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P00752

- KLK_PIG

UniProt

P00752 - KLK_PIG

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Protein
Glandular kallikrein
Gene
N/A
Organism
Sus scrofa (Pig)
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.

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 sitei48 – 481Charge relay system
Active sitei103 – 1031Charge relay system
Active sitei198 – 1981Charge relay system

GO - Molecular functioni

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

GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glandular kallikrein (EC:3.4.21.35)
    Alternative name(s):
    Tissue kallikrein
    OrganismiSus scrofa (Pig)
    Taxonomic identifieri9823 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
    ProteomesiUP000008227: Unplaced

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 77
    PRO_0000027964
    Chaini8 – 246239Glandular kallikrein
    PRO_0000027965Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi14 ↔ 158
    Disulfide bondi33 ↔ 49
    Glycosylationi85 – 851N-linked (GlcNAc...) Reviewed prediction
    Disulfide bondi135 ↔ 204
    Disulfide bondi169 ↔ 183
    Disulfide bondi194 ↔ 219
    Glycosylationi239 – 2391N-linked (GlcNAc...) Reviewed prediction

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    PRIDEiP00752.

    Interactioni

    Subunit structurei

    Monomer.

    Structurei

    Secondary structure

    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi22 – 276
    Beta strandi30 – 3910
    Beta strandi42 – 454
    Helixi47 – 493
    Beta strandi55 – 595
    Beta strandi61 – 655
    Beta strandi71 – 8010
    Turni82 – 854
    Beta strandi105 – 1117
    Beta strandi134 – 1418
    Beta strandi157 – 1648
    Helixi166 – 1705
    Beta strandi181 – 1855
    Beta strandi201 – 2044
    Beta strandi207 – 2126
    Beta strandi226 – 2305
    Helixi231 – 2344
    Helixi235 – 2439

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1HIAX-ray2.40A/X8-87[»]
    B/Y95-246[»]
    2KAIX-ray2.50A8-87[»]
    B95-246[»]
    2PKAX-ray2.05A/X8-87[»]
    B/Y95-246[»]
    ProteinModelPortaliP00752.
    SMRiP00752. Positions 8-87.

    Miscellaneous databases

    EvolutionaryTraceiP00752.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini8 – 243236Peptidase S1
    Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni85 – 10420Kallikrein (autolysis) loop
    Add
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    HOVERGENiHBG013304.

    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.

    P00752-1 [UniParc]FASTAAdd to Basket

    « Hide

    APPIQSRIIG GRECEKNSHP WQVAIYHYSS FQCGGVLVNP KWVLTAAHCK    50
    NDNYEVWLGR HNLFENENTA QFFGVTADFP HPGFNLSLLK XHTKADGKDY 100
    SHDLMLLRLQ SPAKITDAVK VLELPTQEPE LGSTCEASGW GSIEPGPDBF 150
    EFPDEIQCVQ LTLLQNTFCA BAHPBKVTES MLCAGYLPGG KDTCMGDSGG 200
    PLICNGMWQG ITSWGHTPCG SANKPSIYTK LIFYLDWIND TITENP 246
    Length:246
    Mass (Da):27,172
    Last modified:March 27, 2002 - v4
    Checksum:i5991CEDE406A19A1
    GO

    Sequence databases

    PIRiA00938. KQPG.

    Cross-referencesi

    Sequence databases

    PIRi A00938. KQPG.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1HIA X-ray 2.40 A/X 8-87 [» ]
    B/Y 95-246 [» ]
    2KAI X-ray 2.50 A 8-87 [» ]
    B 95-246 [» ]
    2PKA X-ray 2.05 A/X 8-87 [» ]
    B/Y 95-246 [» ]
    ProteinModelPortali P00752.
    SMRi P00752. Positions 8-87.
    ModBasei Search...

    Proteomic databases

    PRIDEi P00752.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG013304.

    Miscellaneous databases

    EvolutionaryTracei P00752.

    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. "Generation of alpha- and beta-kallikreins from porcine pancreatic prokallikrein by the action of trypsin."
      Kamada M., Aoki K., Ikekita M., Kizuki K., Moriya H., Kamo M., Tsugita A.
      Chem. Pharm. Bull. 36:4891-4899(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-15 AND 95-102.
    2. "The primary structure of porcine glandular kallikreins."
      Tschesche H., Mair G., Godec G., Fiedler F., Ehret W., Hirschauer C., Lemon M., Fritz H., Schmidt-Kastner G., Kutzbach C.
      Adv. Exp. Med. Biol. 120:245-260(1979)
      Cited for: PROTEIN SEQUENCE OF 8-87 AND 95-246.
      Tissue: Pancreas.
    3. "The primary structure of the kallikrein from porcine pancreas."
      Ehret W.
      Thesis (1976), University of Munich, Germany
      Cited for: PROTEIN SEQUENCE OF 8-87; 95-127 AND 176-246.
      Tissue: Pancreas.
    4. "Generation of a different type of beta-kallikrein from porcine pancreatic alpha-kallikrein by the action of chymotrypsin --observation of proteolytic processing occurring around 'kallikrein autolysis loop' region."
      Kamada M., Ikekita M., Kurahashi T., Aoki K., Kizuki K., Moriya H., Sweeley C.C., Kamo M., Tsugita A.
      Chem. Pharm. Bull. 38:1053-1057(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 84-98.
    5. "Investigation of the sequence of amino acid residues 127 to 174 of the kallikrein from porcine pancreas."
      Ehret W.
      Thesis (1978), University of Munich, Germany
      Cited for: PROTEIN SEQUENCE OF 128-175.
      Tissue: Pancreas.
    6. Cited for: REVIEW.
    7. "Refined 2-A X-ray crystal structure of porcine pancreatic kallikrein A, a specific trypsin-like serine proteinase. Crystallization, structure determination, crystallographic refinement, structure and its comparison with bovine trypsin."
      Bode W., Chen Z., Bartels K., Kutzbach C., Schmidt-Kastner G., Bartunik H.
      J. Mol. Biol. 164:237-282(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2 ANGSTROMS), SEQUENCE REVISION.
    8. "Refined 2.5 A X-ray crystal structure of the complex formed by porcine kallikrein A and the bovine pancreatic trypsin inhibitor. Crystallization, Patterson search, structure determination, refinement, structure and comparison with its components and with the bovine trypsin-pancreatic trypsin inhibitor complex."
      Chen Z., Bode W.
      J. Mol. Biol. 164:283-311(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF COMPLEX WITH BOVINE PANCREATIC TRYPSIN INHIBITOR.
    9. "A new structural class of serine protease inhibitors revealed by the structure of the hirustasin-kallikrein complex."
      Mittl P.R.E., di Marco S., Fendrich G., Pohlig G., Heim J., Sommerhoff C., Fritz H., Priestle J.P., Gruetter M.G.
      Structure 5:253-264(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF COMPLEX WITH HIRUSTASIN.
    10. "Structural analyses of asparagine-linked oligosaccharides of porcine pancreatic kallikrein."
      Tomiya N., Yamaguchi T., Awaya J., Kurono M., Endo S., Arata Y., Takahashi N., Ishihara H., Mori M., Tejima S.
      Biochemistry 27:7146-7154(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE OF CARBOHYDRATES.

    Entry informationi

    Entry nameiKLK_PIG
    AccessioniPrimary (citable) accession number: P00752
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: March 27, 2002
    Last modified: May 14, 2014
    This is version 107 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Caution

    Native porcine kallikrein is a monomer. Chains of the pancreatic beta-kallikrein are heterogeneous artifacts of proteolytic degradation during isolation.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

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