ctrl chymotrypsin-like [Danio rerio (zebrafish)] - Gene

Summary

Official Symbol: ctrlprovided by ZNC
Official Full Name: chymotrypsin-likeprovided by ZNC
Primary source: ZFIN:ZDB-GENE-040912-147
See related: Ensembl:ENSDARG00000068680 AllianceGenome:ZFIN:ZDB-GENE-040912-147
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:92292
Summary: Predicted to enable serine-type endopeptidase activity. Predicted to be involved in proteolysis. Is expressed in exocrine pancreas and pancreas. Orthologous to human CTRL (chymotrypsin like). [provided by Alliance of Genome Resources, Nov 2024]
Orthologs: all
NEW: Try the new Gene table
Try the new Transcript table

Genomic context

Location:: chromosome: 15

Exon count:: 7

Annotation release	Status	Assembly	Chr	Location
RS_2024_08	current	GRCz11 (GCF_000002035.6)	15	NC_007126.7 (37820867..37829161, complement)
105	previous assembly	GRCz10 (GCF_000002035.5)	15	NC_007126.6 (37919282..37927576, complement)

Chromosome 15 - NC_007126.7 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 hydrolase activity	IEA Inferred from Electronic Annotation more info
enables peptidase activity	IEA Inferred from Electronic Annotation more info
enables serine-type endopeptidase activity	IBA Inferred from Biological aspect of Ancestor more info
enables serine-type endopeptidase activity	IEA Inferred from Electronic Annotation more info
enables serine-type peptidase activity	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in proteolysis	IBA Inferred from Biological aspect of Ancestor more info
acts_upstream_of_or_within proteolysis	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
is_active_in cellular_component	ND No biological Data available more info

General protein information

Go to the top of the page Help

Preferred Names: chymotrypsin-like protease CTRL-1

Names: ctr1l

NP_001004582.1

EC 3.4.21.-

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_001004582.1 → NP_001004582.1 chymotrypsin-like protease CTRL-1 precursor

See identical proteins and their annotated locations for NP_001004582.1

Status: PROVISIONAL

Source sequence(s)

BC081638

UniProtKB/TrEMBL

A8E5F2, F6PAV2, Q66HW9

Related

ENSDARP00000090198.3, ENSDART00000099425.4

Conserved Domains (2) summary

smart00020
Location:31 → 254

Tryp_SPc; Trypsin-like serine protease

cd00190
Location:32 → 257

Tryp_SPc; Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad ...