GeneBe

SERPINF2

serpin family F member 2, the group of Serpin peptidase inhibitors

Basic information

Region (hg38): 17:1742836-1755265

Previous symbols: [ "PLI" ]

Links

ENSG00000167711 ∙ NCBI:5345 ∙ OMIM:613168 ∙ HGNC:9075 ∙ Uniprot:P08697 ∙ AlphaFold ∙ GenCC ∙ jax ∙ Sfari ∙ GnomAD ∙ Pubmed ∙ ClinVar

Phenotypes

GenCC

Source: genCC

  • alpha-2-plasmin inhibitor deficiency (Supportive), mode of inheritance: AR
  • alpha-2-plasmin inhibitor deficiency (Strong), mode of inheritance: AR
  • alpha-2-plasmin inhibitor deficiency (Limited), mode of inheritance: AD
  • alpha-2-plasmin inhibitor deficiency (Definitive), mode of inheritance: AR
  • alpha-2-plasmin inhibitor deficiency (Definitive), mode of inheritance: AR

Clinical Genomic Database

Source: CGD

ConditionInheritanceIntervention CategoriesIntervention/Rationale Manifestation CategoriesReferences
Alpha-2-plasmin inhibitor deficiencyAD/ARHematologicAnti-fibrinolytic agents or FFP can be used to treat bleeding episodes, and to and prevent patients hemorrhagic complications in those who are undergoing surgical interventions; Intramedullary hematoma is also a common feature, and awareness of this potential manifestation can be beneficial in order to institute efficient treatment; Heterozygotes may also have (milder) manifestationsHematologic82839; 156196; 89324; 7095605; 2496145; 2572590; 1806461; 9880645; 10583218; 11472338; 19141165; 19593116; 21873355

ClinVar

This is a list of variants' phenotypes submitted to ClinVar and linked to the SERPINF2 gene.

  • not_specified (58 variants)
  • not_provided (26 variants)
  • SERPINF2-related_disorder (9 variants)
  • Alpha-2-plasmin_inhibitor_deficiency (4 variants)
  • Abnormal_bleeding (2 variants)

Variants pathogenicity by type

Statistics on ClinVar variants can assist in determining whether a specific variant type in the SERPINF2 gene is commonly pathogenic or not. These statistics are base on transcript: NM_000000934.4. Only rare variants are included in the table.

In the table, we include only reliable ClinVar variants with their consequences to MANE Select, Mane Plus Clinical transcripts, or transcripts with TSL equals 1. Click the count to view the source variants.

Warning: slight differences between displayed counts and the number of variants in ClinVar may occur, primarily due to (1) the application of a different transcript and/or consequence by our variant effect predictor or (2) differences in clinical significance: we classify Benign/Likely benign variants as Likely benign and Pathogenic/Likely pathogenic variants as Likely pathogenic.

EffectPLPVUSLBBSum
synonymous
11
clinvar
1
clinvar
 12
missense
1
clinvar
52
clinvar
10
clinvar
1
clinvar
 64
nonsense
0
start loss
0
frameshift
2
clinvar
 2
splice donor/acceptor (+/-2bp)
1
clinvar
 1
Total 3 1 52 21 2

Highest pathogenic variant AF is 0.00000309944

Loading clinvar variants...

GnomAD

Source: gnomAD

GeneTypeBio TypeTranscript Coding Exons Length
SERPINF2protein_codingprotein_codingENST00000324015 912433
pLI Probability
LOF Intolerant 		pRec Probability
LOF Recessive 		Individuals with
no LOFs 		Individuals with
Homozygous LOFs 		Individuals with
Heterozygous LOFs 		Defined p
0.01360.9851257310161257470.0000636
Z-Score Observed Expected Observed/Expected Mutation Rate Total Possible in Transcript
Missense1.232292880.7960.00001813197
Missense in Polyphen4786.8490.541171006
Synonymous-0.1301351331.010.000009431008
Loss of Function2.83721.00.3340.00000100210

LoF frequencies by population

EthnicitySum of pLOFs p
African & African-American0.0001900.000182
Ashkenazi Jewish0.000.00
East Asian0.0002180.000163
Finnish0.000.00
European (Non-Finnish)0.00007120.0000439
Middle Eastern0.0002180.000163
South Asian0.00006540.0000653
Other0.0006540.000326

dbNSFP

Source: dbNSFP

Function
FUNCTION: Serine protease inhibitor. The major targets of this inhibitor are plasmin and trypsin, but it also inactivates matriptase-3/TMPRSS7 and chymotrypsin. {ECO:0000269|PubMed:15853774}.;
Disease
DISEASE: Alpha-2-plasmin inhibitor deficiency (APLID) [MIM:262850]: An autosomal recessive disorder resulting in severe hemorrhagic diathesis. {ECO:0000269|PubMed:10583218, ECO:0000269|PubMed:2572590}. Note=The disease is caused by mutations affecting the gene represented in this entry.;
Pathway
Complement and coagulation cascades - Homo sapiens (human);Blood Clotting Cascade;Dengue-2 Interactions with Complement and Coagulation Cascades;Dengue-2 Interactions with Blood Clotting Cascade;Complement and Coagulation Cascades;Dissolution of Fibrin Clot;Platelet degranulation ;Response to elevated platelet cytosolic Ca2+;Platelet activation, signaling and aggregation;Hemostasis (Consensus)

Recessive Scores

pRec
0.535

Intolerance Scores

loftool
0.0313
rvis_EVS
-0.78
rvis_percentile_EVS
13.05

Haploinsufficiency Scores

pHI
0.222
hipred
Y
hipred_score
0.505
ghis
0.472

Essentials

essential_gene_CRISPR
N
essential_gene_CRISPR2
N
essential_gene_gene_trap
N
gene_indispensability_pred
E
gene_indispensability_score
0.920

Gene Damage Prediction

AllRecessiveDominant
MendelianMediumMediumMedium
Primary ImmunodeficiencyHighMediumHigh
CancerHighMediumHigh

Mouse Genome Informatics

Gene name
Serpinf2
Phenotype
homeostasis/metabolism phenotype;

Gene ontology

Biological process
regulation of blood vessel diameter by renin-angiotensin;platelet degranulation;acute-phase response;response to organic substance;negative regulation of plasminogen activation;negative regulation of endopeptidase activity;collagen fibril organization;positive regulation of collagen biosynthetic process;fibrinolysis;positive regulation of cell differentiation;positive regulation of transcription by RNA polymerase II;positive regulation of JNK cascade;blood vessel morphogenesis;positive regulation of smooth muscle cell proliferation;positive regulation of stress fiber assembly;negative regulation of fibrinolysis;positive regulation of ERK1 and ERK2 cascade;positive regulation of transforming growth factor beta production;positive regulation of cell-cell adhesion mediated by cadherin
Cellular component
extracellular region;fibrinogen complex;extracellular space;cell surface;platelet alpha granule lumen;collagen-containing extracellular matrix;extracellular exosome;blood microparticle
Molecular function
protease binding;endopeptidase inhibitor activity;serine-type endopeptidase inhibitor activity;protein binding;protein homodimerization activity