ARMET

Protein-coding gene in the species Homo sapiens

MANF
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2KVD, 2KVE, 2W51

Identifiers
AliasesMANF, ARMET, ARP, arginine-rich, mutated in early-stage tumors, arginine-rich protein, mesencephalic astrocyte-derived neurotrophic factor, mesencephalic astrocyte derived neurotrophic factor
External IDsOMIM: 601916; MGI: 1922090; HomoloGene: 4383; GeneCards: MANF; OMA:MANF - orthologs
Gene location (Human)
Chromosome 3 (human)
Chr.Chromosome 3 (human)[1]
Chromosome 3 (human)
Genomic location for MANF
Genomic location for MANF
Band3p21.2Start51,385,291 bp[1]
End51,389,397 bp[1]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • islet of Langerhans

  • beta cell

  • body of pancreas

  • right lobe of thyroid gland

  • left lobe of thyroid gland

  • mucosa of transverse colon

  • anterior pituitary

  • left testis

  • right testis

  • pericardium
    n/a
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • growth factor activity
  • RNA binding
  • lipid binding
  • sulfatide binding
Cellular component
  • nucleus
  • extracellular region
  • extracellular space
  • endoplasmic reticulum
  • cytosol
  • endoplasmic reticulum lumen
  • sarcoplasmic reticulum
  • sarcoplasmic reticulum lumen
Biological process
  • response to unfolded protein
  • platelet degranulation
  • neuron projection development
  • dopaminergic neuron differentiation
  • regulation of signaling receptor activity
  • regulation of response to endoplasmic reticulum stress
  • signal transduction
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

7873

74840

Ensembl

ENSG00000145050

ENSMUSG00000032575

UniProt

P55145

Q9CXI5

RefSeq (mRNA)

NM_006010

NM_029103

RefSeq (protein)

NP_006001

n/a

Location (UCSC)Chr 3: 51.39 – 51.39 Mbn/a
PubMed search[2][3]
Wikidata
View/Edit HumanView/Edit Mouse

Arginine-rich, mutated in early-stage tumors (ARMET), arginine-rich protein (ARP), or mesencephalic astrocyte-derived neurotrophic factor (MANF) is a protein that in humans is encoded by the MANF housekeeping gene.[4][5]

This gene encodes a highly conserved protein whose function is known. The protein was initially thought to be longer at the N-terminus and to contain an arginine-rich region but transcribed evidence indicates a smaller open reading frame that does not encode the arginine tract. The presence of a specific mutation changing the previously numbered codon 50 from ATG to AGG, or deletion of that codon, has been reported in a variety of solid tumors. With the protein size correction, this codon is now identified as the initiation codon.[5]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000145050 – Ensembl, May 2017
  2. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ Petrova P, Raibekas A, Pevsner J, Vigo N, Anafi M, Moore MK, Peaire AE, Shridhar V, Smith DI, Kelly J, Durocher Y, Commissiong JW (Jun 2003). "MANF: a new mesencephalic, astrocyte-derived neurotrophic factor with selectivity for dopaminergic neurons". J Mol Neurosci. 20 (2): 173–88. doi:10.1385/JMN:20:2:173. PMID 12794311. S2CID 218459504.
  5. ^ a b "Entrez Gene: ARMET arginine-rich, mutated in early stage tumors".

Further reading

  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • Gevaert K, Goethals M, Martens L, et al. (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801. S2CID 23783563.
  • Lai MC, Kuo HW, Chang WC, Tarn WY (2003). "A novel splicing regulator shares a nuclear import pathway with SR proteins". EMBO J. 22 (6): 1359–69. doi:10.1093/emboj/cdg126. PMC 151058. PMID 12628928.
  • 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Tanaka H, Shimada Y, Harada H, et al. (2000). "Polymorphic variation of the ARP gene on 3p21 in Japanese esophageal cancer patients". Oncol. Rep. 7 (3): 591–3. doi:10.3892/or.7.3.591. PMID 10767373.
  • Shridhar V, Rivard S, Wang X, et al. (1997). "Mutations in the arginine-rich protein gene (ARP) in pancreatic cancer". Oncogene. 14 (18): 2213–6. doi:10.1038/sj.onc.1201054. PMID 9174057. S2CID 21313298.
  • Shridhar R, Shridhar V, Rivard S, et al. (1997). "Mutations in the arginine-rich protein gene, in lung, breast, and prostate cancers, and in squamous cell carcinoma of the head and neck". Cancer Res. 56 (24): 5576–8. PMID 8971156.
  • Shridhar V, Rivard S, Shridhar R, et al. (1996). "A gene from human chromosomal band 3p21.1 encodes a highly conserved arginine-rich protein and is mutated in renal cell carcinomas". Oncogene. 12 (9): 1931–9. PMID 8649854.


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