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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...

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 – 772 PublicationsPRO_0000027964
Chaini8 – 246239Glandular kallikreinPRO_0000027965Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PRIDEiP00752.

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1
246
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00752.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini8 – 243236Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Region

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

Sequence similaritiesi

Belongs to the peptidase S1 family. Kallikrein subfamily.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

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

        10         20         30         40         50
APPIQSRIIG GRECEKNSHP WQVAIYHYSS FQCGGVLVNP KWVLTAAHCK
60 70 80 90 100
NDNYEVWLGR HNLFENENTA QFFGVTADFP HPGFNLSLLK XHTKADGKDY
110 120 130 140 150
SHDLMLLRLQ SPAKITDAVK VLELPTQEPE LGSTCEASGW GSIEPGPDBF
160 170 180 190 200
EFPDEIQCVQ LTLLQNTFCA BAHPBKVTES MLCAGYLPGG KDTCMGDSGG
210 220 230 240
PLICNGMWQG ITSWGHTPCG SANKPSIYTK LIFYLDWIND TITENP
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...
MobiDBi 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: October 1, 2014
This is version 108 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.Curated

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