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P00752 (KLK_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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

EC=3.4.21.35
Alternative name(s):
Tissue kallikrein
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length246 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.

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

Monomer.

Sequence similarities

Belongs to the peptidase S1 family. Kallikrein subfamily.

Contains 1 peptidase S1 domain.

Caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 77
PRO_0000027964
Chain8 – 246239Glandular kallikrein
PRO_0000027965

Regions

Domain8 – 243236Peptidase S1
Region85 – 10420Kallikrein (autolysis) loop

Sites

Active site481Charge relay system
Active site1031Charge relay system
Active site1981Charge relay system

Amino acid modifications

Glycosylation851N-linked (GlcNAc...) Potential
Glycosylation2391N-linked (GlcNAc...) Potential
Disulfide bond14 ↔ 158
Disulfide bond33 ↔ 49
Disulfide bond135 ↔ 204
Disulfide bond169 ↔ 183
Disulfide bond194 ↔ 219

Secondary structure

................................... 246
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00752 [UniParc].

Last modified March 27, 2002. Version 4.
Checksum: 5991CEDE406A19A1

FASTA24627,172
        10         20         30         40         50         60 
APPIQSRIIG GRECEKNSHP WQVAIYHYSS FQCGGVLVNP KWVLTAAHCK NDNYEVWLGR 

        70         80         90        100        110        120 
HNLFENENTA QFFGVTADFP HPGFNLSLLK XHTKADGKDY SHDLMLLRLQ SPAKITDAVK 

       130        140        150        160        170        180 
VLELPTQEPE LGSTCEASGW GSIEPGPDBF EFPDEIQCVQ LTLLQNTFCA BAHPBKVTES 

       190        200        210        220        230        240 
MLCAGYLPGG KDTCMGDSGG PLICNGMWQG ITSWGHTPCG SANKPSIYTK LIFYLDWIND 


TITENP 

« Hide

References

[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]"Porcine glandular kallikreins."
Fiedler F., Fink E., Tschesche H., Fritz H.
Methods Enzymol. 80:493-532(1981) [PubMed] [Europe PMC] [Abstract]
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]Erratum
Mittl P.R.E., di Marco S., Fendrich G., Pohlig G., Heim J., Sommerhoff C., Fritz H., Priestle J.P., Gruetter M.G.
Structure 5:585-585(1997)
[11]"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.

Cross-references

Sequence databases

PIRKQPG. A00938.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP00752.
SMRP00752. Positions 8-87.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP00752.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG013304.

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

EvolutionaryTraceP00752.

Entry information

Entry nameKLK_PIG
AccessionPrimary (citable) accession number: P00752
Entry history
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 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references