8251535

DOI: 10.1016/0304-4165(93)90033-5

PubMed ID: 2241926

Title: Calreticulin is a candidate for a calsequestrin-like function in Ca2(+)-storage compartments (calciosomes) of liver and brain.

PubMed ID: 2241926

DOI: 10.1042/bj2710473

PubMed ID: 12782144

Title: Calreticulin -- an endoplasmic reticulum protein with calcium-binding activity is also found in the extracellular matrix.

PubMed ID: 12782144

DOI: 10.1016/s0945-053x(02)00117-8

PubMed ID: 11842220

Title: TROSY-NMR reveals interaction between ERp57 and the tip of the calreticulin P-domain.

PubMed ID: 11842220

DOI: 10.1073/pnas.042699099

PubMed ID: 11248044

Title: NMR structure of the calreticulin P-domain.

PubMed ID: 11248044

DOI: 10.1073/pnas.051630098

PubMed ID: 12270713

Title: NMR structures of 36 and 73-residue fragments of the calreticulin P-domain.

PubMed ID: 12270713

DOI: 10.1016/s0022-2836(02)00812-4

Sequence Information:

Length: 416
Mass: 47995
Checksum: 2E6713CED31A2970
Sequence:

MLLSVPLLLG LLGLAAADPA IYFKEQFLDG DAWTNRWVES KHKSDFGKFV LSSGKFYGDQ 
EKDKGLQTSQ DARFYALSAR FEPFSNKGQT LVVQFTVKHE QNIDCGGGYV KLFPGGLDQK 
DMHGDSEYNI MFGPDICGPG TKKVHVIFNY KGKNVLINKD IRCKDDEFTH LYTLIVRPDN 
TYEVKIDNSQ VESGSLEDDW DFLPPKKIKD PDAAKPEDWD ERAKIDDPTD SKPEDWDKPE 
HIPDPDAKKP EDWDEEMDGE WEPPVIQNPE YKGEWKPRQI DNPDYKGTWI HPEIDNPEYS 
PDANIYAYDS FAVLGLDLWQ VKSGTIFDNF LITNDEAYAE EFGNETWGVT KAAEKQMKDK 
QDEEQRLKEE EEDKKRKEEE EAEDKEDEDD RDEDEDEEDE KEEDEEDATG QAKDEL

The gene details are incomplete or unavailable at the moment.

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.

Details for: Calr

Associated with

Other Information

Structural homology between the rat calreticulin gene product and the Onchocerca volvulus antigen Ral-1. PubMed ID: 2395661

An endoplasmic reticulum protein, calreticulin, is transported into the acrosome of rat sperm. PubMed ID: 8453984

Retention and retrieval: both mechanisms cooperate to maintain calreticulin in the endoplasmic reticulum. PubMed ID: 7876339

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

Calreticulin is present in the acrosome of spermatids of rat testis. PubMed ID: 1497655

Identification of protein disulfide isomerase and calreticulin as autoimmune antigens in LEC strain of rats. PubMed ID: 8251535

Calreticulin is a candidate for a calsequestrin-like function in Ca2(+)-storage compartments (calciosomes) of liver and brain. PubMed ID: 2241926

Calreticulin -- an endoplasmic reticulum protein with calcium-binding activity is also found in the extracellular matrix. PubMed ID: 12782144

TROSY-NMR reveals interaction between ERp57 and the tip of the calreticulin P-domain. PubMed ID: 11842220

NMR structure of the calreticulin P-domain. PubMed ID: 11248044

NMR structures of 36 and 73-residue fragments of the calreticulin P-domain. PubMed ID: 12270713