[1]	NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. STRAIN=BALB/c; TISSUE=Liver; PubMed=2264928 [NCBI, ExPASy, EBI, Israel, Japan] Seidah N.G., Sawyer N., Hamelin J., Mion P., Beaubien G., Brachpapa L., Rochemont J., Mbikay M., Chretien M.; "Mouse plasma kallikrein: cDNA structure, enzyme characterization, and comparison of protein and mRNA levels among species."; DNA Cell Biol. 9:737-748(1990).
[2]	GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-127, AND MASS SPECTROMETRY. TISSUE=Plasma; DOI=10.1021/pr060186m; PubMed=16944957 [NCBI, ExPASy, EBI, Israel, Japan] Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.; "Proteome-wide characterization of N-glycosylation events by diagonal chromatography."; J. Proteome Res. 5:2438-2447(2006).
[3]	GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-127; ASN-396 AND ASN-494, AND MASS SPECTROMETRY. TISSUE=Plasma; DOI=10.1021/pr0604559; PubMed=17330941 [NCBI, ExPASy, EBI, Israel, Japan] Bernhard O.K., Kapp E.A., Simpson R.J.; "Enhanced analysis of the mouse plasma proteome using cysteine-containing tryptic glycopeptides."; J. Proteome Res. 6:987-995(2007).

Comments

FUNCTION: The enzyme cleaves Lys-Arg and Arg-Ser bonds. It activates, in a reciprocal reaction, factor XII after its binding to a negatively charged surface. It also releases bradykinin from HMW kininogen and may also play a role in the renin-angiotensin system by converting prorenin into renin.
CATALYTIC ACTIVITY: Cleaves selectively Arg-|-Xaa and Lys-|-Xaa bonds, including Lys-|-Arg and Arg-|-Ser bonds in (human) kininogen to release bradykinin.
SUBUNIT: The zymogen is activated by factor XIIa, which cleaves the molecule into a light chain, which contains the active site, and a heavy chain, which associates with HMW kininogen. These chains are linked by one or more disulfide bonds.
SUBCELLULAR LOCATION: Secreted.
SIMILARITY: Belongs to the peptidase S1 family. Plasma kallikrein subfamily [view classification].
SIMILARITY: Contains 4 apple domains.
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

M58588; AAA63393.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

A36557; KQMSPL.

NP_032481.1; -.

3D structure databases

HSSP

P00760; 1EZX. [HSSP ENTRY / PDB]

ModBase

P26262.

Protein family/group databases

MEROPS

S01.212; -.

PTM databases

PhosphoSite

P26262; -.

Organism-specific databases

MGI

MGI:102849; Klkb1.

Gene expression databases

ArrayExpress

P26262; -.

GermOnline

ENSMUSG00000031640; Mus musculus.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from InterPro).
GO:0004252;	Molecular function: serine-type endopeptidase activity (inferred from electronic annotation from InterPro).
GO:0042730;	Biological process: fibrinolysis (inferred from electronic annotation from UniProtKB-KW).
GO:0006954;	Biological process: inflammatory response (inferred from electronic annotation from UniProtKB-KW).
GO:0006508;	Biological process: proteolysis (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR000177; Apple.
IPR003014; PAN.
IPR003609; Pan_app.
IPR001254; Peptidase_S1_S6.
IPR001314; Peptidase_S1A.
Graphical view of domain structure.

Pfam

PF00024; PAN_1; 4.
PF00089; Trypsin; 1.
Pfam graphical view of domain structure.

PRINTS

PR00005; APPLEDOMAIN.
PR00722; CHYMOTRYPSIN.

SMART

SM00223; APPLE; 4.
SM00020; Tryp_SPc; 1.
SMART graphical view of domain structure.

PROSITE

PS00495; APPLE; 4.
PS50948; PAN; 4.
PS50240; TRYPSIN_DOM; 1.
PS00134; TRYPSIN_HIS; 1.
PS00135; TRYPSIN_SER; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

Ensembl

ENSMUSG00000031640; Mus musculus. [Contig view]

GeneID

16621; -.

KEGG

mmu:16621; -.

Phylogenomic databases

HOGENOM

P26262; -.

HOVERGEN

P26262; -.

Other

NextBio

290227; -.

SOURCE

Klkb1; Mus musculus.

