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UniProtKB/Swiss-Prot entry P00752


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name KLK_PIG
Primary accession number P00752
Secondary accession numbers None
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on March 27, 2002 (Sequence version 4)
Annotations were last modified on    September 2, 2008 (Entry version 82)
Name and origin of the protein
Protein name Glandular kallikrein [Precursor]
Synonyms EC 3.4.21.35
Tissue kallikrein
Gene name None
From
Sus scrofa (Pig) [TaxID: 9823] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae; Sus.
Protein existence 1: Evidence at protein level;
References
[1]
PROTEIN SEQUENCE OF 1-15 AND 95-102.
PubMed=3246048 [NCBI, ExPASy, EBI, Israel, Japan]
Kamada M., Aoki K., Ikekita M., Kizuki K., Moriya H., Kamo M., Tsugita A.;
"Generation of alpha- and beta-kallikreins from porcine pancreatic prokallikrein by the action of trypsin.";
Chem. Pharm. Bull. 36:4891-4899(1988).
[2]
PROTEIN SEQUENCE OF 8-87 AND 95-246.
TISSUE=Pancreas;
Tschesche H., Mair G., Godec G., Fiedler F., Ehret W., Hirschauer C., Lemon M., Fritz H., Schmidt-Kastner G., Kutzbach C.;
"The primary structure of porcine glandular kallikreins.";
Adv. Exp. Med. Biol. 120:245-260(1979).
[3]
PROTEIN SEQUENCE OF 8-87; 95-127 AND 176-246.
TISSUE=Pancreas;
Ehret W.;
"The primary structure of the kallikrein from porcine pancreas.";
Thesis (1976), University of Munich, Germany.
[4]
PROTEIN SEQUENCE OF 84-98.
PubMed=2379280 [NCBI, ExPASy, EBI, Israel, Japan]
Kamada M., Ikekita M., Kurahashi T., Aoki K., Kizuki K., Moriya H., Sweeley C.C., Kamo M., Tsugita A.;
"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.";
Chem. Pharm. Bull. 38:1053-1057(1990).
[5]
PROTEIN SEQUENCE OF 128-175.
TISSUE=Pancreas;
Ehret W.;
"Investigation of the sequence of amino acid residues 127 to 174 of the kallikrein from porcine pancreas.";
Thesis (1978), University of Munich, Germany.
[6]
REVIEW.
DOI=10.1016/S0076-6879(81)80042-0; PubMed=7043199 [NCBI, ExPASy, EBI, Israel, Japan]
Fiedler F., Fink E., Tschesche H., Fritz H.;
"Porcine glandular kallikreins.";
Methods Enzymol. 80:493-532(1981).
[7]
X-RAY CRYSTALLOGRAPHY (2 ANGSTROMS), AND SEQUENCE REVISION.
DOI=10.1016/0022-2836(83)90077-3; PubMed=6551452 [NCBI, ExPASy, EBI, Israel, Japan]
Bode W., Chen Z., Bartels K., Kutzbach C., Schmidt-Kastner G., Bartunik H.;
"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.";
J. Mol. Biol. 164:237-282(1983).
[8]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF COMPLEX WITH BOVINE PANCREATIC TRYPSIN INHIBITOR.
DOI=10.1016/0022-2836(83)90078-5; PubMed=6188842 [NCBI, ExPASy, EBI, Israel, Japan]
Chen Z., Bode W.;
"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.";
J. Mol. Biol. 164:283-311(1983).
[9]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF COMPLEX WITH HIRUSTASIN.
DOI=10.1016/S0969-2126(97)00183-4; PubMed=9032072 [NCBI, ExPASy, EBI, Israel, Japan]
Mittl P.R.E., di Marco S., Fendrich G., Pohlig G., Heim J., Sommerhoff C., Fritz H., Priestle J.P., Gruetter M.G.;
"A new structural class of serine protease inhibitors revealed by the structure of the hirustasin-kallikrein complex.";
Structure 5:253-264(1997).
[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]
STRUCTURE OF CARBOHYDRATES.
DOI=10.1021/bi00418a072; PubMed=3196708 [NCBI, ExPASy, EBI, Israel, Japan]
Tomiya N., Yamaguchi T., Awaya J., Kurono M., Endo S., Arata Y., Takahashi N., Ishihara H., Mori M., Tejima S.;
"Structural analyses of asparagine-linked oligosaccharides of porcine pancreatic kallikrein.";
Biochemistry 27:7146-7154(1988).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
PIR A00938; KQPG.
3D structure databases
PDB
1HIA; X-ray; 2.40 A; A/X=8-87, B/Y=95-246.[ExPASy / RCSB / EBI]
2KAI; X-ray; 2.50 A; A=8-87, B=95-246.[ExPASy / RCSB / EBI]
2PKA; X-ray; 2.05 A; A/X=8-87, B/Y=95-246.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1HIA; -.
2KAI; -.
2PKA; -.
SMR P00752; 8-245.
ModBase P00752.
Protein family/group databases
MEROPS S01.160; -.
Family and domain databases
InterPro IPR001254; Peptidase_S1_S6.
IPR001314; Peptidase_S1A.
Graphical view of domain structure.
Pfam PF00089; Trypsin; 1.
Pfam graphical view of domain structure.
PRINTS PR00722; CHYMOTRYPSIN.
SMART SM00020; Tryp_SPc; 1.
SMART graphical view of domain structure.
PROSITE PS50240; TRYPSIN_DOM; 1.
PS00134; TRYPSIN_HIS; 1.
PS00135; TRYPSIN_SER; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P00752.
ProtoNet P00752.
Phylogenomic databases
HOVERGEN P00752; -.
Other
LinkHub P00752; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Direct protein sequencing; Glycoprotein; Hydrolase; Protease; Serine protease; Zymogen.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
PROPEP   1     7  7      PRO_0000027964
CHAIN   8   246  239     Glandular kallikrein. PRO_0000027965
DOMAIN   8   243  236     Peptidase S1. 
REGION   85   104  20     Kallikrein (autolysis) loop. 
ACT_SITE   48    48        Charge relay system. 
ACT_SITE   103   103        Charge relay system. 
ACT_SITE   198   198        Charge relay system. 
CARBOHYD   85    85        N-linked (GlcNAc...) (Potential). 
CARBOHYD   239   239        N-linked (GlcNAc...) (Potential). 
DISULFID   14   158         
DISULFID   33    49         
DISULFID   135   204         
DISULFID   169   183         
DISULFID   194   219         
STRAND   22    27  6      
STRAND   31    39  9      
STRAND   42    45  4      
HELIX   47    49  3      
STRAND   55    59  5      
STRAND   61    65  5      
STRAND   71    80  10      
STRAND   105   109  5      
STRAND   134   137  4      
STRAND   157   164  8      
HELIX   167   172  6      
STRAND   181   185  5      
STRAND   201   204  4      
STRAND   207   212  6      
STRAND   214   218  5      
STRAND   226   230  5      
HELIX   231   234  4      
HELIX   235   244  10      
Sequence information
Length: 246 AA [This is the length of the unprocessed precursor] Molecular weight: 27172 Da [This is the MW of the unprocessed precursor] CRC64: 5991CEDE406A19A1 [This is a checksum on the sequence]
        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 

P00752 in FASTA format

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