P08934 · KNG1_RAT
- ProteinKininogen-1
- GeneKng1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids639 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
Kininogens are inhibitors of thiol proteases. HMW-kininogen plays an important role in blood coagulation by helping to position optimally prekallikrein and factor XI next to factor XII; HMW-kininogen inhibits the thrombin- and plasmin-induced aggregation of thrombocytes. LMW-kininogen inhibits the aggregation of thrombocytes. LMW-kininogen is in contrast to HMW-kininogen not involved in blood clotting.
Bradykinin
The active peptide bradykinin is a potent vasodilatator that is released from HMW-kininogen shows a variety of physiological effects: (A) influence in smooth muscle contraction, (B) induction of hypotension, (C) natriuresis and diuresis, (D) decrease in blood glucose level, (E) it is a mediator of inflammation and causes (E1) increase in vascular permeability, (E2) stimulation of nociceptors (4E3) release of other mediators of inflammation (e.g. prostaglandins), (F) it has a cardioprotective effect (directly via bradykinin action, indirectly via endothelium-derived relaxing factor action).
Miscellaneous
Rats express four types of kininogens: the classical HMW/LMW kininogens and two additional LMW-like kininogens: T-I and T-II.
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 387-388 | Cleavage; by ACE | ||||
Sequence: PF |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Cellular Component | extracellular space | |
Cellular Component | perikaryon | |
Molecular Function | cysteine-type endopeptidase inhibitor activity | |
Molecular Function | protease binding | |
Biological Process | blood coagulation | |
Biological Process | Factor XII activation | |
Biological Process | negative regulation of blood coagulation | |
Biological Process | negative regulation of lymphocyte proliferation | |
Biological Process | negative regulation of proteolysis | |
Biological Process | negative regulation of T cell proliferation | |
Biological Process | positive regulation of cytosolic calcium ion concentration | |
Biological Process | positive regulation of endothelial cell proliferation | |
Biological Process | positive regulation of fibroblast proliferation | |
Biological Process | positive regulation of MAPK cascade | |
Biological Process | vasodilation |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameKininogen-1
- Cleaved into 3 chains
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionP08934
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation, modified residue, peptide.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-18 | |||||
Sequence: MKLITILLLCSRLLPSLA | ||||||
Chain | PRO_0000006696 | 19-380 | Kininogen-1 heavy chain | |||
Sequence: QEEDAQEMDCNDESLFQAVDTALKKYNAGLKSGNQFVLYQVTEGTKKDGSKTFYSFKYQIKEGNCSVQSGFAWQDCDFKDAEEAATGECTATLEKRRNNKFSIATQICNITPGKGPIVTNEYHCLGCMHPISVDSPELGPVLKHAVEHFNNNTKHTHLFALGEVKSADRQVVAGMNYQIIYSIVQTNCSKEDFPSLHEDCVPLPSGDDGECKGNAFVDIHKTIAGFSDSCEFYPGDDLFELLPEDCPGCPRNIPVDSPELKEALGHSIAQLNAENNHTFYFKIDTVKKATSQVVAGTKYVIEFIARETKCSKESNAELTADCETKRLGQSLNCNANVYMRPWENKVVPTVKCKVLDMTSVIR | ||||||
