Extracellular matrix protein 1

Protein found in humans

ECM1

Identifiers
Aliases| ECM1, URBWD, extracellular matrix protein 1
External IDs| OMIM: 602201; MGI: 103060; HomoloGene: 3260; GeneCards: ECM1; OMA:ECM1 - orthologs
| Gene location (Human)

Chr.| Chromosome 1 (human)[1]

Band| 1q21.2| Start| 150,508,062 bp[1]
End| 150,513,789 bp[1]
| Gene location (Mouse)

Chr.| Chromosome 3 (mouse)[2]

Band| 3 F2.1|3 40.91 cM| Start| 95,641,459 bp[2]
End| 95,646,881 bp[2]
| RNA expression pattern

Bgee| | Human| Mouse (ortholog)

|

| Top expressed in

* buccal mucosa cell

* mucosa of pharynx

* stromal cell of endometrium

* oral cavity

* tail of epididymis

* gallbladder

* amniotic fluid

* body of tongue

* epithelium of esophagus

* corpus epididymis

| Top expressed in

* esophagus

* adrenal gland

* urinary bladder

* lip

* zone of skin

* white adipose tissue

* human kidney

* right kidney

* liver

* duodenum

More reference expression data
BioGPS| |

More reference expression data
| Gene ontology

Molecular function|

* interleukin-2 receptor binding
* signal transducer activity
* protease binding
* protein C-terminus binding
* protein binding
* enzyme binding
* laminin binding

Cellular component|

* extracellular matrix
* extracellular exosome
* extracellular region
* platelet dense granule lumen
* extracellular space

Biological process|

* regulation of T cell migration
* negative regulation of peptidase activity
* negative regulation of bone mineralization
* positive regulation of endothelial cell proliferation
* ossification
* regulation of bone mineralization
* regulation of transcription by RNA polymerase II
* biomineral tissue development
* negative regulation of cytokine-mediated signaling pathway
* positive regulation of angiogenesis
* angiogenesis
* positive regulation of I-kappaB kinase/NF-kappaB signaling
* inflammatory response
* regulation of type 2 immune response
* platelet degranulation
* signal transduction

Sources:Amigo / QuickGO
| Orthologs

Species| Human| Mouse
Entrez| |

1893

13601

Ensembl| |

ENSG00000143369

ENSMUSG00000028108

UniProt| |

Q16610

Q61508

RefSeq (mRNA)| |

NM_022664
NM_001202858
NM_004425

NM_001252653
NM_007899
NM_001355070

RefSeq (protein)| |

NP_001189787
NP_004416
NP_073155

NP_001239582
NP_031925
NP_001341999

Location (UCSC)| Chr 1: 150.51 – 150.51 Mb| Chr 3: 95.64 – 95.65 Mb
PubMed search| [3]| [4]
Wikidata
| View/Edit Human| View/Edit Mouse

|

Extracellular matrix protein 1 is a protein that in humans is encoded by the ECM1 gene.[5][6][7]

This gene encodes an extracellular protein containing motifs with a cysteine pattern characteristic of the cysteine pattern of the ligand-binding "double-loop" domains of the albumin protein family. This gene maps outside the epidermal differentiation complex (EDC), a cluster of three gene families involved in epidermal differentiation. Alternatively spliced transcript variants encoding distinct isoforms have been described.[7]

## Diseases

[edit]

ECM1 is implicated in breast cancer, thyroid cancer, hepatocellular carcinoma, and other cancers, and also in ulcerative colitis[8] Germline mutations in ECM-1 cause the genetic disease lipoid proteinosis. Autoimmune attack on ECM-1 is responsible for lichen sclerosus. (see the Atlas of Genetics and Cytogenetics in Oncology and Haematology[9]).

## See also

[edit]

* Lipoid proteinosis

## References

[edit]

1. ^ a b c GRCh38: Ensembl release 89: ENSG00000143369 - Ensembl, May 2017
2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000028108 - 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. ^ Smits P, Ni J, Feng P, Wauters J, Van Hul W, Boutaibi ME, Dillon PJ, Merregaert J (Jan 1998). "The human extracellular matrix gene 1 (ECM1): genomic structure, cDNA cloning, expression pattern, and chromosomal localization". Genomics. 45 (3): 487–95. doi:10.1006/geno.1997.4918. PMID 9367673.
6. ^ Johnson MR, Wilkin DJ, Vos HL, Ortiz de Luna RI, Dehejia AM, Polymeropoulos MH, Francomano CA (May 1998). "Characterization of the human extracellular matrix protein 1 gene on chromosome 1q21". Matrix Biol. 16 (5): 289–92. doi:10.1016/S0945-053X(97)90017-2. PMID 9501329.
7. ^ a b "Entrez Gene: ECM1 extracellular matrix protein 1".
8. ^ "ECM1 (Extracellular matrix protein 1)"..
9. ^ "Atlas of Genetics and Cytogenetics in Oncology and Haematology". atlasgeneticsoncology.org.

