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Plasma kallikrein (EC 3.4.21.34) (Fletcher factor) (Kininogenin) (Plasma prekallikrein) [Cleaved into: Plasma kallikrein heavy chain; Plasma kallikrein light chain]

 KLKB1_MOUSE             Reviewed;         638 AA.
P26262; Q8R0P5;
01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
05-JUL-2017, entry version 165.
RecName: Full=Plasma kallikrein;
EC=3.4.21.34;
AltName: Full=Fletcher factor;
AltName: Full=Kininogenin;
AltName: Full=Plasma prekallikrein;
Contains:
RecName: Full=Plasma kallikrein heavy chain;
Contains:
RecName: Full=Plasma kallikrein light chain;
Flags: Precursor;
Name=Klkb1; Synonyms=Klk3, Pk;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
STRAIN=BALB/cJ; TISSUE=Liver;
PubMed=2264928; DOI=10.1089/dna.1990.9.737;
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]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[3]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-127.
STRAIN=C57BL/6J; TISSUE=Plasma;
PubMed=16944957; DOI=10.1021/pr060186m;
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).
[4]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-127; ASN-396 AND ASN-494.
STRAIN=C57BL/6J; TISSUE=Plasma;
PubMed=17330941; DOI=10.1021/pr0604559;
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).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Heart, Liver, and Lung;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- 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.
-!- ENZYME REGULATION: Inhibited by SERPINA5. {ECO:0000250}.
-!- SUBUNIT: Forms a heterodimer with SERPINA5. 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 (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- SIMILARITY: Belongs to the peptidase S1 family. Plasma kallikrein
subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}.
-----------------------------------------------------------------------
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EMBL; M58588; AAA63393.1; -; mRNA.
EMBL; BC026555; AAH26555.1; -; mRNA.
CCDS; CCDS22275.1; -.
PIR; A36557; KQMSPL.
RefSeq; NP_032481.2; NM_008455.3.
UniGene; Mm.482691; -.
ProteinModelPortal; P26262; -.
SMR; P26262; -.
STRING; 10090.ENSMUSP00000112174; -.
ChEMBL; CHEMBL1250359; -.
MEROPS; S01.212; -.
iPTMnet; P26262; -.
PhosphoSitePlus; P26262; -.
SwissPalm; P26262; -.
MaxQB; P26262; -.
PaxDb; P26262; -.
PeptideAtlas; P26262; -.
PRIDE; P26262; -.
Ensembl; ENSMUST00000026907; ENSMUSP00000026907; ENSMUSG00000109764.
GeneID; 16621; -.
KEGG; mmu:16621; -.
UCSC; uc009lot.4; mouse.
CTD; 3818; -.
MGI; MGI:102849; Klkb1.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00760000118962; -.
HOGENOM; HOG000112467; -.
HOVERGEN; HBG000399; -.
InParanoid; P26262; -.
KO; K01324; -.
OrthoDB; EOG091G0AH5; -.
TreeFam; TF343687; -.
BRENDA; 3.4.21.34; 3474.
Reactome; R-MMU-140837; Intrinsic Pathway of Fibrin Clot Formation.
Reactome; R-MMU-1592389; Activation of Matrix Metalloproteinases.
PRO; PR:P26262; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000031640; -.
Genevisible; P26262; MM.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005615; C:extracellular space; ISO:MGI.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0007597; P:blood coagulation, intrinsic pathway; IEA:InterPro.
GO; GO:0042730; P:fibrinolysis; IEA:UniProtKB-KW.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0031639; P:plasminogen activation; ISO:MGI.
GO; GO:0051919; P:positive regulation of fibrinolysis; ISO:MGI.
CDD; cd00190; Tryp_SPc; 1.
InterPro; IPR000177; Apple.
InterPro; IPR003609; Pan_app.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR034813; Plasma_kallikrein.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
PANTHER; PTHR24256:SF313; PTHR24256:SF313; 1.
Pfam; PF00024; PAN_1; 4.
Pfam; PF00089; Trypsin; 1.
PRINTS; PR00005; APPLEDOMAIN.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00223; APPLE; 4.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
PROSITE; PS00495; APPLE; 4.