Chain | PRO_0000006695 | 19-639 | Kininogen-1 | |||
Sequence: QEEDAQEMDCNDESLFQAVDTALKKYNAGLKSGNQFVLYQVTEGTKKDGSKTFYSFKYQIKEGNCSVQSGFAWQDCDFKDAEEAATGECTATLEKRRNNKFSIATQICNITPGKGPIVTNEYHCLGCMHPISVDSPELGPVLKHAVEHFNNNTKHTHLFALGEVKSADRQVVAGMNYQIIYSIVQTNCSKEDFPSLHEDCVPLPSGDDGECKGNAFVDIHKTIAGFSDSCEFYPGDDLFELLPEDCPGCPRNIPVDSPELKEALGHSIAQLNAENNHTFYFKIDTVKKATSQVVAGTKYVIEFIARETKCSKESNAELTADCETKRLGQSLNCNANVYMRPWENKVVPTVKCKVLDMTSVIRRPPGFSPFRAPRVKKPKESTTVSPSYIARVQEERDPGNEQGPIHGHGWLHAKQIKNKNHQGHKHGHGIGHGHQKPHGLGHGHQLKLDDLKQQREDGYDHRHPVGHGHGQRHGHGHGHGHGRDKHTNKDKNNVKHTDQRRAPLTSSSEDNTTSTQIQGRTEGFTLNPPLAQPAVISRGFQDSGFTEGVIATTSPYDTETHDDLIPDIHVQPDSLSFKLISDFPEATSHKCPGRPWKPVSRKDPTIETTEFSDFDLLDALS | ||||||
Disulfide bond | 28↔609 | Interchain (between heavy and light chains) | ||||
Sequence: CNDESLFQAVDTALKKYNAGLKSGNQFVLYQVTEGTKKDGSKTFYSFKYQIKEGNCSVQSGFAWQDCDFKDAEEAATGECTATLEKRRNNKFSIATQICNITPGKGPIVTNEYHCLGCMHPISVDSPELGPVLKHAVEHFNNNTKHTHLFALGEVKSADRQVVAGMNYQIIYSIVQTNCSKEDFPSLHEDCVPLPSGDDGECKGNAFVDIHKTIAGFSDSCEFYPGDDLFELLPEDCPGCPRNIPVDSPELKEALGHSIAQLNAENNHTFYFKIDTVKKATSQVVAGTKYVIEFIARETKCSKESNAELTADCETKRLGQSLNCNANVYMRPWENKVVPTVKCKVLDMTSVIRRPPGFSPFRAPRVKKPKESTTVSPSYIARVQEERDPGNEQGPIHGHGWLHAKQIKNKNHQGHKHGHGIGHGHQKPHGLGHGHQLKLDDLKQQREDGYDHRHPVGHGHGQRHGHGHGHGHGRDKHTNKDKNNVKHTDQRRAPLTSSSEDNTTSTQIQGRTEGFTLNPPLAQPAVISRGFQDSGFTEGVIATTSPYDTETHDDLIPDIHVQPDSLSFKLISDFPEATSHKC | ||||||
Glycosylation | 82 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 83↔94 | |||||
Sequence: CSVQSGFAWQDC | ||||||
Disulfide bond | 107↔126 | |||||
Sequence: CTATLEKRRNNKFSIATQIC | ||||||
Disulfide bond | 142↔145 | |||||
Sequence: CLGC | ||||||
Glycosylation | 169 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 205 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 206↔218 | |||||
Sequence: CSKEDFPSLHEDC | ||||||
Disulfide bond | 229↔248 | |||||
Sequence: CKGNAFVDIHKTIAGFSDSC | ||||||
Disulfide bond | 264↔267 | |||||
Sequence: CPGC | ||||||
Glycosylation | 294 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 328↔340 | |||||
Sequence: CSKESNAELTADC | ||||||
Modified residue | 332 | Phosphoserine | ||||
Sequence: S | ||||||
Disulfide bond | 351↔370 | |||||
Sequence: CNANVYMRPWENKVVPTVKC | ||||||
Peptide | PRO_0000006697 | 381-389 | Bradykinin | |||
Sequence: RPPGFSPFR | ||||||
Chain | PRO_0000006698 | 390-639 | Kininogen-1 light chain | |||
Sequence: APRVKKPKESTTVSPSYIARVQEERDPGNEQGPIHGHGWLHAKQIKNKNHQGHKHGHGIGHGHQKPHGLGHGHQLKLDDLKQQREDGYDHRHPVGHGHGQRHGHGHGHGHGRDKHTNKDKNNVKHTDQRRAPLTSSSEDNTTSTQIQGRTEGFTLNPPLAQPAVISRGFQDSGFTEGVIATTSPYDTETHDDLIPDIHVQPDSLSFKLISDFPEATSHKCPGRPWKPVSRKDPTIETTEFSDFDLLDALS | ||||||
Glycosylation | 529 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
Bradykinin is released from kininogen by plasma kallikrein.
Phosphorylated by FAM20C in the extracellular medium.
Bradykinin
Bradykinin is inactivated by ACE, which removes the dipeptide Arg-Phe from its C-terminus.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Plasma.
