[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). TISSUE=Pancreas; DOI=10.1021/bi00348a030; PubMed=3004571 [NCBI, ExPASy, EBI, Israel, Japan] Fukushima D., Kitamura N., Nakanishi S.; "Nucleotide sequence of cloned cDNA for human pancreatic kallikrein."; Biochemistry 24:8037-8043(1985).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. TISSUE=Kidney; DOI=10.1021/bi00409a003; PubMed=2898948 [NCBI, ExPASy, EBI, Israel, Japan] Evans B.A., Yun Z.X., Close J.A., Tregear G.W., Kitamura N., Nakanishi S., Callen D.F., Baker E., Hyland V.J., Sutherland G.R., Richards R.I.; "Structure and chromosomal localization of the human renal kallikrein gene."; Biochemistry 27:3124-3129(1988).
[3]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). TISSUE=Salivary gland; PubMed=2686621 [NCBI, ExPASy, EBI, Israel, Japan] Angermann A., Bergmann C., Appelhans H.; "Cloning and expression of human salivary-gland kallikrein in Escherichia coli."; Biochem. J. 262:787-793(1989).
[4]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING, TISSUE SPECIFICITY, AND VARIANT LYS-186. PubMed=7749372 [NCBI, ExPASy, EBI, Israel, Japan] Chen L.-M., Murray S.R., Chai K.X., Chao L., Chao J.; "Molecular cloning and characterization of a novel kallikrein transcript in colon and its distribution in human tissues."; Braz. J. Med. Biol. Res. 27:1829-1838(1994).
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1006/bbrc.2000.3448; PubMed=11006094 [NCBI, ExPASy, EBI, Israel, Japan] Yousef G.M., Chang A., Scorilas A., Diamandis E.P.; "Genomic organization of the human kallikrein gene family on chromosome 19q13.3-q13.4."; Biochem. Biophys. Res. Commun. 276:125-133(2000).
[6]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1016/S0378-1119(00)00382-6; PubMed=11054574 [NCBI, ExPASy, EBI, Israel, Japan] Gan L., Lee I., Smith R., Argonza-Barrett R., Lei H., McCuaig J., Moss P., Paeper B., Wang K.; "Sequencing and expression analysis of the serine protease gene cluster located in chromosome 19q13 region."; Gene 257:119-130(2000).
[7]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Li T., Du G., Dai Y.; "Kallikrein cDNA from the pancreas of a Chinese patient."; Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
[8]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LYS-186. Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.; "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[9]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LYS-186. SeattleSNPs variation discovery resource; Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
[10]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). TISSUE=Pancreas; 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).
[11]	NUCLEOTIDE SEQUENCE [MRNA] OF 18-262 (ISOFORM 1). TISSUE=Kidney; PubMed=3853975 [NCBI, ExPASy, EBI, Israel, Japan] Baker A.R., Shine J.; "Human kidney kallikrein: cDNA cloning and sequence analysis."; DNA 4:445-450(1985).
[12]	PROTEIN SEQUENCE OF 25-262 (ISOFORM 1), AND GLYCOSYLATION AT SER-93; ASN-102; SER-104; ASN-108; ASN-165 AND SER-167. TISSUE=Urine; PubMed=3163150 [NCBI, ExPASy, EBI, Israel, Japan] Kellermann J., Lottspeich F., Geiger R., Deutzmann R.; "Human urinary kallikrein -- amino acid sequence and carbohydrate attachment sites."; Protein Seq. Data Anal. 1:177-182(1988).
[13]	PROTEIN SEQUENCE OF 25-262 (ISOFORM 1). TISSUE=Urine; PubMed=2666327 [NCBI, ExPASy, EBI, Israel, Japan] Lu H.S., Lin F.-K., Chao L., Chao J.; "Human urinary kallikrein. Complete amino acid sequence and sites of glycosylation."; Int. J. Pept. Protein Res. 33:237-249(1989).
[14]	PROTEIN SEQUENCE OF 25-55 (ISOFORM 1). TISSUE=Urine; PubMed=393608 [NCBI, ExPASy, EBI, Israel, Japan] Lottspeich F., Geiger R., Henschen A., Kutzbach C.; "N-terminal amino acid sequence of human urinary kallikrein homology with other serine proteases."; Hoppe-Seyler's Z. Physiol. Chem. 360:1947-1950(1979).
[15]	PROTEIN SEQUENCE OF 28-47 (ISOFORM 1). TISSUE=Urine; PubMed=3635530 [NCBI, ExPASy, EBI, Israel, Japan] Takahashi S., Irie A., Katayama Y., Ito K., Miyake Y.; "N-terminal amino acid sequence of human urinary prokallikrein."; J. Biochem. 99:989-992(1986).

