KLKB1_BOVIN
ID KLKB1_BOVIN Reviewed; 636 AA.
AC Q2KJ63;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 114.
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;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
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 {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Plasma kallikrein
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC105498; AAI05499.1; -; mRNA.
DR RefSeq; NP_001039817.1; NM_001046352.2.
DR AlphaFoldDB; Q2KJ63; -.
DR SMR; Q2KJ63; -.
DR STRING; 9913.ENSBTAP00000012503; -.
DR MEROPS; S01.212; -.
DR PaxDb; Q2KJ63; -.
DR PRIDE; Q2KJ63; -.
DR Ensembl; ENSBTAT00000012503; ENSBTAP00000012503; ENSBTAG00000009501.
DR GeneID; 533547; -.
DR KEGG; bta:533547; -.
DR CTD; 3818; -.
DR VEuPathDB; HostDB:ENSBTAG00000009501; -.
DR VGNC; VGNC:30683; KLKB1.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000161669; -.
DR HOGENOM; CLU_031604_0_0_1; -.
DR InParanoid; Q2KJ63; -.
DR OMA; RGEKCKC; -.
DR OrthoDB; 1314811at2759; -.
DR TreeFam; TF343687; -.
DR Reactome; R-BTA-140837; Intrinsic Pathway of Fibrin Clot Formation.
DR Reactome; R-BTA-1592389; Activation of Matrix Metalloproteinases.
DR Proteomes; UP000009136; Chromosome 27.
DR Bgee; ENSBTAG00000009501; Expressed in liver and 16 other tissues.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:AgBase.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR GO; GO:0042730; P:fibrinolysis; IEA:UniProtKB-KW.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0031639; P:plasminogen activation; IEA:Ensembl.
DR GO; GO:0051919; P:positive regulation of fibrinolysis; IEA:Ensembl.
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; 3.
DR Pfam; PF14295; PAN_4; 1.
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 2: Evidence at transcript level;
KW Blood coagulation; Disulfide bond; Fibrinolysis; Glycoprotein; Hemostasis;
KW Hydrolase; Inflammatory response; Protease; Reference proteome; Repeat;
KW Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT CHAIN 20..391
FT /note="Plasma kallikrein heavy chain"
FT /id="PRO_0000285880"
FT CHAIN 392..636
FT /note="Plasma kallikrein light chain"
FT /id="PRO_0000285881"
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 294..377
FT /note="Apple 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 392..627
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 435
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 484
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 579
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 454
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 495
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 294..377
FT /evidence="ECO:0000250"
FT DISULFID 320..349
FT /evidence="ECO:0000250"
FT DISULFID 324..330
FT /evidence="ECO:0000250"
FT DISULFID 420..436
FT /evidence="ECO:0000250"
FT DISULFID 518..585
FT /evidence="ECO:0000250"
FT DISULFID 549..564
FT /evidence="ECO:0000250"
FT DISULFID 575..603
FT /evidence="ECO:0000250"
SQ SEQUENCE 636 AA; 70994 MW; 75DE0562291F03F2 CRC64;
MIALRQAAYF ICLFATVSCG CLTQLYHNIF FRGGDVSAMY TPDAQYCQLM CTFHPRCLLF
SFLPENSTSD ADKRFGCFLK DSVTGTLPRV SRTGAISGHS LKRCGHQISA CHRSIYKGID
MRGVNFNASK VRSAKECQER CTNNIHCQFF TYATKTFFSA EYRNTCLLKR SPQGTPTRIK
VLSDVESGFS LKACGNSKIG CRVDIFQHSA FSDVDVAGII APDAFVCRTI CTYHPSCLFF
TFYTNAWKTD SQRNVCFLKT SQSGSPSSPT PQENAISGYS LLTCKQTLPG TEPCHSKIYP
QVAFEGEELH VTFVKGVDGC QETCTKMIRC QFFTYSLFPE DCRGEKCKCS LRLSLDGSPT
NITYGTQASS GYSLRLCKRG DSRVCTTKRT RIVGGTNASW GEWPWQVSLQ VKQRAQSHLC
GGSIIGRQWV LTAAHCFDGL LLSNIWRIYG GILNLSEITT ETSFSQIKEI IVHPNYKISE
GSHDIALIKL EAPLNFTDLQ KAICLPSKDD TKPVYTDCWI TGWGFTEEKG KIQNTLQKAN
IPLISNEECQ KSYRDYKITK QMICAGYKEG GKDACKGDSG GPLVCQHEET WHLVGITSWG
EGCARREQPG VYTKVAEYVD WILEKTQDSH GQPLRK