## Further reading

[edit]

* Viliavin GD, Panchenko KP, Nishanov F, Budaev KD (1978). "[Acid-producing function of the stomach in pyloric ulcers]". Sovetskaia Meditsina (12): 43–5. PMID 601588.
* Smits P, Poumay Y, Karperien M, et al. (2000). "Differentiation-dependent alternative splicing and expression of the extracellular matrix protein 1 gene in human keratinocytes". J. Invest. Dermatol. 114 (4): 718–24. doi:10.1046/j.1523-1747.2000.00916.x. PMID 10733679.
* Hamada T, McLean WH, Ramsay M, et al. (2002). "Lipoid proteinosis maps to 1q21 and is caused by mutations in the extracellular matrix protein 1 gene (ECM1)". Hum. Mol. Genet. 11 (7): 833–40. doi:10.1093/hmg/11.7.833. PMID 11929856.
* 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.
* Hamada T, Wessagowit V, South AP, et al. (2003). "Extracellular matrix protein 1 gene (ECM1) mutations in lipoid proteinosis and genotype-phenotype correlation". J. Invest. Dermatol. 120 (3): 345–50. doi:10.1046/j.1523-1747.2003.12073.x. PMID 12603844.
* Matsuda A, Suzuki Y, Honda G, et al. (2003). "Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways". Oncogene. 22 (21): 3307–18. doi:10.1038/sj.onc.1206406. PMID 12761501.
* Wang L, Yu J, Ni J, et al. (2003). "Extracellular matrix protein 1 (ECM1) is over-expressed in malignant epithelial tumors". Cancer Lett. 200 (1): 57–67. doi:10.1016/S0304-3835(03)00350-1. PMID 14550953.
* 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.
* Horev L, Potikha T, Ayalon S, et al. (2006). "A novel splice-site mutation in ECM-1 gene in a consanguineous family with lipoid proteinosis". Exp. Dermatol. 14 (12): 891–7. doi:10.1111/j.1600-0625.2005.00374.x. PMID 16274456. S2CID 25598548.
* Liu T, Qian WJ, Gritsenko MA, et al. (2006). "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry". J. Proteome Res. 4 (6): 2070–80. doi:10.1021/pr0502065. PMC 1850943. PMID 16335952.
* Fujimoto N, Terlizzi J, Aho S, et al. (2006). "Extracellular matrix protein 1 inhibits the activity of matrix metalloproteinase 9 through high-affinity protein/protein interactions". Exp. Dermatol. 15 (4): 300–7. doi:10.1111/j.0906-6705.2006.00409.x. PMID 16512877. S2CID 40715604.
* Lim J, Hao T, Shaw C, et al. (2006). "A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration". Cell. 125 (4): 801–14. doi:10.1016/j.cell.2006.03.032. PMID 16713569. S2CID 13709685.
* Han B, Zhang X, Liu Q, et al. (2007). "Homozygous missense mutation in the ECM1 gene in Chinese siblings with lipoid proteinosis". Acta Derm. Venereol. 87 (5): 387–9. doi:10.2340/00015555-0292. PMID 17721643.

* v
* t
* e

Protein: scleroproteins

Extracellular
matrix|

| Collagen|

| Fibril forming|

* type I
* COL1A1
* COL1A2
* type II (COL2A1)
* type III
* type V
* COL5A1
* COL5A2
* COL5A3
* COL24A1
* COL26A1

|

Other|

* FACIT: type IX
* COL9A1
* COL9A2
* COL9A3
* type XII (COL12A1)
* COL14A1
* COL16A1
* COL19A1
* COL20A1
* COL21A1
* COL22A1

* basement membrane: type IV
* COL4A1
* COL4A2
* COL4A3
* COL4A4
* COL4A5
* COL4A6

* multiplexin: COL15A1
* type XVIII
* COL18A1
* Endostatin

* transmembrane: COL13A1
* COL17A1
* COL23A1
* COL25A1

* other: type VI
* COL6A1
* COL6A2
* COL6A3
* COL6A5
* type VII (COL7A1)
* type VIII
* COL8A1
* COL8A2
* type X (COL10A1)
* type XI
* COL11A1
* COL11A2
* COL27A1
* COL28A1

Enzymes|

* Prolyl hydroxylase/Lysyl hydroxylase
* Cartilage associated protein/Leprecan
* ADAMTS2
* Procollagen peptidase
* Lysyl oxidase

Laminin|

* alpha
* LAMA1
* LAMA2
* LAMA3
* LAMA4
* LAMA5
* beta
* LAMB1
* LAMB2
* LAMB3
* LAMB4
* gamma
* LAMC1
* LAMC2
* LAMC3

Other|

* ALCAM
* Elastin
* Tropoelastin
* Vitronectin
* FRAS1
* FREM2
* Decorin
* FAM20C
* ECM1
* Matrix gla protein
* Tectorin
* TECTA
* TECTB

Other|

* Keratin/Cytokeratin
* Gelatin
* Reticulin
* Cartilage oligomeric matrix protein

See also
diseases

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