Comments

FUNCTION: Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin.
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.
ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name 1

Isoform ID P06870-1

This is the isoform sequence displayed in this entry.

Name 2

Isoform ID P06870-2

Features which should be applied to build the isoform sequence: VSP_037483.
TISSUE SPECIFICITY: Isoform 2 is expressed in pancreas, salivary glands, kidney, colon, prostate gland, testis, spleen and the colon adenocarcinoma cell line T84.
PTM: The O-linked polysaccharides on Ser-93, Ser-104 and Ser-167 are probably the mucin type linked to GalNAc. In PubMed:3163150, GalNAc was detected with the corresponding peptides but not located.
SIMILARITY: Belongs to the peptidase S1 family. Kallikrein subfamily [view classification].
SIMILARITY: Contains 1 peptidase S1 domain [view classification].
WEB RESOURCE: Name=Wikipedia; Note=Kallikrein entry; URL="http://en.wikipedia.org/wiki/Kallikrein";.
WEB RESOURCE: Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/klk1/";.

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

M25629; AAA36136.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M33109; AAA59455.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M33105; AAA59455.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M33106; AAA59455.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M33107; AAA59455.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M33108; AAA59455.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X13561; CAA31912.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF277050; AAF86333.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF243527; AAG33353.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY703451; AAU12569.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BT007253; AAP35917.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY094609; AAM11874.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC005313; AAH05313.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M12706; AAA59201.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00304808; -.

PIR

A24696; KQHU.
B24696; B24696.

RefSeq

NP_002248.1; -.

UniGene

Hs.123107

3D structure databases

PDB

1SPJ; X-ray; 1.70 A; A=25-262.

[ExPASy / RCSB / EBI]

PDBsum

1SPJ; -.

ModBase

P06870.

Protein family/group databases

MEROPS

S01.160; -.

PTM databases

GlycoSuiteDB

P06870; -.

Enzyme and pathway databases

BRENDA

3.4.21.35; 247.

Organism-specific databases

GC19M056014; -.

HGNC:6357; KLK1.

147910; gene+phenotype. [NCBI / EBI]

PharmGKB

PA224; -.

Gene expression databases

Bgee

P06870; -.

CleanEx

HS_KLK1; -.

GermOnline

ENSG00000167748; Homo sapiens.

Ontologies

GO:0004252;	Molecular function: serine-type endopeptidase activity (traceable author statement from ProtInc).
GO:0006508;	Biological process: proteolysis (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR018114; Peptidase_S1/S6_AS.
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

ENSG00000167748; Homo sapiens. [Contig view]

GeneID

3816; -.

KEGG

hsa:3816; -.

Phylogenomic databases

HOGENOM

P06870; -.

HOVERGEN

P06870; -.

Other

DrugBank

DB00009; Alteplase.
DB00029; Anistreplase.
DB00015; Reteplase.
DB00031; Tenecteplase.

15001; -.

KLK1; Homo sapiens.

