Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Glandular kallikrein-10

Gene

Klk10

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei63 – 631Charge relay system
Active sitei118 – 1181Charge relay system
Active sitei211 – 2111Charge relay system

GO - Molecular functioni

  1. serine-type endopeptidase activity Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Protein family/group databases

MEROPSiS01.165.

Names & Taxonomyi

Protein namesi
Recommended name:
Glandular kallikrein-10 (EC:3.4.21.35)
Short name:
K10
Short name:
rGK-10
Alternative name(s):
Endopeptidase K
Proteinase B
T-kininogenase
Tissue kallikrein
Cleaved into the following 2 chains:
Gene namesi
Name:Klk10
Synonyms:Klk-10
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 1

Organism-specific databases

RGDi1303242. Klk10.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818CuratedAdd
BLAST
Propeptidei19 – 246Activation peptide3 PublicationsPRO_0000028013
Chaini25 – 259235Glandular kallikrein-10PRO_0000028014Add
BLAST
Chaini25 – 11187T-kininogenase light chainPRO_0000028015Add
BLAST
Chaini112 – 259148T-kininogenase heavy chainPRO_0000028016Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi31 ↔ 171PROSITE-ProRule annotation
Disulfide bondi48 ↔ 64PROSITE-ProRule annotation
Glycosylationi91 – 911N-linked (GlcNAc...)Sequence Analysis
Glycosylationi106 – 1061N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi150 ↔ 217PROSITE-ProRule annotation
Disulfide bondi182 ↔ 196PROSITE-ProRule annotation
Disulfide bondi207 ↔ 232PROSITE-ProRule annotation

Post-translational modificationi

Probably N- and O-glycosylated.

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiP36375.
PRIDEiP36375.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

GenevestigatoriP36375.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000048581.

Structurei

3D structure databases

ProteinModelPortaliP36375.
SMRiP36375. Positions 25-259.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 256232Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S1 family. Kallikrein subfamily.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG5640.
GeneTreeiENSGT00760000118862.
HOGENOMiHOG000251820.
HOVERGENiHBG013304.
InParanoidiP36375.
OMAiIINEYLC.
OrthoDBiEOG75B84T.
PhylomeDBiP36375.
TreeFamiTF331065.

Family and domain databases

InterProiIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P36375-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWFLILFLAL SLGGIDAAPP GQSRIVGGYK CEKNSQPWQV AIINEYLCGG
60 70 80 90 100
VLIDPSWVIT AAHCYSNYYH VLLGRNNLFE DEPFAQYRFV NQSFPHPDYK
110 120 130 140 150
PFLMRNHTRQ RGDDYSNDLM LLHLSEPADI TDGVKVIDLP TEEPKVGSTC
160 170 180 190 200
LASGWGSTKP LNWELPDDLQ CVNIHLLSNE KCIEAYEQKV TDLMLCAGEM
210 220 230 240 250
DGRKDTCKGD SGGPLICDGV LQGITSWGNV PCAEPYNPGV YTKLIKFTSW

IKEVMKENP
Length:259
Mass (Da):28,981
Last modified:June 12, 2007 - v2
Checksum:i18DBC31C6086E5F7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti44 – 441N → IET AA sequence (PubMed:2303430).Curated
Sequence conflicti130 – 1312IT → DS AA sequence (PubMed:3482210).Curated
Sequence conflicti143 – 1431E → G AA sequence (PubMed:2303430).Curated
Sequence conflicti148 – 1481S → G AA sequence (PubMed:2303430).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03000574 Genomic DNA. No translation available.
S48142 mRNA. Translation: AAB24071.1.
PIRiA44284.
B35545.
RefSeqiNP_001128645.1. NM_001135173.1.
XP_003748896.1. XM_003748848.3.
UniGeneiRn.220730.

Genome annotation databases

EnsembliENSRNOT00000041899; ENSRNOP00000048581; ENSRNOG00000046670.
ENSRNOT00000045756; ENSRNOP00000050040; ENSRNOG00000046297.
GeneIDi100911689.
292858.
KEGGirno:100911689.
rno:292858.
UCSCiRGD:1303242. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03000574 Genomic DNA. No translation available.
S48142 mRNA. Translation: AAB24071.1.
PIRiA44284.
B35545.
RefSeqiNP_001128645.1. NM_001135173.1.
XP_003748896.1. XM_003748848.3.
UniGeneiRn.220730.

3D structure databases

ProteinModelPortaliP36375.
SMRiP36375. Positions 25-259.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000048581.

Protein family/group databases

MEROPSiS01.165.

Proteomic databases

PaxDbiP36375.
PRIDEiP36375.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000041899; ENSRNOP00000048581; ENSRNOG00000046670.
ENSRNOT00000045756; ENSRNOP00000050040; ENSRNOG00000046297.
GeneIDi100911689.
292858.
KEGGirno:100911689.
rno:292858.
UCSCiRGD:1303242. rat.

Organism-specific databases

CTDi292858.
RGDi1303242. Klk10.

Phylogenomic databases

eggNOGiCOG5640.
GeneTreeiENSGT00760000118862.
HOGENOMiHOG000251820.
HOVERGENiHBG013304.
InParanoidiP36375.
OMAiIINEYLC.
OrthoDBiEOG75B84T.
PhylomeDBiP36375.
TreeFamiTF331065.

Miscellaneous databases

NextBioi634935.

Gene expression databases

GenevestigatoriP36375.

Family and domain databases

InterProiIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiKLK10_RAT
AccessioniPrimary (citable) accession number: P36375
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 12, 2007
Last modified: January 7, 2015
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.