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Spn27A Serpin 27A [ Drosophila melanogaster (fruit fly) ]

Gene ID: 45815, updated on 11-Apr-2024

Summary

Official Symbol
Spn27Aprovided by FlyBase
Official Full Name
Serpin 27Aprovided by FlyBase
Primary source
FLYBASE:FBgn0028990
Locus tag
Dmel_CG11331
See related
AllianceGenome:FB:FBgn0028990
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
CG11331; Dm-Spn27A; Dmel\CG11331; EST1; sp27A; Sp27A; Spn27; spn27A; Spn27a
Summary
Enables serine-type endopeptidase inhibitor activity. Involved in several processes, including behavioral response to ethanol; defense response to other organism; and negative regulation melanotic encapsulation of foreign target. Located in perivitelline space. Is expressed in several structures, including embryonic/larval dorsal vessel; extraembryonic structure; presumptive embryonic/larval digestive system; yolk; and yolk nucleus. Human ortholog(s) of this gene implicated in familial encephalopathy with neuroserpin inclusion bodies. Orthologous to human SERPINI1 (serpin family I member 1). [provided by Alliance of Genome Resources, Apr 2022]
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Genomic context

Location:
26F6-26F6; 2-21 cM
Exon count:
1
Annotation release Status Assembly Chr Location
Release 6.54 current Release 6 plus ISO1 MT (GCF_000001215.4) 2L NT_033779.5 (6671065..6673347, complement)
Release 5.57 previous assembly Release 5 (GCF_000001215.2) 2L NT_033779.4 (6671065..6673347, complement)

Chromosome 2L - NT_033779.5Genomic Context describing neighboring genes Neighboring gene uncharacterized protein Neighboring gene uncharacterized protein Neighboring gene cup Neighboring gene Galactose-1-phosphate uridylyltransferase Neighboring gene cortex Neighboring gene Non-SMC element 1

Genomic regions, transcripts, and products

Pathways from PubChem

Interactions

Products Interactant Other Gene Complex Source Pubs Description

General gene information

Gene Ontology Provided by FlyBase

Function Evidence Code Pubs
enables serine-type endopeptidase inhibitor activity IDA
Inferred from Direct Assay
more info
PubMed 
enables serine-type endopeptidase inhibitor activity IEA
Inferred from Electronic Annotation
more info
 
Component Evidence Code Pubs
located_in extracellular region IDA
Inferred from Direct Assay
more info
PubMed 
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 perivitelline space IDA
Inferred from Direct Assay
more info
PubMed 

General protein information

Preferred Names
serpin 27A
Names
CG11331-PA
CG11331-PB
Dm-serpin-27A
Serpin-27A
Serpin27A
Spn27A-PA
Spn27A-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_033779.5 Reference assembly

    Range
    6671065..6673347 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001273214.1NP_001260143.1  serpin 27A, isoform B [Drosophila melanogaster]

    See identical proteins and their annotated locations for NP_001260143.1

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    Q9V3N1
    Conserved Domains (1) summary
    cd00172
    Location:72440
    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_143767.3NP_652024.1  serpin 27A, isoform A [Drosophila melanogaster]

    See identical proteins and their annotated locations for NP_652024.1

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    Q9V3N1
    Related
    FBpp0078950
    Conserved Domains (1) summary
    cd00172
    Location:72440
    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 ...