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

Keywords

3D-structure; Alternative splicing; Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase; Polymorphism; Protease; Serine protease; Signal; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 18`	`18`	`Probable.`
`PROPEP`	`19 24`	`6`	`Activation peptide (Probable).`	`PRO_0000027923`
`CHAIN`	`25 262`	`238`	`Kallikrein-1.`	`PRO_0000027924`
`DOMAIN`	`25 259`	`235`	`Peptidase S1.`
`ACT_SITE`	`65 65`		`Charge relay system.`
`ACT_SITE`	`120 120`		`Charge relay system.`
`ACT_SITE`	`214 214`		`Charge relay system.`
`CARBOHYD`	`93 93`		`O-linked (GalNAc...).`
`CARBOHYD`	`102 102`		`N-linked (GlcNAc...).`
`CARBOHYD`	`104 104`		`O-linked (GalNAc...).`
`CARBOHYD`	`108 108`		`N-linked (GlcNAc...).`
`CARBOHYD`	`165 165`		`N-linked (GlcNAc...); partial.`
`CARBOHYD`	`167 167`		`O-linked (GalNAc...).`
`DISULFID`	`31 174`		`By similarity.`
`DISULFID`	`50 66`		`By similarity.`
`DISULFID`	`153 220`		`By similarity.`
`DISULFID`	`185 199`		`By similarity.`
`DISULFID`	`210 235`		`By similarity.`
`VAR_SEQ`	`1 69`		`MWFLVLCLALSLGGTGAAPPIQSRIVGGWECEQHSQPWQA` `ALYHFSTFQCGGILVHRQWVLTAAHCISD -> MLPCPIPFSPSRLLIPPFPSFPS (in isoform 2).`	`VSP_037483`
`VARIANT`	`77 77`	`1`	`R -> H (in dbSNP:rs5515 [NCBI]).`	`VAR_014567`
`VARIANT`	`145 145`	`1`	`Q -> E (in dbSNP:rs5516 [NCBI]).`	`VAR_006625`
`VARIANT`	`186 186`	`1`	`E -> K (in dbSNP:rs5517 [NCBI]).`	`VAR_006626`
`VARIANT`	`193 193`	`1`	`V -> E (in dbSNP:rs5518 [NCBI]).`	`VAR_014568`
`CONFLICT`	`114 114`		`D -> N (in Ref. 7; AAU12569).`
`CONFLICT`	`139 139`		`V -> F (in Ref. 7; AAU12569).`
`CONFLICT`	`188 188`		`A -> V (in Ref. 8; AAP35917 and 10; AAH05313).`
`STRAND`	`39 44`	`6`
`STRAND`	`47 56`	`10`
`STRAND`	`59 62`	`4`
`HELIX`	`64 66`	`3`
`STRAND`	`69 76`	`8`
`STRAND`	`88 90`	`3`
`STRAND`	`92 97`	`6`
`HELIX`	`103 106`	`4`
`TURN`	`112 114`	`3`
`STRAND`	`122 128`	`7`
`STRAND`	`152 159`	`8`
`STRAND`	`161 165`	`5`
`STRAND`	`173 180`	`8`
`HELIX`	`182 188`	`7`
`STRAND`	`197 201`	`5`
`STRAND`	`206 208`	`3`
`STRAND`	`217 220`	`4`
`STRAND`	`223 230`	`8`
`STRAND`	`242 246`	`5`
`HELIX`	`247 250`	`4`
`HELIX`	`251 260`	`10`

Sequence information

Length: 262 AA [This is the length of the unprocessed precursor]

Molecular weight: 28890 Da [This is the MW of the unprocessed precursor]

CRC64: 772AD14A93A496C0 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MWFLVLCLAL SLGGTGAAPP IQSRIVGGWE CEQHSQPWQA ALYHFSTFQC GGILVHRQWV 

        70         80         90        100        110        120 
LTAAHCISDN YQLWLGRHNL FDDENTAQFV HVSESFPHPG FNMSLLENHT RQADEDYSHD 

       130        140        150        160        170        180 
LMLLRLTEPA DTITDAVKVV ELPTQEPEVG STCLASGWGS IEPENFSFPD DLQCVDLKIL 

       190        200        210        220        230        240 
PNDECEKAHV QKVTDFMLCV GHLEGGKDTC VGDSGGPLMC DGVLQGVTSW GYVPCGTPNK 

       250        260 
PSVAVRVLSY VKWIEDTIAE NS

P06870 in FASTA 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