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P36375 (KLK10_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glandular kallikrein-10

Short name=K10
Short name=rGK-10
EC=3.4.21.35
Alternative name(s):
Endopeptidase K
Proteinase B
T-kininogenase
Tissue kallikrein

Cleaved into the following 2 chains:

  1. T-kininogenase light chain
  2. T-kininogenase heavy chain
Gene names
Name:Klk10
Synonyms:Klk-10
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length259 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin. This protein may be involved in the regulation of renal function.

Catalytic activity

Preferential cleavage of Arg-|-Xaa bonds in small molecule substrates. Highly selective action to release kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of Met-|-Xaa or Leu-|-Xaa.

Subunit structure

Heterodimer of a light chain and heavy chain linked by a disulfide bond.

Tissue specificity

Kidney and submandibular gland, where it is found in the granular convoluted tubule and striated duct cells. It is likely that the enzyme is mainly synthesized in the granular convoluted tubules and then transferred to other tissues by release into the vasculature or interstitial space. Ref.2

Post-translational modification

Probably N- and O-glycosylated.

Sequence similarities

Belongs to the peptidase S1 family. Kallikrein subfamily.

Contains 1 peptidase S1 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Probable
Propeptide19 – 246Activation peptide Probable
PRO_0000028013
Chain25 – 259235Glandular kallikrein-10
PRO_0000028014
Chain25 – 11187T-kininogenase light chain
PRO_0000028015
Chain112 – 259148T-kininogenase heavy chain
PRO_0000028016

Regions

Domain25 – 256232Peptidase S1

Sites

Active site631Charge relay system
Active site1181Charge relay system
Active site2111Charge relay system

Amino acid modifications

Glycosylation911N-linked (GlcNAc...) Potential
Glycosylation1061N-linked (GlcNAc...) Potential
Disulfide bond31 ↔ 171 By similarity
Disulfide bond48 ↔ 64 By similarity
Disulfide bond150 ↔ 217 By similarity
Disulfide bond182 ↔ 196 By similarity
Disulfide bond207 ↔ 232 By similarity

Experimental info

Sequence conflict441N → IET AA sequence Ref.4
Sequence conflict130 – 1312IT → DS AA sequence Ref.3
Sequence conflict1431E → G AA sequence Ref.4
Sequence conflict1481S → G AA sequence Ref.4

Sequences

Sequence LengthMass (Da)Tools
P36375 [UniParc].

Last modified June 12, 2007. Version 2.
Checksum: 18DBC31C6086E5F7

FASTA25928,981
        10         20         30         40         50         60 
MWFLILFLAL SLGGIDAAPP GQSRIVGGYK CEKNSQPWQV AIINEYLCGG VLIDPSWVIT 

        70         80         90        100        110        120 
AAHCYSNYYH VLLGRNNLFE DEPFAQYRFV NQSFPHPDYK PFLMRNHTRQ RGDDYSNDLM 

       130        140        150        160        170        180 
LLHLSEPADI TDGVKVIDLP TEEPKVGSTC LASGWGSTKP LNWELPDDLQ CVNIHLLSNE 

       190        200        210        220        230        240 
KCIEAYEQKV TDLMLCAGEM DGRKDTCKGD SGGPLICDGV LQGITSWGNV PCAEPYNPGV 

       250 
YTKLIKFTSW IKEVMKENP 

« Hide

References

« Hide 'large scale' references
[1]"Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. expand/collapse author list , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Brown Norway.
[2]"Molecular cloning and characterization of rKlk10, a cDNA encoding T-kininogenase from rat submandibular gland and kidney."
Ma J.-X., Chao J., Chao L.
Biochemistry 31:10922-10928(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 16-259, PARTIAL PROTEIN SEQUENCE, TISSUE SPECIFICITY.
Tissue: Kidney and Submandibular gland.
[3]"Characterization of serine proteinases isolated from rat submaxillary gland: with special reference to the degradation of rat kininogens by these enzymes."
Kato H., Nakanishi E., Enjyoji K., Hayashi I., Oh-Ishi S., Iwanaga S.
J. Biochem. 102:1389-1404(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-47 AND 112-132.
Tissue: Submandibular gland.
[4]"Purification and characterization of a kallikrein-like T-kininogenase."
Xiong W., Chen L.-M., Chao J.
J. Biol. Chem. 265:2822-2827(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-47 AND 112-148.
Tissue: Submandibular gland.
[5]"Microheterogeneity of rat submaxillary gland kallikrein k10, a member of the kallikrein family."
Gutman N., Elmoujahed A., Brillard M., du Sorbier B., Gauthier F.
Eur. J. Biochem. 197:425-429(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-47; 110-139 AND 194-247.
Tissue: Submandibular gland.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AABR03000574 Genomic DNA. No translation available.
S48142 mRNA. Translation: AAB24071.1.
PIRA44284.
B35545.
RefSeqNP_001128645.1. NM_001135173.1.
XP_003748896.1. XM_003748848.2.
UniGeneRn.220730.

3D structure databases

ProteinModelPortalP36375.
SMRP36375. Positions 25-259.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000048581.

Protein family/group databases

MEROPSS01.165.

Proteomic databases

PaxDbP36375.
PRIDEP36375.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000041899; ENSRNOP00000048581; ENSRNOG00000046670.
ENSRNOT00000045756; ENSRNOP00000050040; ENSRNOG00000046297.
GeneID100911689.
292858.
KEGGrno:100911689.
rno:292858.
UCSCRGD:1303242. rat.

Organism-specific databases

CTD292858.
RGD1303242. Klk10.

Phylogenomic databases

eggNOGCOG5640.
GeneTreeENSGT00750000117405.
HOGENOMHOG000251820.
HOVERGENHBG013304.
InParanoidP36375.
OMAIINEYLC.
OrthoDBEOG75B84T.
PhylomeDBP36375.
TreeFamTF331065.

Gene expression databases

GenevestigatorP36375.

Family and domain databases

InterProIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio634935.

Entry information

Entry nameKLK10_RAT
AccessionPrimary (citable) accession number: P36375
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 12, 2007
Last modified: May 14, 2014
This is version 116 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

Peptidase families

Classification of peptidase families and list of entries