Structure
Family & Domains
Features
Showing features for domain, compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 28-132 | Cystatin kininogen-type 1 | ||||
Sequence: CNDESLFQAVDTALKKYNAGLKSGNQFVLYQVTEGTKKDGSKTFYSFKYQIKEGNCSVQSGFAWQDCDFKDAEEAATGECTATLEKRRNNKFSIATQICNITPGK | ||||||
Domain | 151-254 | Cystatin kininogen-type 2 | ||||
Sequence: VDSPELGPVLKHAVEHFNNNTKHTHLFALGEVKSADRQVVAGMNYQIIYSIVQTNCSKEDFPSLHEDCVPLPSGDDGECKGNAFVDIHKTIAGFSDSCEFYPGD | ||||||
Domain | 273-376 | Cystatin kininogen-type 3 | ||||
Sequence: VDSPELKEALGHSIAQLNAENNHTFYFKIDTVKKATSQVVAGTKYVIEFIARETKCSKESNAELTADCETKRLGQSLNCNANVYMRPWENKVVPTVKCKVLDMT | ||||||
Compositional bias | 438-459 | Basic residues | ||||
Sequence: NHQGHKHGHGIGHGHQKPHGLG | ||||||
Region | 438-462 | Disordered | ||||
Sequence: NHQGHKHGHGIGHGHQKPHGLGHGH | ||||||
Region | 476-547 | Disordered | ||||
Sequence: GYDHRHPVGHGHGQRHGHGHGHGHGRDKHTNKDKNNVKHTDQRRAPLTSSSEDNTTSTQIQGRTEGFTLNPP | ||||||
Compositional bias | 484-500 | Basic residues | ||||
Sequence: GHGHGQRHGHGHGHGHG | ||||||
Compositional bias | 501-516 | Basic and acidic residues | ||||
Sequence: RDKHTNKDKNNVKHTD | ||||||
Compositional bias | 517-543 | Polar residues | ||||
Sequence: QRRAPLTSSSEDNTTSTQIQGRTEGFT |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing.
P08934-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- NameHMW
- Length639
- Mass (Da)70,933
- Last updated1988-11-01 v1
- ChecksumD3172DF94FF56AF5
P08934-2
- NameLMW
Computationally mapped potential isoform sequences
There are 9 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8I6AXR2 | A0A8I6AXR2_RAT | Kng2 | 426 | ||
A0A0G2JVQ5 | A0A0G2JVQ5_RAT | Kng2 | 677 | ||
A0A8I6ACG6 | A0A8I6ACG6_RAT | Kng2 | 458 | ||
A0A8I5ZWQ0 | A0A8I5ZWQ0_RAT | Kng2 | 625 | ||
Q5PQU1 | Q5PQU1_RAT | Kng2 | 430 | ||
A0A8I5Y6S4 | A0A8I5Y6S4_RAT | Kng2 | 430 | ||
A0A8I6GER1 | A0A8I6GER1_RAT | Kng2l1 | 639 | ||
A0A8I5ZK39 | A0A8I5ZK39_RAT | Kng2 | 420 | ||
A0A8I5ZRM0 | A0A8I5ZRM0_RAT | Kng2 | 638 |
Features
Showing features for sequence conflict, alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 61 | in Ref. 2 | ||||
Sequence: E → K | ||||||
Alternative sequence | VSP_001265 | 402-433 | in isoform LMW | |||
Sequence: VSPSYIARVQEERDPGNEQGPIHGHGWLHAKQ → RLLNSCEYKGRLLKAGAGPAPERQAEASTVTP | ||||||
Alternative sequence | VSP_001266 | 434-639 | in isoform LMW | |||
Sequence: Missing | ||||||
Compositional bias | 438-459 | Basic residues | ||||
Sequence: NHQGHKHGHGIGHGHQKPHGLG | ||||||
Compositional bias | 484-500 | Basic residues | ||||
Sequence: GHGHGQRHGHGHGHGHG | ||||||
Compositional bias | 501-516 | Basic and acidic residues | ||||
Sequence: RDKHTNKDKNNVKHTD | ||||||
Compositional bias | 517-543 | Polar residues | ||||
Sequence: QRRAPLTSSSEDNTTSTQIQGRTEGFT |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L29428 EMBL· GenBank· DDBJ | AAA41486.1 EMBL· GenBank· DDBJ | mRNA | ||
M11884 EMBL· GenBank· DDBJ | AAA41487.1 EMBL· GenBank· DDBJ | mRNA | ||
M14369 EMBL· GenBank· DDBJ | AAA41484.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M14369 EMBL· GenBank· DDBJ | AAA41485.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
M16455 EMBL· GenBank· DDBJ | AAA41482.1 EMBL· GenBank· DDBJ | Genomic DNA |