Klk1c10 kallikrein 1-related peptidase C10 [Rattus norvegicus (Norway rat)] - Gene

Summary

Symbol: Klk1c10provided by RGD
Full Name: kallikrein 1-related peptidase C10provided by RGD
Primary source: RGD:1561403
See related: Ensembl:ENSRNOG00000046297 AllianceGenome:RGD:1561403
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Rattus norvegicus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus
Also known as: Klk10; rGK-10
Summary: Predicted to enable serine-type endopeptidase activity. [provided by Alliance of Genome Resources, Apr 2022]
Expression: Restricted expression toward (RPKM 38.5) See more
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Genomic context

Location:: 1q22

Exon count:: 5

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCr8 (GCF_036323735.1)	1	NC_086019.1 (103539527..103543586, complement)
RS_2023_06	previous assembly	mRatBN7.2 (GCF_015227675.2)	1	NC_051336.1 (94402993..94407052, complement)
106	previous assembly	Rnor_6.0 (GCF_000001895.5)	1	NC_005100.4 (99890294..99894353, complement)

Chromosome 1 - NC_086019.1 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: A rat RNA-Seq transcriptomic BodyMap across 11 organs and 4 developmental stages
Description: 320 RNA samples isolated from 11 organs (adrenal gland, brain, heart, kidney, liver, lung, muscle, spleen, thymus, and testes or uterus) from both sexes of Fischer 344 rats across four developmental stages (2-, 6-, 21-, and 104-weeks-old)
BioProject: PRJNA238328
Publication: PMID 24510058
Analysis date: Mon Jun 6 17:44:12 2016

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

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General gene information

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Gene Ontology Provided by RGD

Function	Evidence Code	Pubs
enables endopeptidase activity	ISO Inferred from Sequence Orthology more info
enables hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides	ISO Inferred from Sequence Orthology more info
enables serine-type endopeptidase activity	IEA Inferred from Electronic Annotation more info
enables serine-type endopeptidase activity	ISO Inferred from Sequence Orthology more info

Process	Evidence Code	Pubs
involved_in positive regulation of antibacterial peptide production	ISO Inferred from Sequence Orthology more info
involved_in proteolysis	ISO Inferred from Sequence Orthology more info

Component	Evidence Code	Pubs
located_in extracellular space	ISO Inferred from Sequence Orthology more info
part_of protein-containing complex	ISO Inferred from Sequence Orthology more info

General protein information

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Preferred Names: glandular kallikrein-10

Names: K10; T-kininogenase; endopeptidase K; glandular kallikrein-10-like; proteinase B antigen; tissue kallikrein

NP_001128645.1

EC 3.4.21.35

NCBI Reference Sequences (RefSeq)

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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_001135173.1 → NP_001128645.1 glandular kallikrein-10 precursor

See identical proteins and their annotated locations for NP_001128645.1

Status: VALIDATED

Source sequence(s)

JAXUCZ010000001

UniProtKB/Swiss-Prot

P36375

Related

ENSRNOP00000050040.4, ENSRNOT00000045756.5

Conserved Domains (2) summary

smart00020
Location:24 → 251

Tryp_SPc; Trypsin-like serine protease

cd00190
Location:25 → 254

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 ...