P00752 (KLK_PIG) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Glandular kallikrein EC=3.4.21.35 Alternative name(s): Tissue kallikrein
Organism	Sus scrofa (Pig) [Complete proteome]
Taxonomic identifier	9823 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length	246 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Molecular function	Hydrolase Protease Serine protease
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Propeptide

1 – 7

7

PRO_0000027964

Chain

8 – 246

239

Glandular kallikrein

PRO_0000027965

Regions

Domain

8 – 243

236

Peptidase S1

Region

85 – 104

20

Kallikrein (autolysis) loop

Sites

Active site

48

1

Charge relay system

Active site

103

1

Charge relay system

Active site

198

1

Charge relay system

Amino acid modifications

Glycosylation

85

1

N-linked (GlcNAc...) Potential

Glycosylation

239

1

N-linked (GlcNAc...) Potential

Disulfide bond

14 ↔ 158

Disulfide bond

33 ↔ 49

Disulfide bond

135 ↔ 204

Disulfide bond

169 ↔ 183

Disulfide bond

194 ↔ 219

Secondary structure

1

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246

Helix Strand Turn

Details...

Beta strand

22 – 27

6

Beta strand

31 – 39

9

Beta strand

42 – 45

4

Helix

47 – 49

3

Beta strand

55 – 59

5

Beta strand

61 – 65

5

Beta strand

71 – 80

10

Beta strand

105 – 109

5

Beta strand

134 – 137

4

Beta strand

157 – 164

8

Helix

167 – 172

6

Beta strand

181 – 185

5

Beta strand

201 – 204

4

Beta strand

207 – 212

6

Beta strand

214 – 218

5

Beta strand

226 – 230

5

Helix

231 – 234

4

Helix

235 – 244

10

Sequences

	Sequence		Length	Mass (Da)
	P00752 [UniParc]. Last modified March 27, 2002. Version 4. Checksum: 5991CEDE406A19A1	FASTA	246	27,172
	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

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: 3246048] [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: 2379280] [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: 7043199] [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: 6551452] [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: 6188842] [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: 9032072] [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: 3196708] [Abstract] Cited for: STRUCTURE OF CARBOHYDRATES.
+	Additional computationally mapped references.

Cross-references

Sequence databases

PIR

KQPG. A00938.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P00752.

SMR

P00752. Positions 8-87.

ModBase

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Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Phylogenomic databases

HOVERGEN

HBG013304.

Family and domain databases

InterPro

IPR009003. Pept_cys/ser_Trypsin-like.
IPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
[Graphical view]

Pfam

PF00089. Trypsin. 1 hit.
[Graphical view]

PRINTS

PR00722. CHYMOTRYPSIN.

SMART

SM00020. Tryp_SPc. 1 hit.
[Graphical view]

SUPFAM

SSF50494. Pept_Ser_Cys. 1 hit.

PROSITE

PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

ProtoNet

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Entry information

Entry name

KLK_PIG

Accession

Primary (citable) accession number: P00752

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	March 27, 2002
Last modified:	November 16, 2011
This is version 95 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program