ECM1

Protein identityUniProt · HPA

UniProt accession

Q16610

Gene

ECM1

Ensembl

ENSG00000143369

Chromosome

1

Canonical length

540 aa

Protein class

Disease related genes, Human disease related genes, Plasma proteins, Predicted secreted proteins

Subcellular location

Nucleoplasm,Cytosol

Secretome location

Secreted to extracellular matrix

OverviewNCBI Gene

This gene encodes a soluble protein that is involved in endochondral bone formation, angiogenesis, and tumor biology. It also interacts with a variety of extracellular and structural proteins, contributing to the maintenance of skin integrity and homeostasis. Mutations in this gene are associated with lipoid proteinosis disorder (also known as hyalinosis cutis et mucosae or Urbach-Wiethe disease) that is characterized by generalized thickening of skin, mucosae and certain viscera. Alternatively spliced transcript variants encoding distinct isoforms have been described for this gene. [provided by RefSeq, Feb 2011]

Canonical amino-acid sequenceUniProt

540 residues, UniProt reviewed canonical sequence.

>Q16610|ECM1
     1  MGTTARAALV LTYLAVASAA SEGGFTATGQ RQLRPEHFQE VGYAAPPSPP LSRSLPMDHP
    61  DSSQHGPPFE GQSQVQPPPS QEATPLQQEK LLPAQLPAEK EVGPPLPQEA VPLQKELPSL
   121  QHPNEQKEGT PAPFGDQSHP EPESWNAAQH CQQDRSQGGW GHRLDGFPPG RPSPDNLNQI
   181  CLPNRQHVVY GPWNLPQSSY SHLTRQGETL NFLEIGYSRC CHCRSHTNRL ECAKLVWEEA
   241  MSRFCEAEFS VKTRPHWCCT RQGEARFSCF QEEAPQPHYQ LRACPSHQPD ISSGLELPFP
   301  PGVPTLDNIK NICHLRRFRS VPRNLPATDP LQRELLALIQ LEREFQRCCR QGNNHTCTWK
   361  AWEDTLDKYC DREYAVKTHH HLCCRHPPSP TRDECFARRA PYPNYDRDIL TIDIGRVTPN
   421  LMGHLCGNQR VLTKHKHIPG LIHNMTARCC DLPFPEQACC AEEEKLTFIN DLCGPRRNIW
   481  RDPALCCYLS PGDEQVNCFN INYLRNVALV SGDTENAKGQ GEQGSTGGTN ISSTSEPKEE

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against ECM1 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.

Antibody reachability

Secreted

Secreted

Yes

Transmembrane segments

0

Mean surface accessibility (rSASA)

0.43

Highest tissue expression

1,332 nTPM

Expression across tissuesHPA

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about ECM1.

Disease | AllUniProt

Conditions ECM1 is implicated in, by any mechanism.

• Lipoid proteinosis (LiP) MIM:247100

Disease | GeneticClinVar

35 pathogenic / likely-pathogenic of 194 ClinVar records.

Conditions with pathogenic or likely-pathogenic variants.

• Lipid proteinosis
• ECM1-related disorder
• Gastric cancer

ReferencesPubMed · IEDB

Publications for ECM1 from three distinct lines of evidence, kept separate because they answer different questions: whether antibodies are directed at the protein, whether a B-cell epitope has been mapped on it, and whether a T-cell epitope has. Each is labelled with its source.

Sources: PubMed — antigen-level antibody evidence from a custom retrieval. Records matching a controlled set of autoantibody terms (the MeSH descriptors Autoantibodies and Autoantigens, with title and abstract term variants) were obtained through NCBI E-utilities, and their titles and abstracts parsed for constructions that direct an antibody at a named protein rather than for co-occurrence. Captured names were resolved against UniProt nomenclature and each antigen adjudicated individually against the source text. Bibliographic records from PubMed and MeSH, U.S. National Library of Medicine; citation metrics from NIH iCite (Hutchins et al., PLoS Biology 2016). Titles link to PubMed; abstracts are not reproduced here. The NLM does not endorse this analysis.

Genetic constraint and essentialitygnomAD · DepMap

Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.

gnomAD LOEUF (loss-of-function intolerance)

1.13

gnomAD pLI

0

gnomAD missense Z

-0.22

DepMap mean gene effect

-0.21

DepMap dependency class

selective

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 4% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

• angiogenesis
• biomineral tissue development
• chondrocyte development
• endochondral bone growth
• inflammatory response
• negative regulation of bone mineralization
• negative regulation of cytokine-mediated signaling pathway
• negative regulation of peptidase activity
• ossification
• positive regulation of angiogenesis
• positive regulation of canonical NF-kappaB signal transduction
• positive regulation of endothelial cell proliferation
• regulation of bone mineralization
• regulation of T cell migration
• regulation of transcription by RNA polymerase II
• signal transduction
• regulation of type 2 immune response

Molecular functions

• interleukin-2 receptor binding
• protease binding

Cellular components

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

Protein domainsUniProt · Pfam · InterPro

• Serum albumin-like
• Extracellular matrix protein 1
• Extracellular matrix protein 1 (ECM1)

KeywordsUniProt

• Angiogenesis
• Biomineralization
• Extracellular matrix
• Glycoprotein
• Mineral balance
• Osteogenesis
• Repeat
• Secreted
• Signal

InteractionsUniProt · HPA

Protein binding partners of ECM1 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.

• LAMB3
• MMP9
• EFEMP1