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P36375

- KLK10_RAT

UniProt

P36375 - KLK10_RAT

Protein

Glandular kallikrein-10

Gene

Klk10

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 2 (12 Jun 2007)
      Previous versions | rss
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    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

    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.
    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

    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:
    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

    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: October 1, 2014
    This is version 117 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