SERPINE2

Protein identityUniProt · HPA

UniProt accession

P07093

Gene

SERPINE2

Ensembl

ENSG00000135919

Chromosome

2

Canonical length

398 aa

Protein class

Plasma proteins, Predicted secreted proteins

Subcellular location

Golgi apparatus

Secretome location

Secreted in female reproductive system

OverviewNCBI Gene

This gene encodes a member of the serpin family of proteins, a group of proteins that inhibit serine proteases. Thrombin, urokinase, plasmin and trypsin are among the proteases that this family member can inhibit. This gene is a susceptibility gene for chronic obstructive pulmonary disease and for emphysema. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Aug 2012]

Canonical amino-acid sequenceUniProt

398 residues, UniProt reviewed canonical sequence.

>P07093|SERPINE2
     1  MNWHLPLFLL ASVTLPSICS HFNPLSLEEL GSNTGIQVFN QIVKSRPHDN IVISPHGIAS
    61  VLGMLQLGAD GRTKKQLAMV MRYGVNGVGK ILKKINKAIV SKKNKDIVTV ANAVFVKNAS
   121  EIEVPFVTRN KDVFQCEVRN VNFEDPASAC DSINAWVKNE TRDMIDNLLS PDLIDGVLTR
   181  LVLVNAVYFK GLWKSRFQPE NTKKRTFVAA DGKSYQVPML AQLSVFRCGS TSAPNDLWYN
   241  FIELPYHGES ISMLIALPTE SSTPLSAIIP HISTKTIDSW MSIMVPKRVQ VILPKFTAVA
   301  QTDLKEPLKV LGITDMFDSS KANFAKITTG SENLHVSHIL QKAKIEVSED GTKASAATTA
   361  ILIARSSPPW FIVDRPFLFF IRHNPTGAVL FMGQINKP

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against SERPINE2 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)

0.26

Highest tissue expression

1,025 nTPM

Expression across tissuesHPA

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about SERPINE2.

Disease | ImmuneIEDB

Conditions an epitope on SERPINE2 was assayed in.

• skin melanoma T cell

ReferencesPubMed · IEDB

Publications for SERPINE2 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. IEDB — curated epitope assays from the Immune Epitope Database (Vita et al., Nucleic Acids Research 2019). 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)

0.45

gnomAD pLI

0.73

gnomAD missense Z

1.59

DepMap mean gene effect

0.15

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

• cell differentiation
• detection of mechanical stimulus involved in sensory perception
• innervation
• long-term synaptic potentiation
• negative regulation of blood coagulation
• negative regulation of cell growth
• negative regulation of cell population proliferation
• negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
• negative regulation of plasminogen activation
• negative regulation of platelet aggregation
• negative regulation of protein catabolic process
• negative regulation of protein processing
• negative regulation of proteolysis
• negative regulation of smoothened signaling pathway
• negative regulation of sodium ion transport
• platelet activation
• positive regulation of astrocyte differentiation
• protein catabolic process
• regulation of cell migration
• regulation of synaptic transmission, glutamatergic
• regulation of timing of cell differentiation
• secretion by cell
• secretory granule organization
• cerebellar granular layer morphogenesis
• mating plug formation
• seminal vesicle epithelium development

Molecular functions

• glycosaminoglycan binding
• heparin binding
• serine-type endopeptidase inhibitor activity
• signaling receptor binding

Cellular components

• cytosol
• extracellular matrix
• extracellular region
• extracellular space
• extracellular vesicle
• neuromuscular junction
• platelet alpha granule

Protein domainsUniProt · Pfam · InterPro

• Serpin family
• Serpin, conserved site
• Serpin domain
• Serpin superfamily
• Serpin superfamily, domain 1
• Serpin superfamily, domain 2
• Serpin (serine protease inhibitor)

KeywordsUniProt

• Developmental protein
• Differentiation
• Glycoprotein
• Heparin-binding
• Neurogenesis
• Protease inhibitor
• Secreted
• Serine protease inhibitor
• Signal