Peflin

PEF1
Identifiers
Aliases	PEF1, ABP32, PEF1A, penta-EF-hand domain containing 1
External IDs	MGI: 1915148 HomoloGene: 56569 GeneCards: PEF1
Gene ontology Molecular function • calcium ion binding • poly(A) RNA binding • protein binding • protein dimerization activity • metal ion binding • calcium-dependent cysteine-type endopeptidase activity • protein heterodimerization activity Cellular component • cytoplasm • extracellular exosome • membrane Biological process • response to calcium ion • proteolysis Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	553115	67898
Ensembl	ENSG00000162517	ENSMUSG00000028779
UniProt	Q9UBV8	Q8BFY6
RefSeq (mRNA)	NM_012392	NM_026441
RefSeq (protein)	NP_036524.1	NP_080717.2
Location (UCSC)	Chr 1: 31.63 – 31.64 Mb	Chr 4: 130.1 – 130.13 Mb
PubMed search	[1]	[2]
Wikidata

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Peflin is a protein that in humans is encoded by the PEF1 gene.^[3][4][5]

PEF1 is a Ca(2+)-binding protein that belongs to the penta-EF hand (PEF) protein family, which includes the calpain small subunit (CAPNS1; MIM 114170), sorcin (SRI; MIM 182520), grancalcin (GCA; MIM 607030), and ALG2 (PDCD6; MIM 601057) (Kitaura et al., 2001).[supplied by OMIM]^[5]

Interactions

PEF1 has been shown to interact with PDCD6.^[6]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. Kitaura Y, Watanabe M, Satoh H, Kawai T, Hitomi K, Maki M (Oct 1999). "Peflin, a novel member of the five-EF-hand-protein family, is similar to the apoptosis-linked gene 2 (ALG-2) protein but possesses nonapeptide repeats in the N-terminal hydrophobic region". Biochem Biophys Res Commun. 263 (1): 68–75. doi:10.1006/bbrc.1999.1189. PMID 10486255.
4. Kitaura Y, Satoh H, Takahashi H, Shibata H, Maki M (Mar 2002). "Both ALG-2 and peflin, penta-EF-hand (PEF) proteins, are stabilized by dimerization through their fifth EF-hand regions". Arch Biochem Biophys. 399 (1): 12–8. doi:10.1006/abbi.2001.2736. PMID 11883899.
5. "Entrez Gene: PEF1 penta-EF-hand domain containing 1".
6. Kitaura, Y; Matsumoto S; Satoh H; Hitomi K; Maki M (Apr 2001). "Peflin and ALG-2, members of the penta-EF-hand protein family, form a heterodimer that dissociates in a Ca2+-dependent manner". J. Biol. Chem. United States. 276 (17): 14053–8. doi:10.1074/jbc.M008649200. ISSN 0021-9258. PMID 11278427.

Further reading

• Kitaura Y, Matsumoto S, Satoh H, et al. (2001). "Peflin and ALG-2, members of the penta-EF-hand protein family, form a heterodimer that dissociates in a Ca2+-dependent manner.". J. Biol. Chem. 276 (17): 14053–8. doi:10.1074/jbc.M008649200. PMID 11278427.
• Satoh H, Nakano Y, Shibata H, Maki M (2002). "The penta-EF-hand domain of ALG-2 interacts with amino-terminal domains of both annexin VII and annexin XI in a Ca2+-dependent manner.". Biochim. Biophys. Acta. 1600 (1-2): 61–7. doi:10.1016/S1570-9639(02)00445-4. PMID 12445460.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Hansen C, Tarabykina S, la Cour JM, et al. (2003). "The PEF family proteins sorcin and grancalcin interact in vivo and in vitro.". FEBS Lett. 545 (2-3): 151–4. doi:10.1016/S0014-5793(03)00518-0. PMID 12804766.
• Clark HF, Gurney AL, Abaya E, et al. (2003). "The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment.". Genome Res. 13 (10): 2265–70. doi:10.1101/gr.1293003. PMC 403697. PMID 12975309.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
• Jordanova A, Irobi J, Thomas FP, et al. (2006). "Disrupted function and axonal distribution of mutant tyrosyl-tRNA synthetase in dominant intermediate Charcot-Marie-Tooth neuropathy.". Nat. Genet. 38 (2): 197–202. doi:10.1038/ng1727. PMID 16429158.