KLKB1_RAT
ID KLKB1_RAT Reviewed; 638 AA.
AC P14272;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Plasma kallikrein;
DE EC=3.4.21.34;
DE AltName: Full=Fletcher factor;
DE AltName: Full=Kininogenin;
DE AltName: Full=Plasma prekallikrein;
DE Contains:
DE RecName: Full=Plasma kallikrein heavy chain;
DE Contains:
DE RecName: Full=Plasma kallikrein light chain;
DE Flags: Precursor;
GN Name=Klkb1; Synonyms=Klk3, Pk;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1993180; DOI=10.1021/bi00220a027;
RA Beaubien G., Rosinski-Chupin I., Mattei M.-G., Mbikay M., Chretien M.,
RA Seidah N.G.;
RT "Gene structure and chromosomal localization of plasma kallikrein.";
RL Biochemistry 30:1628-1635(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND GLYCOSYLATION AT
RP ASN-396.
RX PubMed=2598771; DOI=10.1089/dna.1989.8.563;
RA Seidah N.G., Ladenheim R., Mbikay M., Hamelin J., Lutfalla G., Rougeon F.,
RA Lazure C., Chretien M.;
RT "The cDNA structure of rat plasma kallikrein.";
RL DNA 8:563-574(1989).
CC -!- FUNCTION: The enzyme cleaves Lys-Arg and Arg-Ser bonds. It activates,
CC in a reciprocal reaction, factor XII after its binding to a negatively
CC charged surface. It also releases bradykinin from HMW kininogen and may
CC also play a role in the renin-angiotensin system by converting prorenin
CC into renin.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleaves selectively Arg-|-Xaa and Lys-|-Xaa bonds, including
CC Lys-|-Arg and Arg-|-Ser bonds in (human) kininogen to release
CC bradykinin.; EC=3.4.21.34;
CC -!- ACTIVITY REGULATION: Inhibited by SERPINA5. {ECO:0000250}.
CC -!- SUBUNIT: Forms a heterodimer with SERPINA5. The zymogen is activated by
CC factor XIIa, which cleaves the molecule into a light chain, which
CC contains the active site, and a heavy chain, which associates with HMW
CC kininogen. These chains are linked by one or more disulfide bonds (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Plasma kallikrein
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; M62357; AAA74563.1; -; Genomic_DNA.
DR EMBL; M62358; AAA74563.1; JOINED; Genomic_DNA.
DR EMBL; M62346; AAA74563.1; JOINED; Genomic_DNA.
DR EMBL; M62347; AAA74563.1; JOINED; Genomic_DNA.
DR EMBL; M62349; AAA74563.1; JOINED; Genomic_DNA.
DR EMBL; M62350; AAA74563.1; JOINED; Genomic_DNA.
DR EMBL; M62351; AAA74563.1; JOINED; Genomic_DNA.
DR EMBL; M62352; AAA74563.1; JOINED; Genomic_DNA.
DR EMBL; M62353; AAA74563.1; JOINED; Genomic_DNA.
DR EMBL; M62354; AAA74563.1; JOINED; Genomic_DNA.
DR EMBL; M62355; AAA74563.1; JOINED; Genomic_DNA.
DR EMBL; M62356; AAA74563.1; JOINED; Genomic_DNA.
DR EMBL; M30282; AAA41463.1; -; mRNA.
DR EMBL; M58590; AAA42069.1; -; mRNA.
DR PIR; A39180; KQRTPL.
DR AlphaFoldDB; P14272; -.
DR SMR; P14272; -.
DR STRING; 10116.ENSRNOP00000019237; -.
DR BindingDB; P14272; -.
DR ChEMBL; CHEMBL4105792; -.
DR MEROPS; S01.212; -.
DR GlyGen; P14272; 6 sites.
DR iPTMnet; P14272; -.
DR PhosphoSitePlus; P14272; -.
DR PaxDb; P14272; -.
DR RGD; 67382; Klkb1.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; P14272; -.
DR PhylomeDB; P14272; -.
DR BRENDA; 3.4.21.34; 5301.
DR Reactome; R-RNO-140837; Intrinsic Pathway of Fibrin Clot Formation.
DR Reactome; R-RNO-1592389; Activation of Matrix Metalloproteinases.
DR PRO; PR:P14272; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0007597; P:blood coagulation, intrinsic pathway; ISO:RGD.
DR GO; GO:0042730; P:fibrinolysis; IEA:UniProtKB-KW.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0097421; P:liver regeneration; IEP:RGD.
DR GO; GO:0031639; P:plasminogen activation; ISO:RGD.
DR GO; GO:0051919; P:positive regulation of fibrinolysis; ISO:RGD.
DR GO; GO:0006508; P:proteolysis; ISO:RGD.
DR GO; GO:0031638; P:zymogen activation; ISO:RGD.
DR CDD; cd01100; APPLE_Factor_XI_like; 4.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 1.
DR InterPro; IPR000177; Apple.
DR InterPro; IPR003609; Pan_app.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR Pfam; PF00024; PAN_1; 4.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00005; APPLEDOMAIN.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00223; APPLE; 4.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS00495; APPLE; 4.
DR PROSITE; PS50948; PAN; 4.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW Blood coagulation; Direct protein sequencing; Disulfide bond; Fibrinolysis;
KW Glycoprotein; Hemostasis; Hydrolase; Inflammatory response; Protease;
KW Reference proteome; Repeat; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..19
FT CHAIN 20..390
FT /note="Plasma kallikrein heavy chain"
FT /id="PRO_0000028025"
FT CHAIN 391..638
FT /note="Plasma kallikrein light chain"
FT /id="PRO_0000028026"
FT DOMAIN 21..104
FT /note="Apple 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 111..194
FT /note="Apple 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 201..284
FT /note="Apple 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 292..375
FT /note="Apple 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 391..626
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 434
FT /note="Charge relay system"
FT ACT_SITE 483
FT /note="Charge relay system"
FT ACT_SITE 578
FT /note="Charge relay system"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 396
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:2598771"
FT CARBOHYD 453
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 494
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 21..104
FT /evidence="ECO:0000250"
FT DISULFID 47..77
FT /evidence="ECO:0000250"
FT DISULFID 51..57
FT /evidence="ECO:0000250"
FT DISULFID 111..194
FT /evidence="ECO:0000250"
FT DISULFID 137..166
FT /evidence="ECO:0000250"
FT DISULFID 141..147
FT /evidence="ECO:0000250"
FT DISULFID 201..284
FT /evidence="ECO:0000250"
FT DISULFID 227..256
FT /evidence="ECO:0000250"
FT DISULFID 231..237
FT /evidence="ECO:0000250"
FT DISULFID 292..375
FT /evidence="ECO:0000250"
FT DISULFID 318..347
FT /evidence="ECO:0000250"
FT DISULFID 322..328
FT /evidence="ECO:0000250"
FT DISULFID 340..345
FT /evidence="ECO:0000250"
FT DISULFID 383..503
FT /evidence="ECO:0000250"
FT DISULFID 419..435
FT /evidence="ECO:0000250"
FT DISULFID 517..584
FT /evidence="ECO:0000250"
FT DISULFID 548..563
FT /evidence="ECO:0000250"
FT DISULFID 574..602
FT /evidence="ECO:0000250"
SQ 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
