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Spn28F Serpin 28F [ Drosophila melanogaster (fruit fly) ]

Gene ID: 49807, updated on 4-Jan-2025

Summary

Official Symbol
Spn28Fprovided by FlyBase
Official Full Name
Serpin 28Fprovided by FlyBase
Primary source
FLYBASE:FBgn0028987
Locus tag
Dmel_CG8137
See related
AllianceGenome:FB:FBgn0028987
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
CG8137; Dmel\CG8137; sp2; Sp2; spn2; Spn2
Summary
Predicted to enable hormone binding activity and serine-type endopeptidase inhibitor activity. Involved in sexual reproduction. Located in extracellular space. Is expressed in several structures, including adult head; adult hemolymph; female reproductive system; ovary; and sperm storage organ. Human ortholog(s) of this gene implicated in antithrombin III deficiency; disseminated intravascular coagulation; intermediate coronary syndrome; thrombosis; and toxic shock syndrome. Orthologous to several human genes including SERPINB1 (serpin family B member 1); SERPINB12 (serpin family B member 12); and SERPINB13 (serpin family B member 13). [provided by Alliance of Genome Resources, Jan 2025]
Orthologs
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Genomic context

See Spn28F in Genome Data Viewer
Location:
28F5-28F5; 2-30 cM
Exon count:
4
Annotation release Status Assembly Chr Location
Release 6.54 current Release 6 plus ISO1 MT (GCF_000001215.4) 2L NT_033779.5 (8240414..8241800, complement)
Release 5.57 previous assembly Release 5 (GCF_000001215.2) 2L NT_033779.4 (8240414..8241800, complement)

Chromosome 2L - NT_033779.5Genomic Context describing neighboring genes Neighboring gene Sorting nexin 6 Neighboring gene PDGF- and VEGF-receptor related Neighboring gene long non-coding RNA:CR43262 Neighboring gene uncharacterized protein Neighboring gene uncharacterized protein

Genomic regions, transcripts, and products

General gene information

Gene Ontology Provided by FlyBase

Function Evidence Code Pubs
enables hormone binding ISS
Inferred from Sequence or Structural Similarity
more info
PubMed 
enables serine-type endopeptidase inhibitor activity IEA
Inferred from Electronic Annotation
more info
 
enables serine-type endopeptidase inhibitor activity ISS
Inferred from Sequence or Structural Similarity
more info
PubMed 
Process Evidence Code Pubs
involved_in negative regulation of proteolysis ISS
Inferred from Sequence or Structural Similarity
more info
PubMed 
involved_in sexual reproduction HEP PubMed 
involved_in sexual reproduction IEP
Inferred from Expression Pattern
more info
PubMed 
Component Evidence Code Pubs
located_in extracellular region ISM
Inferred from Sequence Model
more info
PubMed 
located_in extracellular space HDA 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 extracellular space ISM
Inferred from Sequence Model
more info
PubMed 

General protein information

Preferred Names
serpin 28F
Names
CG8137-PA
Spn28F-PA
serine protease inhibitor 2
serpin 2

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
    8240414..8241800 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_080218.5NP_524957.2  serpin 28F [Drosophila melanogaster]

    See identical proteins and their annotated locations for NP_524957.2

    Status: REVIEWED

    UniProtKB/TrEMBL
    C5WLL8, Q9VLQ7
    Related
    FBpp0079243
    Conserved Domains (1) summary
    cd00172
    Location:14370
    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 ...