Seroatlas · Human Serome Atlas

MMP11

Stromelysin-3

Also known as: MMP11_HUMAN, STMY3

Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene

Protein identityUniProt · HPA

UniProt accession: P24347
Gene: MMP11
Ensembl: ENSG00000099953
Chromosome: 22
Canonical length: 488 aa
Protein class: Cancer-related genes, Enzymes, Predicted secreted proteins
Subcellular location: Golgi apparatus,Cytosol
Secretome location: Secreted to extracellular matrix

OverviewNCBI Gene

Proteins of the matrix metalloproteinase (MMP) 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. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. However, the enzyme encoded by this gene is activated intracellularly by furin within the constitutive secretory pathway. Also in contrast to other MMP's, this enzyme cleaves alpha 1-proteinase inhibitor but weakly degrades structural proteins of the extracellular matrix. [provided by RefSeq, Jul 2008]

Canonical amino-acid sequenceUniProt

488 residues, UniProt reviewed canonical sequence.

>P24347|MMP11
     1  MAPAAWLRSA AARALLPPML LLLLQPPPLL ARALPPDAHH LHAERRGPQP WHAALPSSPA
    61  PAPATQEAPR PASSLRPPRC GVPDPSDGLS ARNRQKRFVL SGGRWEKTDL TYRILRFPWQ
   121  LVQEQVRQTM AEALKVWSDV TPLTFTEVHE GRADIMIDFA RYWHGDDLPF DGPGGILAHA
   181  FFPKTHREGD VHFDYDETWT IGDDQGTDLL QVAAHEFGHV LGLQHTTAAK ALMSAFYTFR
   241  YPLSLSPDDC RGVQHLYGQP WPTVTSRTPA LGPQAGIDTN EIAPLEPDAP PDACEASFDA
   301  VSTIRGELFF FKAGFVWRLR GGQLQPGYPA LASRHWQGLP SPVDAAFEDA QGHIWFFQGA
   361  QYWVYDGEKP VLGPAPLTEL GLVRFPVHAA LVWGPEKNKI YFFRGRDYWR FHPSTRRVDS
   421  PVPRRATDWR GVPSEIDAAF QDADGYAYFL RGRLYWKFDP VKVKALEGFP RLVGPDFFGC
   481  AEPANTFL

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against MMP11 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): 0.36
Highest tissue expression: 134 nTPM

Expression across tissuesHPA

Tissue

endometrium: 134 nTPM
cervix: 87 nTPM
placenta: 37 nTPM
ovary: 15 nTPM
smooth muscle: 8.8 nTPM
heart muscle: 7 nTPM

Single-cell type

proximal tubule cells: 2.7 nCPM
ependymal cells: 1.3 nCPM
microglia: 1.3 nCPM
astrocytes: 1.2 nCPM
bergmann glia: 1.2 nCPM
papillary tip epithelial cells: 1.1 nCPM

Immune cell

plasmacytoid DC: 4.5 nTPM
memory B-cell: 0.8 nTPM
naive B-cell: 0.7 nTPM
naive CD4 T-cell: 0.1 nTPM
total PBMC: 0.1 nTPM
basophil: 0 nTPM

Brain region

medulla oblongata: 0.2 nTPM
thalamus: 0.2 nTPM
amygdala: 0.1 nTPM
cerebral cortex: 0.1 nTPM
hypothalamus: 0.1 nTPM
midbrain: 0.1 nTPM

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): 0.84
gnomAD pLI: 0
gnomAD missense Z: 0.65
DepMap mean gene effect: 0.01
DepMap dependency class: none

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

Molecular functions

Cellular components

Protein domainsUniProt · Pfam · InterPro

KeywordsUniProt

Antibody and autoantibody relevanceSeroatlas analysis

Seroatlas reads MMP11 as an antibody target. Whether an autoantibody or antibody against MMP11 could matter depends on whether native MMP11 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.

MMP11 is annotated as secreted, so native MMP11 circulates and is directly accessible to antibodies. Secreted and cell-surface proteins are the autoantibody targets most likely to act like drugs, blocking or depleting the native protein.

Annotation status

The present source text does not explicitly label MMP11 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.

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