UniRef

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

Keywords

Blood coagulation; Direct protein sequencing; Fibrinolysis; Glycoprotein; Hydrolase; Inflammatory response; Protease; Repeat; Secreted; Serine protease; Signal; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 19`	`19`
`CHAIN`	`20 390`	`371`	`Plasma kallikrein heavy chain.`	`PRO_0000028023`
`CHAIN`	`391 638`	`248`	`Plasma kallikrein light chain.`	`PRO_0000028024`
`DOMAIN`	`21 104`	`84`	`Apple 1.`
`DOMAIN`	`111 194`	`84`	`Apple 2.`
`DOMAIN`	`201 284`	`84`	`Apple 3.`
`DOMAIN`	`292 375`	`84`	`Apple 4.`
`DOMAIN`	`391 626`	`236`	`Peptidase S1.`
`ACT_SITE`	`434 434`		`Charge relay system.`
`ACT_SITE`	`483 483`		`Charge relay system.`
`ACT_SITE`	`578 578`		`Charge relay system.`
`CARBOHYD`	`127 127`		`N-linked (GlcNAc...).`
`CARBOHYD`	`215 215`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`308 308`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`396 396`		`N-linked (GlcNAc...).`
`CARBOHYD`	`494 494`		`N-linked (GlcNAc...).`
`DISULFID`	`21 104`		`By similarity.`
`DISULFID`	`47 77`		`By similarity.`
`DISULFID`	`51 57`		`By similarity.`
`DISULFID`	`111 194`		`By similarity.`
`DISULFID`	`137 166`		`By similarity.`
`DISULFID`	`141 147`		`By similarity.`
`DISULFID`	`201 284`		`By similarity.`
`DISULFID`	`227 256`		`By similarity.`
`DISULFID`	`231 237`		`By similarity.`
`DISULFID`	`292 375`		`By similarity.`
`DISULFID`	`318 347`		`By similarity.`
`DISULFID`	`322 328`		`By similarity.`
`DISULFID`	`340 345`		`By similarity.`
`DISULFID`	`383 503`		`By similarity.`
`DISULFID`	`419 435`		`By similarity.`
`DISULFID`	`517 584`		`By similarity.`
`DISULFID`	`548 563`		`By similarity.`
`DISULFID`	`574 602`		`By similarity.`

Sequence information

Length: 638 AA [This is the length of the unprocessed precursor]

Molecular weight: 71369 Da [This is the MW of the unprocessed precursor]

CRC64: CC27C93AB1086599 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MILFNRVGYF VSLFATVSCG CMTQLYKNTF FRGGDLAAIY TPDAQYCQKM CTFHPRCLLF 

        70         80         90        100        110        120 
SFLAVTPPKE TNKRFGCFMK ESITGTLPRI HRTGAISGHS LKQCGHQISA CHRDIYKGLD 

       130        140        150        160        170        180 
MRGSNFNISK TDNIEECQKL CTNNFHCQFF TYATSAFYRP EYRKKCLLKH SASGTPTSIK 

       190        200        210        220        230        240 
SADNLVSGFS LKSCALSEIG CPMDIFQHSA FADLNVSQVI TPDAFVCRTI CTFHPNCLFF 

       250        260        270        280        290        300 
TFYTNEWETE SQRNVCFLKT SKSGRPSPPI PQENAISGYS LLTCRKTRPE PCHSKIYSGV 

       310        320        330        340        350        360 
DFEGEELNVT FVQGADVCQE TCTKTIRCQF FIYSLLPQDC KEEGCKCSLR LSTDGSPTRI 

       370        380        390        400        410        420 
TYGMQGSSGY SLRLCKLVDS PDCTTKINAR IVGGTNASLG EWPWQVSLQV KLVSQTHLCG 

       430        440        450        460        470        480 
GSIIGRQWVL TAAHCFDGIP YPDVWRIYGG ILSLSEITKE TPSSRIKELI IHQEYKVSEG 

       490        500        510        520        530        540 
NYDIALIKLQ TPLNYTEFQK PICLPSKADT NTIYTNCWVT GWGYTKEQGE TQNILQKATI 

       550        560        570        580        590        600 
PLVPNEECQK KYRDYVINKQ MICAGYKEGG TDACKGDSGG PLVCKHSGRW QLVGITSWGE 

       610        620        630 
GCGRKDQPGV YTKVSEYMDW ILEKTQSSDV RALETSSA

P26262 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