serpinb1 serpin peptidase inhibitor, clade B (ovalbumin), member 1 [Danio rerio (zebrafish)] - Gene

Summary

Official Symbol: serpinb1provided by ZNC
Official Full Name: serpin peptidase inhibitor, clade B (ovalbumin), member 1provided by ZNC
Primary source: ZFIN:ZDB-GENE-040718-400
See related: Ensembl:ENSDARG00000055416 AllianceGenome:ZFIN:ZDB-GENE-040718-400
Gene type: protein coding
RefSeq status: PROVISIONAL
Organism: Danio rerio
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; Danionidae; Danioninae; Danio
Also known as: zgc:91981; si:dkey-177p2.11; si:dkey-177p2.12
Summary: Predicted to enable peptidase inhibitor activity. Predicted to contribute to serine-type endopeptidase inhibitor activity. Predicted to be involved in negative regulation of endopeptidase activity and negative regulation of interleukin-1 beta production. Predicted to act upstream of or within negative regulation of peptidase activity. Predicted to be active in extracellular space. Is expressed in gut; hatching gland; and lens. Orthologous to human SERPINB1 (serpin family B member 1). [provided by Alliance of Genome Resources, Apr 2022]
Orthologs: all
NEW: Try the new Gene table
Try the new Transcript table

Genomic context

Location:: chromosome: 20

Exon count:: 7

Annotation release	Status	Assembly	Chr	Location
106	current	GRCz11 (GCF_000002035.6)	20	NC_007131.7 (26880876..26886849)
105	previous assembly	GRCz10 (GCF_000002035.5)	20	NC_007131.6 (26981786..26987759)

Chromosome 20 - NC_007131.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

Go to the top of the page Help

Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

Go to the top of the page Help

See details

Project title: Sequencing the Zebrafish transcriptome from a range of tissues and developmental stages
Description: Sequencing the Zebrafish transcriptome from a range of tissues and developmental stages
BioProject: PRJEB1986
Analysis date: Fri Dec 8 19:48:10 2017

Bibliography

Go to the top of the page Help

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Submit: New GeneRIF Correction

General gene information

Go to the top of the page Help

Gene Ontology Provided by ZFIN

Function	Evidence Code	Pubs
enables serine-type endopeptidase inhibitor activity	IBA Inferred from Biological aspect of Ancestor more info
enables serine-type endopeptidase inhibitor activity	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in negative regulation of endopeptidase activity	IBA Inferred from Biological aspect of Ancestor more info

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

General protein information

Go to the top of the page Help

Preferred Names: leukocyte elastase inhibitor

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_001002653.1 → NP_001002653.1 leukocyte elastase inhibitor

See identical proteins and their annotated locations for NP_001002653.1

Status: PROVISIONAL

Source sequence(s)

BC076524

UniProtKB/TrEMBL

A0A286YBB5, A3KNH1, Q6DG30

Related

ENSDARP00000072235.5, ENSDART00000077769.7

Conserved Domains (1) summary

cl00137
Location:5 → 379

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 ...