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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_RAT               Reviewed;         638 AA.
P14272;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
01-JAN-1990, sequence version 1.
05-JUL-2017, entry version 143.
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;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1993180; DOI=10.1021/bi00220a027;
Beaubien G., Rosinski-Chupin I., Mattei M.-G., Mbikay M., Chretien M.,
Seidah N.G.;
"Gene structure and chromosomal localization of plasma kallikrein.";
Biochemistry 30:1628-1635(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND
GLYCOSYLATION AT ASN-396.
PubMed=2598771; DOI=10.1089/dna.1989.8.563;
Seidah N.G., Ladenheim R., Mbikay M., Hamelin J., Lutfalla G.,
Rougeon F., Lazure C., Chretien M.;
"The cDNA structure of rat plasma kallikrein.";
DNA 8:563-574(1989).
-!- 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; M62357; AAA74563.1; -; Genomic_DNA.
EMBL; M62358; AAA74563.1; JOINED; Genomic_DNA.
EMBL; M62346; AAA74563.1; JOINED; Genomic_DNA.
EMBL; M62347; AAA74563.1; JOINED; Genomic_DNA.
EMBL; M62349; AAA74563.1; JOINED; Genomic_DNA.
EMBL; M62350; AAA74563.1; JOINED; Genomic_DNA.
EMBL; M62351; AAA74563.1; JOINED; Genomic_DNA.
EMBL; M62352; AAA74563.1; JOINED; Genomic_DNA.
EMBL; M62353; AAA74563.1; JOINED; Genomic_DNA.
EMBL; M62354; AAA74563.1; JOINED; Genomic_DNA.
EMBL; M62355; AAA74563.1; JOINED; Genomic_DNA.
EMBL; M62356; AAA74563.1; JOINED; Genomic_DNA.
EMBL; M30282; AAA41463.1; -; mRNA.
EMBL; M58590; AAA42069.1; -; mRNA.
PIR; A39180; KQRTPL.
UniGene; Rn.9880; -.
ProteinModelPortal; P14272; -.
SMR; P14272; -.
STRING; 10116.ENSRNOP00000019237; -.
MEROPS; S01.212; -.
iPTMnet; P14272; -.
PhosphoSitePlus; P14272; -.
PaxDb; P14272; -.
PRIDE; P14272; -.
RGD; 67382; Klkb1.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
HOGENOM; HOG000112467; -.
HOVERGEN; HBG000399; -.
InParanoid; P14272; -.
PhylomeDB; P14272; -.
BRENDA; 3.4.21.34; 5301.
PRO; PR:P14272; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005615; C:extracellular space; IDA:RGD.
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:0097421; P:liver regeneration; IEP:RGD.
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_0000028025.
CHAIN 391 638 Plasma kallikrein light chain.
/FTId=PRO_0000028026.
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:0000305}.
CARBOHYD 215 215 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 308 308 N-linked (GlcNAc...) asparagine.
{ECO:0000305}.
CARBOHYD 396 396 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:2598771}.
CARBOHYD 453 453 N-linked (GlcNAc...) asparagine.
{ECO:0000305}.
CARBOHYD 459 459 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 494 494 N-linked (GlcNAc...) asparagine.
{ECO:0000305}.
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}.
SEQUENCE 638 AA; 71274 MW; 454BEB27E8CA8F88 CRC64;
MILFKQVGYF VSLFATVSCG CLSQLYANTF FRGGDLAAIY TPDAQHCQKM CTFHPRCLLF
SFLAVSPTKE TDKRFGCFMK ESITGTLPRI HRTGAISGHS LKQCGHQLSA CHQDIYEGLD
MRGSNFNISK TDSIEECQKL CTNNIHCQFF TYATKAFHRP EYRKSCLLKR SSSGTPTSIK
PVDNLVSGFS LKSCALSEIG CPMDIFQHFA FADLNVSQVV TPDAFVCRTV CTFHPNCLFF
TFYTNEWETE SQRNVCFLKT SKSGRPSPPI IQENAVSGYS LFTCRKARPE PCHFKIYSGV
AFEGEELNAT FVQGADACQE TCTKTIRCQF FTYSLLPQDC KAEGCKCSLR LSTDGSPTRI
TYEAQGSSGY SLRLCKVVES SDCTTKINAR IVGGTNSSLG EWPWQVSLQV KLVSQNHMCG
GSIIGRQWIL TAAHCFDGIP YPDVWRIYGG ILNLSEITNK TPFSSIKELI IHQKYKMSEG
SYDIALIKLQ TPLNYTEFQK PICLPSKADT NTIYTNCWVT GWGYTKERGE TQNILQKATI
PLVPNEECQK KYRDYVITKQ MICAGYKEGG IDACKGDSGG PLVCKHSGRW QLVGITSWGE
GCARKEQPGV YTKVAEYIDW ILEKIQSSKE RALETSPA


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