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P36375

- KLK10_RAT

UniProt

P36375 - KLK10_RAT

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Protein

Glandular kallikrein-10

Gene
Klk10, Klk-10
Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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 – 1818 InferredAdd
BLAST
Propeptidei19 – 246Activation peptide InferredPRO_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 ↔ 171 By similarity
Disulfide bondi48 ↔ 64 By similarity
Glycosylationi91 – 911N-linked (GlcNAc...) Reviewed prediction
Glycosylationi106 – 1061N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi150 ↔ 217 By similarity
Disulfide bondi182 ↔ 196 By similarity
Disulfide bondi207 ↔ 232 By similarity

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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 256232Peptidase S1Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG5640.
GeneTreeiENSGT00750000117405.
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

MWFLILFLAL SLGGIDAAPP GQSRIVGGYK CEKNSQPWQV AIINEYLCGG    50
VLIDPSWVIT AAHCYSNYYH VLLGRNNLFE DEPFAQYRFV NQSFPHPDYK 100
PFLMRNHTRQ RGDDYSNDLM LLHLSEPADI TDGVKVIDLP TEEPKVGSTC 150
LASGWGSTKP LNWELPDDLQ CVNIHLLSNE KCIEAYEQKV TDLMLCAGEM 200
DGRKDTCKGD SGGPLICDGV LQGITSWGNV PCAEPYNPGV YTKLIKFTSW 250
IKEVMKENP 259
Length:259
Mass (Da):28,981
Last modified:June 12, 2007 - v2
Checksum:i18DBC31C6086E5F7
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti44 – 441N → IET AA sequence 1 Publication
Sequence conflicti130 – 1312IT → DS AA sequence 1 Publication
Sequence conflicti143 – 1431E → G AA sequence 1 Publication
Sequence conflicti148 – 1481S → G AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_003748848.2.
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:
EMBL
GenBank
DDBJ
Links Updated
AABR03000574 Genomic DNA. No translation available.
S48142 mRNA. Translation: AAB24071.1 .
PIRi A44284.
B35545.
RefSeqi NP_001128645.1. NM_001135173.1.
XP_003748896.1. XM_003748848.2.
UniGenei Rn.220730.

3D structure databases

ProteinModelPortali P36375.
SMRi P36375. Positions 25-259.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000048581.

Protein family/group databases

MEROPSi S01.165.

Proteomic databases

PaxDbi P36375.
PRIDEi P36375.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000041899 ; ENSRNOP00000048581 ; ENSRNOG00000046670 .
ENSRNOT00000045756 ; ENSRNOP00000050040 ; ENSRNOG00000046297 .
GeneIDi 100911689.
292858.
KEGGi rno:100911689.
rno:292858.
UCSCi RGD:1303242. rat.

Organism-specific databases

CTDi 292858.
RGDi 1303242. Klk10.

Phylogenomic databases

eggNOGi COG5640.
GeneTreei ENSGT00750000117405.
HOGENOMi HOG000251820.
HOVERGENi HBG013304.
InParanoidi P36375.
OMAi IINEYLC.
OrthoDBi EOG75B84T.
PhylomeDBi P36375.
TreeFami TF331065.

Miscellaneous databases

NextBioi 634935.

Gene expression databases

Genevestigatori P36375.

Family and domain databases

InterProi IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view ]
Pfami PF00089. Trypsin. 1 hit.
[Graphical view ]
PRINTSi PR00722. CHYMOTRYPSIN.
SMARTi SM00020. Tryp_SPc. 1 hit.
[Graphical view ]
SUPFAMi SSF50494. SSF50494. 1 hit.
PROSITEi PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: May 14, 2014
This is version 116 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

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