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P08932 (KNT2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
T-kininogen 2
Alternative name(s):
Alpha-1-MAP
Major acute phase protein
T-kininogen II
Thiostatin

Cleaved into the following 3 chains:

  1. T-kininogen 2 heavy chain
    Alternative name(s):
    T-kininogen II heavy chain
  2. T-kinin
  3. T-kininogen 2 light chain
    Alternative name(s):
    T-kininogen II light chain
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length430 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

Subcellular location

Secreted › extracellular space.

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.

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.

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.

Sequence similarities

Contains 3 cystatin kininogen-type domains.

Sequence caution

The sequence AAA41570.1 differs from that shown. Reason: Frameshift at positions 180 and 181.

Ontologies

Keywords
   Biological processAcute phase
   Cellular componentSecreted
   DomainRepeat
Signal
   Molecular functionProtease inhibitor
Thiol protease inhibitor
Vasoactive
Vasodilator
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processacute-phase response

Inferred from electronic annotation. Source: UniProtKB-KW

vasodilation

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncysteine-type endopeptidase inhibitor activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818
Chain19 – 430412T-kininogen 2
PRO_0000006703
Chain19 – 375357T-kininogen 2 heavy chain
PRO_0000006704
Peptide376 – 38611T-kinin
PRO_0000006705
Chain387 – 43044T-kininogen 2 light chain
PRO_0000006706

Regions

Domain28 – 131104Cystatin kininogen-type 1
Domain150 – 253104Cystatin kininogen-type 2
Domain272 – 375104Cystatin kininogen-type 3

Amino acid modifications

Glycosylation821N-linked (GlcNAc...) Potential
Glycosylation1261N-linked (GlcNAc...) Potential
Glycosylation1681N-linked (GlcNAc...) Potential
Glycosylation2041N-linked (GlcNAc...) Potential
Glycosylation3261N-linked (GlcNAc...) Potential
Disulfide bond28 ↔ 404Interchain (between heavy and light chains) By similarity
Disulfide bond83 ↔ 94 By similarity
Disulfide bond107 ↔ 125 By similarity
Disulfide bond141 ↔ 144 By similarity
Disulfide bond205 ↔ 217 By similarity
Disulfide bond228 ↔ 247 By similarity
Disulfide bond263 ↔ 266 By similarity
Disulfide bond327 ↔ 339 By similarity
Disulfide bond350 ↔ 369 By similarity

Experimental info

Sequence conflict26 – 272MD → LN AA sequence Ref.2
Sequence conflict281C → R in AAA41570. Ref.2
Sequence conflict551L → V AA sequence Ref.2
Sequence conflict611E → K AA sequence Ref.2
Sequence conflict1661F → S AA sequence Ref.2
Sequence conflict1791T → R AA sequence Ref.2
Sequence conflict1931N → D in AAA41570. Ref.2
Sequence conflict2121F → S AA sequence Ref.2
Sequence conflict2291R → T AA sequence Ref.2
Sequence conflict2331Y → H AA sequence Ref.2
Sequence conflict4151A → L in AAA41570. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P08932 [UniParc].

Last modified February 1, 2005. Version 2.
Checksum: D94628D848C81525

FASTA43047,704
        10         20         30         40         50         60 
MKLITILLLC SRLLPSLAQE EGAQEMDCND ETVFQAVDTA LKKYNAELES GNQFLLYRVT 

        70         80         90        100        110        120 
EGTKKDGAET LYSFKYQIKE GNCSVQSGLT WQDCDFKDAE EAATGECTTT LGKKENKFSV 

       130        140        150        160        170        180 
ATQICNITPG KGPKKTEEDL CVGCFQPIPM DSSDLKPVLK HAVEHFNNNT KHTHLFALTE 

       190        200        210        220        230        240 
VKSAHSQVVA GMNYKIIYSI VQTNCSKEDF PFLREDCVPL PYGDHGECRG HTYVDIHNTI 

       250        260        270        280        290        300 
AGFSQSCDLY PGDDLFSLLP KKCFGCPKNI PVDSPELKEA LGHSIAQLNA QHNHLFYFKI 

       310        320        330        340        350        360 
DTVKKATSQV VAGTKYVIEF IARETNCSKQ TNTELTADCE TKHLGQSLNC NANVYMRPWE 

       370        380        390        400        410        420 
NKVVPTVRCQ ALDMMISRPP GFSPFRLVQV QETKEGTTRL LNSCEYKGRL SKAGAGPAPD 

       430 
HQAEASTVTP

« Hide

References

« Hide 'large scale' references
[1]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Liver.
[2]"The relationship between rat major acute phase protein and the kininogens."
Anderson K.P., Heath E.C.
J. Biol. Chem. 260:12065-12071(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 5-430, PARTIAL PROTEIN SEQUENCE.
[3]"Primary structures of the mRNAs encoding the rat precursors for bradykinin and T-kinin. Structural relationship of kininogens with major acute phase protein and alpha 1-cysteine proteinase inhibitor."
Furuto-Kato S., Matsumoto A., Kitamura N., Nakanishi S.
J. Biol. Chem. 260:12054-12059(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 238-430.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BC088161 mRNA. Translation: AAH88161.1.
M11661 mRNA. Translation: AAA41570.1. Frameshift.
M11885 mRNA. Translation: AAA41491.1.
IPIIPI00679245.
PIRB28055.
RefSeqNP_001009628.1. NM_001009628.1.
UniGeneRn.128333.
Rn.44576.

3D structure databases

ProteinModelPortalP08932.
ModBaseSearch...

Protein family/group databases

MEROPSI25.018.

PTM databases

GlycoSuiteDBP08932.

Proteomic databases

PaxDbP08932.
PRIDEP08932.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID288001.
KEGGrno:288001.
UCSCRGD:1359376. rat.

Organism-specific databases

CTD288001.

Phylogenomic databases

eggNOGNOG72605.
HOGENOMHOG000113239.
HOVERGENHBG006224.
OrthoDBEOG4QNMVT.

Gene expression databases

ArrayExpressP08932.
GenevestigatorP08932.
GermOnlineENSRNOG00000030387. Rattus norvegicus.

Family and domain databases

InterProIPR027358. Kininogen-type_cystatin_dom.
IPR000010. Prot_inh_cystat.
IPR018073. Prot_inh_cystat_CS.
[Graphical view]
PfamPF00031. Cystatin. 3 hits.
[Graphical view]
SMARTSM00043. CY. 3 hits.
[Graphical view]
PROSITEPS00287. CYSTATIN. 2 hits.
PS51647. CYSTATIN_KININOGEN. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio627394.

Entry information

Entry nameKNT2_RAT
AccessionPrimary (citable) accession number: P08932
Secondary accession number(s): Q5M894
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: February 1, 2005
Last modified: May 1, 2013
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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