MMP1

Protein identityUniProt · HPA

UniProt accession

P03956

Gene

MMP1

Ensembl

ENSG00000196611

Chromosome

11

Canonical length

469 aa

Protein class

Cancer-related genes, Candidate cardiovascular disease genes, Enzymes, Human disease related genes, Plasma proteins, Predicted secreted proteins

Subcellular location

Vesicles

Secretome location

Secreted to extracellular matrix

OverviewNCBI Gene

This gene encodes a member of the peptidase M10 family of matrix metalloproteinases (MMPs). Proteins in this family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. The encoded preproprotein is proteolytically processed to generate the mature protease. This secreted protease breaks down the interstitial collagens, including types I, II, and III. The gene is part of a cluster of MMP genes on chromosome 11. Mutations in this gene are associated with chronic obstructive pulmonary disease (COPD). Alternative splicing results in multiple transcript variants, at least one of which encodes an isoform that is proteolytically processed. [provided by RefSeq, Jan 2016]

Canonical amino-acid sequenceUniProt

469 residues, UniProt reviewed canonical sequence.

>P03956|MMP1
     1  MHSFPPLLLL LFWGVVSHSF PATLETQEQD VDLVQKYLEK YYNLKNDGRQ VEKRRNSGPV
    61  VEKLKQMQEF FGLKVTGKPD AETLKVMKQP RCGVPDVAQF VLTEGNPRWE QTHLTYRIEN
   121  YTPDLPRADV DHAIEKAFQL WSNVTPLTFT KVSEGQADIM ISFVRGDHRD NSPFDGPGGN
   181  LAHAFQPGPG IGGDAHFDED ERWTNNFREY NLHRVAAHEL GHSLGLSHST DIGALMYPSY
   241  TFSGDVQLAQ DDIDGIQAIY GRSQNPVQPI GPQTPKACDS KLTFDAITTI RGEVMFFKDR
   301  FYMRTNPFYP EVELNFISVF WPQLPNGLEA AYEFADRDEV RFFKGNKYWA VQGQNVLHGY
   361  PKDIYSSFGF PRTVKHIDAA LSEENTGKTY FFVANKYWRY DEYKRSMDPG YPKMIAHDFP
   421  GIGHKVDAVF MKDGFFYFFH GTRQYKFDPK TKRILTLQKA NSWFNCRKN

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against MMP1 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)

0.27

Highest tissue expression

71 nTPM

Expression across tissuesHPA

ReferencesPubMed · IEDB

Publications for MMP1 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)

1.53

gnomAD pLI

0

gnomAD missense Z

-1.12

DepMap mean gene effect

0.18

DepMap dependency class

none

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 3% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

• cellular response to UV-A
• collagen catabolic process
• extracellular matrix disassembly
• extracellular matrix organization
• positive regulation of protein-containing complex assembly
• proteolysis

Molecular functions

• endopeptidase activity
• metalloendopeptidase activity
• peptidase activity
• serine-type endopeptidase activity
• zinc ion binding

Cellular components

• extracellular matrix
• extracellular region

Protein domainsUniProt · Pfam · InterPro

• Hemopexin-like domain
• Peptidase M10, metallopeptidase
• Peptidoglycan binding-like
• Peptidase, metallopeptidase
• Hemopexin, conserved site
• Hemopexin-like repeats
• Peptidase M10A, cysteine switch, zinc binding site
• Peptidase M10A
• Metallopeptidase, catalytic domain superfamily
• Peptidase M10A, catalytic domain
• PGBD-like superfamily
• Hemopexin-like domain superfamily
• Hemopexin
• Matrixin
• Putative peptidoglycan binding domain

KeywordsUniProt

• Autocatalytic cleavage
• Calcium
• Collagen degradation
• Disulfide bond
• Extracellular matrix
• Glycoprotein
• Host-virus interaction
• Hydrolase
• Metal-binding
• Metalloprotease
• Phosphoprotein
• Protease
• Repeat
• Secreted
• Signal
• Zinc
• Zymogen

InteractionsUniProt · HPA

Protein binding partners of MMP1 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.

• TIMP1