Spn42Da Serpin 42Da [Drosophila melanogaster (fruit fly)] - Gene

Summary

Official Symbol: Spn42Daprovided by FlyBase
Official Full Name: Serpin 42Daprovided by FlyBase
Primary source: FLYBASE:FBgn0265137
Locus tag: Dmel_CG9453
See related: AllianceGenome:FB:FBgn0265137
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: CG9453; Dmel\CG9453; dSerp2; Serp2; sp4; Sp4; spn4; Spn4; Spn4A
Summary: Enables cysteine-type endopeptidase inhibitor activity and serine-type endopeptidase inhibitor activity. Involved in negative regulation of peptide hormone processing. Located in extracellular space. Is expressed in several structures, including adult head; adult heart; dorsal ectoderm; epithelium; and gut section. 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, Dec 2024]
Orthologs: all
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Genomic context

Location:: 42D6-42D6; 2-55 cM

Exon count:: 8

Annotation release	Status	Assembly	Chr	Location
Release 6.54	current	Release 6 plus ISO1 MT (GCF_000001215.4)	2R	NT_033778.4 (6875906..6878927, complement)
Release 5.57	previous assembly	Release 5 (GCF_000001215.2)	2R	NT_033778.3 (2763411..2766432, complement)

Chromosome 2R - NT_033778.4 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

High resolution structure confirm for the first time that the Serpin 42 Da isoforms are typical inhibitory serpin family members with the conserved serpin fold and inhibitory mechanism.
Title: High resolution structure of cleaved Serpin 42 Da from Drosophila melanogaster.
involved in the cellular regulation of prohormone convertases
Title: Drosophila serpin 4 functions as a neuroserpin-like inhibitor of subtilisin-like proprotein convertases.
Spn4 gene represents a versatile defence tool kit that may provide multiple antiproteolytic functions.
Title: The Spn4 gene from Drosophila melanogaster is a multipurpose defence tool directed against proteases from three different peptidase families.
Results report the identification of Spn4A, a previously uncharacterized secretory pathway serine protease inhibitor (serpin) from Drosophila melanogaster that contains a consensus furin cleavage site.
Title: The Spn4 gene of Drosophila encodes a potent furin-directed secretory pathway serpin.

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Homology

NCBI Orthologs

Orthologs from OrthoDB

Gene Ontology Provided by FlyBase

Function	Evidence Code	Pubs
enables cysteine-type endopeptidase inhibitor activity	IDA Inferred from Direct Assay more info	PubMed
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

Process	Evidence Code	Pubs
involved_in negative regulation of peptide hormone processing	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in negative regulation of protein processing	IMP Inferred from Mutant Phenotype 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	IDA Inferred from Direct Assay more info	PubMed
located_in extracellular space	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: serpin 42Da

Names: CG9453-PA; CG9453-PB; CG9453-PD; CG9453-PE; CG9453-PF; CG9453-PG; CG9453-PH; CG9453-PI; CG9453-PJ; CG9453-PK; CG9453-PL; Serp2; Spn42Da-PA; Spn42Da-PB; Spn42Da-PD; Spn42Da-PE; Spn42Da-PF; Spn42Da-PG; Spn42Da-PH; Spn42Da-PI; Spn42Da-PJ; Spn42Da-PK; Spn42Da-PL; neuroserpin; serine protease inhibitor 4; serpin 4; serpin 42 Da

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

NT_033778.4 Reference assembly

Range

6875906..6878927 complement

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_206034.2 → NP_995756.1 serpin 42Da, isoform I [Drosophila melanogaster]

See identical proteins and their annotated locations for NP_995756.1

Status: REVIEWED

UniProtKB/TrEMBL

Q8MPN7, Q8T0M5, Q9V991

Conserved Domains (1) summary

cd00172
Location:45 → 404

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 ...
NM_206033.2 → NP_995755.1 serpin 42Da, isoform J [Drosophila melanogaster]

