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Spn42De Serpin 42De [ Drosophila melanogaster (fruit fly) ]

Gene ID: 35602, updated on 4-Jan-2025

Summary

Official Symbol
Spn42Deprovided by FlyBase
Official Full Name
Serpin 42Deprovided by FlyBase
Primary source
FLYBASE:FBgn0033115
Locus tag
Dmel_CG9460
See related
AllianceGenome:FB:FBgn0033115
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Drosophila melanogaster
Lineage
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; Drosophilidae; Drosophila; Sophophora
Also known as
CG9460; Dmel\CG9460; dSERPINA1; spn42De
Summary
Predicted to enable serine-type endopeptidase inhibitor activity. Predicted to be involved in negative regulation of proteolysis. Predicted to be active in extracellular space. Is expressed in several structures, including embryonic dorsal epidermis; embryonic epipharynx; embryonic foregut; embryonic head epidermis; and embryonic hypopharynx. Human ortholog(s) of this gene implicated in Alzheimer's disease and familial encephalopathy with neuroserpin inclusion bodies. Orthologous to several human genes including SERPINI1 (serpin family I member 1) and SERPINI2 (serpin family I member 2). [provided by Alliance of Genome Resources, Jan 2025]
Orthologs
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Genomic context

See Spn42De in Genome Data Viewer
Location:
42D6-42D6; 2-55 cM
Exon count:
5
Annotation release Status Assembly Chr Location
Release 6.54 current Release 6 plus ISO1 MT (GCF_000001215.4) 2R NT_033778.4 (6885552..6888262)
Release 5.57 previous assembly Release 5 (GCF_000001215.2) 2R NT_033778.3 (2773057..2775767)

Chromosome 2R - NT_033778.4Genomic Context describing neighboring genes Neighboring gene antisense RNA:CR44169 Neighboring gene Serpin 42Db Neighboring gene Serpin 42Dc Neighboring gene Serpin 42Dd Neighboring gene uncharacterized protein Neighboring gene uncharacterized protein Neighboring gene missing-in-metastasis

Genomic regions, transcripts, and products

General gene information

Gene Ontology Provided by FlyBase

Function Evidence Code Pubs
enables serine-type endopeptidase inhibitor activity IEA
Inferred from Electronic Annotation
more info
 
Process Evidence Code Pubs
involved_in negative regulation of proteolysis ISM
Inferred from Sequence Model
more info
PubMed 
Component Evidence Code Pubs
is_active_in extracellular space IBA
Inferred from Biological aspect of Ancestor
more info
 
located_in extracellular space IEA
Inferred from Electronic Annotation
more info
 
located_in extracellular space ISM
Inferred from Sequence Model
more info
PubMed 

General protein information

Preferred Names
serpin 42De
Names
CG9460-PA
CG9460-PB
Spn42De-PA
Spn42De-PB

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NT_033778.4 Reference assembly

    Range
    6885552..6888262
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001259226.2NP_001246155.1  serpin 42De, isoform B [Drosophila melanogaster]

    See identical proteins and their annotated locations for NP_001246155.1

    Status: REVIEWED

    UniProtKB/TrEMBL
    A0A0B4K6Q4
    Conserved Domains (1) summary
    cd00172
    Location:13383
    SERPIN; SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate ...
  2. NM_136402.4NP_610246.3  serpin 42De, isoform A [Drosophila melanogaster]

    See identical proteins and their annotated locations for NP_610246.3

    Status: REVIEWED

    UniProtKB/TrEMBL
    Q8SZF4
    Related
    FBpp0085497
    Conserved Domains (1) summary
    cd00172
    Location:31401
    SERPIN; SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate ...