P01048 · KNT1_RAT
- ProteinT-kininogen 1
- GeneMap1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids430 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Kininogens are plasma glycoproteins with a number of functions: 1 as precursor of the active peptide bradykinin they effect smooth muscle contraction, induction of hypotension and increase of vascular permeability. 2 They play a role in blood coagulation by helping to position optimally prekallikrein and factor XI next to factor XII. 3 They are inhibitor of thiol proteases.
Miscellaneous
Rats express four types of kininogens: the classical HMW and LMW kininogens produced by alternative splicing of the same gene, and two additional LMW-like kininogens: T-I and T-II.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | cysteine-type endopeptidase inhibitor activity | |
Biological Process | acute-phase response | |
Biological Process | negative regulation of blood coagulation | |
Biological Process | positive regulation of cytosolic calcium ion concentration | |
Biological Process | vasodilation |
Keywords
- Molecular function
- Biological process
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameT-kininogen 1
- Alternative names
- 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 accessionP01048
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for signal, modified residue, chain, disulfide bond, glycosylation, peptide.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-18 | |||||
Sequence: MKLITILLLCSRLLPSLA | ||||||
Modified residue | 19 | Pyrrolidone carboxylic acid | ||||
Sequence: Q | ||||||
Chain | PRO_0000006700 | 19-375 | T-kininogen 1 heavy chain | |||
Sequence: QEEGAQELNCNDETVFQAVDTALKKYNAELESGNQFVLYRVTEGTKKDGAETLYSFKYQIKEGNCSVQSGLTWQDCDFKDAEEAATGECTTTLGKKENKFSVATQICNITPGKGPKKTEEDLCVGCFQPIPMDSSDLKPVLKHAVEHFNNNTKHTHLFALREVKSAHSQVVAGMNYKIIYSIVQTNCSKEDFPSLREDCVPLPYGDHGECTGHTHVDIHNTIAGFSQSCDLYPGDDLFELLPKNCRGCPREIPVDSPELKEALGHSIAQLNAQHNHIFYFKIDTVKKATSQVVAGVIYVIEFIARETNCSKQSKTELTADCETKHLGQSLNCNANVYMRPWENKVVPTVRCQALDMM | ||||||
Chain | PRO_0000006699 | 19-430 | T-kininogen 1 | |||
Sequence: QEEGAQELNCNDETVFQAVDTALKKYNAELESGNQFVLYRVTEGTKKDGAETLYSFKYQIKEGNCSVQSGLTWQDCDFKDAEEAATGECTTTLGKKENKFSVATQICNITPGKGPKKTEEDLCVGCFQPIPMDSSDLKPVLKHAVEHFNNNTKHTHLFALREVKSAHSQVVAGMNYKIIYSIVQTNCSKEDFPSLREDCVPLPYGDHGECTGHTHVDIHNTIAGFSQSCDLYPGDDLFELLPKNCRGCPREIPVDSPELKEALGHSIAQLNAQHNHIFYFKIDTVKKATSQVVAGVIYVIEFIARETNCSKQSKTELTADCETKHLGQSLNCNANVYMRPWENKVVPTVRCQALDMMISRPPGFSPFRLVRVQETKEGTTRLLNSCEYKGRLSKARAGPAPDHQAEASTVTP | ||||||
Disulfide bond | 28↔404 | Interchain (between heavy and light chains) | ||||
Sequence: CNDETVFQAVDTALKKYNAELESGNQFVLYRVTEGTKKDGAETLYSFKYQIKEGNCSVQSGLTWQDCDFKDAEEAATGECTTTLGKKENKFSVATQICNITPGKGPKKTEEDLCVGCFQPIPMDSSDLKPVLKHAVEHFNNNTKHTHLFALREVKSAHSQVVAGMNYKIIYSIVQTNCSKEDFPSLREDCVPLPYGDHGECTGHTHVDIHNTIAGFSQSCDLYPGDDLFELLPKNCRGCPREIPVDSPELKEALGHSIAQLNAQHNHIFYFKIDTVKKATSQVVAGVIYVIEFIARETNCSKQSKTELTADCETKHLGQSLNCNANVYMRPWENKVVPTVRCQALDMMISRPPGFSPFRLVRVQETKEGTTRLLNSC | ||||||
Glycosylation | 82 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 83↔94 | |||||
Sequence: CSVQSGLTWQDC | ||||||
Disulfide bond | 107↔125 | |||||
Sequence: CTTTLGKKENKFSVATQIC | ||||||
Disulfide bond | 141↔144 | |||||
Sequence: CVGC | ||||||
Glycosylation | 168 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 204 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 205↔217 | |||||
Sequence: CSKEDFPSLREDC | ||||||
Disulfide bond | 228↔247 | |||||
Sequence: CTGHTHVDIHNTIAGFSQSC | ||||||
Disulfide bond | 263↔266 | |||||
Sequence: CRGC | ||||||
Glycosylation | 326 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 327↔339 | |||||
Sequence: CSKQSKTELTADC | ||||||
Disulfide bond | 350↔369 | |||||
Sequence: CNANVYMRPWENKVVPTVRC | ||||||
Peptide | PRO_0000006701 | 376-386 | T-kinin | |||
Sequence: ISRPPGFSPFR | ||||||
Chain | PRO_0000006702 | 387-430 | T-kininogen 1 light chain | |||
Sequence: LVRVQETKEGTTRLLNSCEYKGRLSKARAGPAPDHQAEASTVTP |
Post-translational modification
As T-kinin is preceded by a Met instead of an Arg or Lys, it is not released from its precursor by either tissue or plasma kallikrein.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Plasma.