See identical proteins and their annotated locations for NP_995755.1

Status: REVIEWED

UniProtKB/TrEMBL

Q8MPN5, Q9U1I5

Conserved Domains (1) summary

cd00172
Location:13 → 372

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 ...
NM_206039.3 → NP_995761.1 serpin 42Da, isoform D [Drosophila melanogaster]

See identical proteins and their annotated locations for NP_995761.1

Status: REVIEWED

UniProtKB/TrEMBL

Q8MPN8, Q8T0M5, Q9V991

Conserved Domains (1) summary

cd00172
Location:45 → 408

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 ...
NM_206037.3 → NP_995759.1 serpin 42Da, isoform F [Drosophila melanogaster]

See identical proteins and their annotated locations for NP_995759.1

Status: REVIEWED

UniProtKB/TrEMBL

Q8MM49, Q8T0M5, Q9V991

Conserved Domains (1) summary

cd00172
Location:45 → 408

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 ...
NM_206038.3 → NP_995760.1 serpin 42Da, isoform E [Drosophila melanogaster]

See identical proteins and their annotated locations for NP_995760.1

Status: REVIEWED

UniProtKB/TrEMBL

Q8MM49, Q8T0M5, Q9V991

Conserved Domains (1) summary

cd00172
Location:45 → 408

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 ...
NM_165495.4 → NP_724511.2 serpin 42Da, isoform L [Drosophila melanogaster]

See identical proteins and their annotated locations for NP_724511.2

Status: REVIEWED

UniProtKB/TrEMBL

Q8MM39, Q8T0M5, Q9V991

Conserved Domains (1) summary

cd00172
Location:13 → 376

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 ...
NM_206036.2 → NP_995758.1 serpin 42Da, isoform G [Drosophila melanogaster]

See identical proteins and their annotated locations for NP_995758.1

Status: REVIEWED

UniProtKB/TrEMBL

Q8MPN6, Q9U1I5

Conserved Domains (1) summary

cd00172
Location:13 → 376

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 ...
NM_206032.2 → NP_995754.1 serpin 42Da, isoform K [Drosophila melanogaster]

See identical proteins and their annotated locations for NP_995754.1

Status: REVIEWED

UniProtKB/TrEMBL

Q8MM39, Q8T0M5, Q9V991

Conserved Domains (1) summary

cd00172
Location:13 → 376

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 ...
NM_206035.2 → NP_995757.1 serpin 42Da, isoform H [Drosophila melanogaster]

See identical proteins and their annotated locations for NP_995757.1

Status: REVIEWED

UniProtKB/TrEMBL

Q8MM39, Q8T0M5, Q9V991

Conserved Domains (1) summary

cd00172
Location:13 → 376

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 ...
NM_080216.3 → NP_524955.2 serpin 42Da, isoform B [Drosophila melanogaster]

See identical proteins and their annotated locations for NP_524955.2

Status: REVIEWED

UniProtKB/TrEMBL

Q7K8Y5, Q9U1I5

Related

FBpp0085523

Conserved Domains (1) summary

cd00172
Location:45 → 408

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 ...
NM_165496.3 → NP_724512.1 serpin 42Da, isoform A [Drosophila melanogaster]

See identical proteins and their annotated locations for NP_724512.1

Status: REVIEWED

UniProtKB/TrEMBL

Q7K8Y3, Q9U1I5

Related

FBpp0085524

Conserved Domains (1) summary

cd00172
Location:13 → 376

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 ...

Nucleotide		Protein
Heading	Accession and Version	Protein

Protein Accession	Links
Protein Accession	GenPept Link	UniProtKB Link
Q7K8Y3		Q7K8Y3
Q7K8Y5		Q7K8Y5
Q8MM39		Q8MM39
Q8MM49		Q8MM49
Q8MPN5		Q8MPN5
Q8MPN6		Q8MPN6
Q8MPN7		Q8MPN7
Q8MPN8		Q8MPN8
Q8T0M5		Q8T0M5
Q9U1I5		Q9U1I5