PROSITE; PS50948; PAN; 4.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
1: Evidence at protein level;
Blood coagulation; Complete proteome; Direct protein sequencing;
Disulfide bond; Fibrinolysis; Glycoprotein; Hemostasis; Hydrolase;
Inflammatory response; Protease; Reference proteome; Repeat; Secreted;
Serine protease; Signal; Zymogen.
SIGNAL 1 19
CHAIN 20 390 Plasma kallikrein heavy chain.
/FTId=PRO_0000028023.
CHAIN 391 638 Plasma kallikrein light chain.
/FTId=PRO_0000028024.
DOMAIN 21 104 Apple 1. {ECO:0000255|PROSITE-
ProRule:PRU00315}.
DOMAIN 111 194 Apple 2. {ECO:0000255|PROSITE-
ProRule:PRU00315}.
DOMAIN 201 284 Apple 3. {ECO:0000255|PROSITE-
ProRule:PRU00315}.
DOMAIN 292 375 Apple 4. {ECO:0000255|PROSITE-
ProRule:PRU00315}.
DOMAIN 391 626 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
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...) asparagine.
{ECO:0000269|PubMed:16944957,
ECO:0000269|PubMed:17330941}.
CARBOHYD 215 215 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 308 308 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 396 396 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17330941}.
CARBOHYD 494 494 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17330941}.
DISULFID 21 104 {ECO:0000250}.
DISULFID 47 77 {ECO:0000250}.
DISULFID 51 57 {ECO:0000250}.
DISULFID 111 194 {ECO:0000250}.
DISULFID 137 166 {ECO:0000250}.
DISULFID 141 147 {ECO:0000250}.
DISULFID 201 284 {ECO:0000250}.
DISULFID 227 256 {ECO:0000250}.
DISULFID 231 237 {ECO:0000250}.
DISULFID 292 375 {ECO:0000250}.
DISULFID 318 347 {ECO:0000250}.
DISULFID 322 328 {ECO:0000250}.
DISULFID 340 345 {ECO:0000250}.
DISULFID 383 503 {ECO:0000250}.
DISULFID 419 435 {ECO:0000250}.
DISULFID 517 584 {ECO:0000250}.
DISULFID 548 563 {ECO:0000250}.
DISULFID 574 602 {ECO:0000250}.
CONFLICT 603 603 A -> G (in Ref. 1; AAA63393).
{ECO:0000305}.
SEQUENCE 638 AA; 71383 MW; CC27C93F4B57C599 CRC64;
MILFNRVGYF VSLFATVSCG CMTQLYKNTF FRGGDLAAIY TPDAQYCQKM CTFHPRCLLF
SFLAVTPPKE TNKRFGCFMK ESITGTLPRI HRTGAISGHS LKQCGHQISA CHRDIYKGLD
MRGSNFNISK TDNIEECQKL CTNNFHCQFF TYATSAFYRP EYRKKCLLKH SASGTPTSIK
SADNLVSGFS LKSCALSEIG CPMDIFQHSA FADLNVSQVI TPDAFVCRTI CTFHPNCLFF
TFYTNEWETE SQRNVCFLKT SKSGRPSPPI PQENAISGYS LLTCRKTRPE PCHSKIYSGV
DFEGEELNVT FVQGADVCQE TCTKTIRCQF FIYSLLPQDC KEEGCKCSLR LSTDGSPTRI
TYGMQGSSGY SLRLCKLVDS PDCTTKINAR IVGGTNASLG EWPWQVSLQV KLVSQTHLCG
GSIIGRQWVL TAAHCFDGIP YPDVWRIYGG ILSLSEITKE TPSSRIKELI IHQEYKVSEG
NYDIALIKLQ TPLNYTEFQK PICLPSKADT NTIYTNCWVT GWGYTKEQGE TQNILQKATI
PLVPNEECQK KYRDYVINKQ MICAGYKEGG TDACKGDSGG PLVCKHSGRW QLVGITSWGE
GCARKDQPGV YTKVSEYMDW ILEKTQSSDV RALETSSA


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