Induction
In response to an inflammatory stimulant. T-kininogen II synthesis is induced and the plasma concentration of T-kininogen I is raised.
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 28-131 | Cystatin kininogen-type 1 | ||||
Sequence: CNDETVFQAVDTALKKYNAELESGNQFVLYRVTEGTKKDGAETLYSFKYQIKEGNCSVQSGLTWQDCDFKDAEEAATGECTTTLGKKENKFSVATQICNITPGK | ||||||
Domain | 150-253 | Cystatin kininogen-type 2 | ||||
Sequence: MDSSDLKPVLKHAVEHFNNNTKHTHLFALREVKSAHSQVVAGMNYKIIYSIVQTNCSKEDFPSLREDCVPLPYGDHGECTGHTHVDIHNTIAGFSQSCDLYPGD | ||||||
Domain | 272-375 | Cystatin kininogen-type 3 | ||||
Sequence: VDSPELKEALGHSIAQLNAQHNHIFYFKIDTVKKATSQVVAGVIYVIEFIARETNCSKQSKTELTADCETKHLGQSLNCNANVYMRPWENKVVPTVRCQALDMM | ||||||
Region | 411-430 | Disordered | ||||
Sequence: SKARAGPAPDHQAEASTVTP |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length430
- Mass (Da)47,775
- Last updated2005-02-01 v2
- ChecksumFEBBF28FA44793C3
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 7 | in Ref. 5; CAA26162 | ||||
Sequence: L → V | ||||||
Sequence conflict | 19 | in Ref. 6; AA sequence | ||||
Sequence: Q → E | ||||||
Sequence conflict | 61 | in Ref. 1; AAA41489 | ||||
Sequence: E → K | ||||||
Sequence conflict | 114 | in Ref. 2; no nucleotide entry | ||||
Sequence: K → R | ||||||
Sequence conflict | 166 | in Ref. 1; AAA41489 | ||||
Sequence: F → S | ||||||
Sequence conflict | 179-181 | in Ref. 2; no nucleotide entry | ||||
Sequence: REV → TKI | ||||||
Sequence conflict | 212 | in Ref. 2; no nucleotide entry | ||||
Sequence: S → F | ||||||
Sequence conflict | 214 | in Ref. 5; CAA26162 | ||||
Sequence: R → H | ||||||
Sequence conflict | 257 | in Ref. 2; no nucleotide entry | ||||
Sequence: E → S | ||||||
Sequence conflict | 287 | in Ref. 5; CAA26162 | ||||
Sequence: Q → R | ||||||
Sequence conflict | 389 | in Ref. 2; no nucleotide entry | ||||
Sequence: R → Q | ||||||
Sequence conflict | 414 | in Ref. 2; no nucleotide entry and 5; CAA26162 | ||||
Sequence: R → G | ||||||
Sequence conflict | 420 | in Ref. 5; CAA26162 | ||||
Sequence: D → E | ||||||
Sequence conflict | 421 | in Ref. 5; CAA26162 and 7; no nucleotide entry | ||||
Sequence: H → R | ||||||
Sequence conflict | 430 | in Ref. 1; AAA41489, 6; AA sequence, 8, 9 and 10; AA sequence | ||||
Sequence: P → S |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M11883 EMBL· GenBank· DDBJ | AAA41489.1 EMBL· GenBank· DDBJ | mRNA | ||
M16454 EMBL· GenBank· DDBJ | AAA41568.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M14356 EMBL· GenBank· DDBJ | AAA41492.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X02299 EMBL· GenBank· DDBJ | CAA26162.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. |