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CAMLG
Identifiers
Aliases	CAMLG, CAML, GET2, calcium modulating ligand
External IDs	OMIM: 601118; MGI: 104728; HomoloGene: 1323; GeneCards: CAMLG; OMA:CAMLG - orthologs
Gene location (Human) Chr. Chromosome 5 (human) Band 5q31.1 Start 134,738,495 bp End 134,752,157 bp
Gene location (Mouse) Chr. Chromosome 13 (mouse) Band 13 B1|13 30.06 cM Start 55,770,818 bp End 55,780,224 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in secondary oocyte sperm Brodmann area 23 cartilage tissue ganglionic eminence trigeminal ganglion Achilles tendon superior vestibular nucleus nipple Brodmann area 9 Top expressed in medial ganglionic eminence spermatocyte condyle neural layer of retina fossa facial motor nucleus saccule substantia nigra trigeminal ganglion ventricular zone More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein binding cell adhesion molecule binding ubiquitin protein ligase binding Cellular component integral component of membrane endoplasmic reticulum membrane cytoplasm Biological process defense response viral process receptor recycling epidermal growth factor receptor signaling pathway signal transduction negative regulation of protein ubiquitination negative regulation of proteasomal ubiquitin-dependent protein catabolic process protein stabilization Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 819 12328 Ensembl ENSG00000164615 ENSMUSG00000021501 UniProt P49069 P49070 RefSeq (mRNA) NM_001745 NM_007596 RefSeq (protein) NP_001736 NP_031622 Location (UCSC) Chr 5: 134.74 – 134.75 Mb Chr 13: 55.77 – 55.78 Mb PubMed search
Wikidata
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Calcium modulating ligand (CAMLG or CAML), also known as calcium-modulating cyclophilin ligand, is a signalling protein recognized by the TNF receptor TACI.

Function

The immunosuppressant drug cyclosporin A blocks a calcium-dependent signal from the T-cell receptor (TCR) that normally leads to T-cell activation. When bound to cyclophilin B, cyclosporin A binds and inactivates the key signaling intermediate calcineurin. The protein encoded by this gene functions similarly to cyclosporin A, binding to cyclophilin B and acting downstream of the TCR and upstream of calcineurin by causing an influx of calcium. This integral membrane protein appears to be a new participant in the calcium signal transduction pathway, implicating cyclophilin B in calcium signaling, even in the absence of cyclosporin.

Interactions

CAMLG has been shown to interact with TNFRSF13B.

References

1. ^ GRCh38: Ensembl release 89: ENSG00000164615 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000021501 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Bram RJ, Valentine V, Shapiro DN, Jenkins NA, Gilbert DJ, Copeland NG (March 1997). "The gene for calcium-modulating cyclophilin ligand (CAMLG) is located on human chromosome 5q23 and a syntenic region of mouse chromosome 13". Genomics. 31 (2): 257–60. doi:10.1006/geno.1996.0044. PMID 8824814.
6. ^ "Entrez Gene: CAMLG calcium modulating ligand".
7. von Bülow GU, Bram RJ (October 1997). "NF-AT activation induced by a CAML-interacting member of the tumor necrosis factor receptor superfamily". Science. 278 (5335): 138–41. doi:10.1126/science.278.5335.138. PMID 9311921.
8. Xia XZ, Treanor J, Senaldi G, Khare SD, Boone T, Kelley M, Theill LE, Colombero A, Solovyev I, Lee F, McCabe S, Elliott R, Miner K, Hawkins N, Guo J, Stolina M, Yu G, Wang J, Delaney J, Meng SY, Boyle WJ, Hsu H (July 2000). "TACI is a TRAF-interacting receptor for TALL-1, a tumor necrosis factor family member involved in B cell regulation". J. Exp. Med. 192 (1): 137–43. doi:10.1084/jem.192.1.137. PMC 1887716. PMID 10880535.

Further reading

• Bram RJ, Crabtree GR (1994). "Calcium signalling in T cells stimulated by a cyclophilin B-binding protein". Nature. 371 (6495): 355–8. Bibcode:1994Natur.371..355B. doi:10.1038/371355a0. PMID 7522304. S2CID 4318545.
• von Bülow GU, Bram RJ (1997). "NF-AT activation induced by a CAML-interacting member of the tumor necrosis factor receptor superfamily". Science. 278 (5335): 138–41. doi:10.1126/science.278.5335.138. PMID 9311921.
• Holloway MP, Bram RJ (1998). "Co-localization of calcium-modulating cyclophilin ligand with intracellular calcium pools". J. Biol. Chem. 273 (26): 16346–50. doi:10.1074/jbc.273.26.16346. PMID 9632697.
• Tovey SC, Bootman MD, Lipp P, Berridge MJ, Bram RJ (2000). "Calcium-modulating cyclophilin ligand desensitizes hormone-evoked calcium release". Biochem. Biophys. Res. Commun. 276 (1): 97–100. doi:10.1006/bbrc.2000.3442. PMID 11006089.
• Larramendy ML, Niini T, Elonen E, Nagy B, Ollila J, Vihinen M, Knuutila S (2003). "Overexpression of translocation-associated fusion genes of FGFRI, MYC, NPMI, and DEK, but absence of the translocations in acute myeloid leukemia. A microarray analysis". Haematologica. 87 (6): 569–77. PMID 12031912.
• Feng P, Park J, Lee BS, Lee SH, Bram RJ, Jung JU (2002). "Kaposi's sarcoma-associated herpesvirus mitochondrial K7 protein targets a cellular calcium-modulating cyclophilin ligand to modulate intracellular calcium concentration and inhibit apoptosis". J. Virol. 76 (22): 11491–504. doi:10.1128/JVI.76.22.11491-11504.2002. PMC 136794. PMID 12388711.
• Tran DD, Russell HR, Sutor SL, van Deursen J, Bram RJ (2003). "CAML is required for efficient EGF receptor recycling". Dev. Cell. 5 (2): 245–56. doi:10.1016/S1534-5807(03)00207-7. PMID 12919676.
• Kumar R, Lutz W, Frank E, Im HJ (2004). "Immediate early gene X-1 interacts with proteins that modulate apoptosis". Biochem. Biophys. Res. Commun. 323 (4): 1293–8. doi:10.1016/j.bbrc.2004.09.006. PMC 2895269. PMID 15451437.
• Guo S, Lopez-Ilasaca M, Dzau VJ (2005). "Identification of calcium-modulating cyclophilin ligand (CAML) as transducer of angiotensin II-mediated nuclear factor of activated T cells (NFAT) activation". J. Biol. Chem. 280 (13): 12536–41. doi:10.1074/jbc.M500296200. PMID 15668245.
• Nagano J, Kitamura K, Hujer KM, Ward CJ, Bram RJ, Hopfer U, Tomita K, Huang C, Miller RT (2006). "Fibrocystin interacts with CAML, a protein involved in Ca2+ signaling". Biochem. Biophys. Res. Commun. 338 (2): 880–9. doi:10.1016/j.bbrc.2005.10.022. PMID 16243292.

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