[1]	NUCLEOTIDE SEQUENCE. TISSUE=Testis; PubMed=11082197 [NCBI, ExPASy, EBI, Israel, Japan] Matsui H., Moriyama A., Takahashi T.; "Cloning and characterization of mouse Klk27, a novel tissue kallikrein expressed in testicular Leydig cells and exhibiting chymotrypsin-like specificity."; Eur. J. Biochem. 267:6858-6865(2000).
[2]	NUCLEOTIDE SEQUENCE, FUNCTION, ENZYME REGULATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION. TISSUE=Testis; DOI=10.1210/en.142.11.4918; PubMed=11606460 [NCBI, ExPASy, EBI, Israel, Japan] Matsui H., Takahashi T.; "Mouse testicular Leydig cells express Klk21, a tissue kallikrein that cleaves fibronectin and IGF-binding protein-3."; Endocrinology 142:4918-4929(2001).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=FVB/N; TISSUE=Salivary gland; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[4]	NUCLEOTIDE SEQUENCE OF 17-54 AND 70-122. STRAIN=BALB/c; TISSUE=Liver; PubMed=3036794 [NCBI, ExPASy, EBI, Israel, Japan] Evans B.A., Drinkwater C.C., Richards R.I.; "Mouse glandular kallikrein genes. Structure and partial sequence analysis of the kallikrein gene locus."; J. Biol. Chem. 262:8027-8034(1987).

Comments

FUNCTION: Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin. Displays trypsin-like substrate specificity and shows activity towards casein, gelatin, fibronectin and IGFBP3.
CATALYTIC ACTIVITY: Preferential cleavage of Arg-|-Xaa bonds in small molecule substrates. Highly selective action to release kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of Met-|-Xaa or Leu-|-Xaa.
ENZYME REGULATION: Inhibited by protease inhibitors diisopropylfluorophosphate, leupeptin, antipain, benzamidine, phenylmethylsulfonyl fluoride and soybean trypsin inhibitor.
TISSUE SPECIFICITY: Expressed in testis and submaxillary gland. In the testis, expression localized specifically to Leydig cells in the interstitial tissues.
DEVELOPMENTAL STAGE: Detectable in testis 4 weeks after birth, becoming more prominent thereafter.
INDUCTION: By T protein.
SIMILARITY: Belongs to the peptidase S1 family. Kallikrein subfamily [view classification].
SIMILARITY: Contains 1 peptidase S1 domain [view classification].

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AB039276; BAA92319.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC012243; AAH12243.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M18597; AAA39359.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M18617; AAA39360.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

I70036; I70036.
I70037; I70037.

RefSeq

NP_034772.1; -.

UniGene

Mm.443292

3D structure databases

HSSP

P00757; 1SGF. [HSSP ENTRY / PDB]

SMR

Q61759; 25-261.

ModBase

Q61759.

Protein family/group databases

MEROPS

S01.038; -.

Organism-specific databases

MGI

MGI:892022; Klk1b21.

Gene expression databases

ArrayExpress

Q61759; -.

CleanEx

MM_KLK1B21; -.

GermOnline

ENSMUSG00000066516; Mus musculus.

Ontologies

GO:0005615;	Cellular component: extracellular space (inferred from direct assay from MGI).
GO:0008233;	Molecular function: peptidase activity (inferred from direct assay from MGI).
GO:0006508;	Biological process: proteolysis (inferred from direct assay from MGI).
QuickGo view.

Family and domain databases

InterPro

IPR001254; Peptidase_S1_S6.
IPR001314; Peptidase_S1A.
Graphical view of domain structure.

Pfam

PF00089; Trypsin; 1.
Pfam graphical view of domain structure.

PRINTS

PR00722; CHYMOTRYPSIN.

SMART

SM00020; Tryp_SPc; 1.
SMART graphical view of domain structure.

PROSITE

PS50240; TRYPSIN_DOM; 1.
PS00134; TRYPSIN_HIS; 1.
PS00135; TRYPSIN_SER; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

Ensembl

ENSMUSG00000066516; Mus musculus. [Contig view]

GeneID

16616; -.

KEGG

mmu:16616; -.

Phylogenomic databases

HOVERGEN

Q61759; -.

Other

NextBio

290211; -.

SOURCE

Klk1b21; Mus musculus.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Glycoprotein; Hydrolase; Protease; Serine protease; Signal; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 17`	`17`	`Potential.`
`PROPEP`	`18 24`	`7`	`Activation peptide (By similarity).`	`PRO_0000027987`
`CHAIN`	`25 261`	`237`	`Kallikrein 1-related peptidase b21.`	`PRO_0000027988`
`DOMAIN`	`25 258`	`234`	`Peptidase S1.`
`ACT_SITE`	`65 65`		`Charge relay system (By similarity).`
`ACT_SITE`	`120 120`		`Charge relay system (By similarity).`
`ACT_SITE`	`213 213`		`Charge relay system (By similarity).`
`CARBOHYD`	`102 102`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`31 173`		`By similarity.`
`DISULFID`	`50 66`		`By similarity.`
`DISULFID`	`152 219`		`By similarity.`
`DISULFID`	`184 198`		`By similarity.`
`DISULFID`	`209 234`		`By similarity.`

Sequence information

Length: 261 AA [This is the length of the unprocessed precursor]

Molecular weight: 28690 Da [This is the MW of the unprocessed precursor]

CRC64: 608B976BC78E03EE [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRFLILFLAL SLGEIDAAPP VQSRIVGGFN CEKNSQPWHV AVFRYNKYIC GGVLLNPNWV 

        70         80         90        100        110        120 
LTAAHCYGNQ YNVWLGKNKL FQHESSAQHR LVSKSFPHPD YNMSLMNDHT PHPEDDYSND 

       130        140        150        160        170        180 
LMLLRLSKPA DITDAVKPID LPTEEPKLGS TCLASGWGSI TPTKWQIPND LQCGFIKPLP 

       190        200        210        220        230        240 
NENCAKAYIH KVTDVMLCAG EMGGGKDTCA GDSGGPLICD GVLQGITSWG SIPCAKPNAP 

       250        260 
AIYTKLIKFT SWIKDTMAKN P

Q61759 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools