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P15948 (K1B22_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 114. 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:
Kallikrein 1-related peptidase b22

EC=3.4.21.35
Alternative name(s):
Beta-NGF-endopeptidase
Epidermal growth factor-binding protein type A
Short name=EGF-BP A
Glandular kallikrein K22
Short name=mGK-22
Nerve growth factor beta chain endopeptidase
Tissue kallikrein 22
Gene names
Name:Klk1b22
Synonyms:Klk-22, Klk22
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length259 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.

Sequence similarities

Belongs to the peptidase S1 family. Kallikrein subfamily.

Contains 1 peptidase S1 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717
Propeptide18 – 247Activation peptide
PRO_0000027989
Chain25 – 259235Kallikrein 1-related peptidase b22
PRO_0000027990

Regions

Domain25 – 256232Peptidase S1

Sites

Active site651Charge relay system
Active site1181Charge relay system
Active site2111Charge relay system

Amino acid modifications

Glycosylation1021N-linked (GlcNAc...) Probable
Disulfide bond31 ↔ 171 By similarity
Disulfide bond50 ↔ 66 By similarity
Disulfide bond150 ↔ 217 By similarity
Disulfide bond182 ↔ 196 By similarity
Disulfide bond207 ↔ 232 By similarity

Sequences

Sequence LengthMass (Da)Tools
P15948 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: D7745794D8A87B9C

FASTA25928,384
        10         20         30         40         50         60 
MRFLILFLTL SLGGIDAAPP VQSRILGGFK CEKNSQPWQV AVYYLDEYLC GGVLLDRNWV 

        70         80         90        100        110        120 
LTAAHCYEDK YNIWLGKNKL FQDEPSAQHR LVSKSFPHPD FNMSLLQSVP TGADLSNDLM 

       130        140        150        160        170        180 
LLRLSKPADI TDVVKPIDLP TTEPKLGSTC LASGWGSINQ LIYQNPNDLQ CVSIKLHPNE 

       190        200        210        220        230        240 
VCVKAHILKV TDVMLCAGEM NGGKDTCKGD SGGPLICDGV LQGITSWGST PCGEPNAPAI 

       250 
YTKLIKFTSW IKDTMAKNP 

« Hide

References

[1]"Mouse glandular kallikrein genes: identification and characterization of the genes encoding the epidermal growth factor binding proteins."
Drinkwater C.C., Evans B.A., Richards R.I.
Biochemistry 26:6750-6756(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: BALB/c.
Tissue: Salivary gland.
[2]"Beta-NGF-endopeptidase: structure and activity of a kallikrein encoded by the gene mGK-22."
Fahnestock M., Woo J.E., Lopez G.A., Snow J., Walz D.A., Arici M.J., Mobley W.C.
Biochemistry 30:3443-3450(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-54.
[3]"mGK-6-derived true tissue kallikrein is synthesized, processed, and targeted through a regulated secretory pathway in mouse pituitary AtT-20 cells."
Peters J., Takahashi S., Tada M., Miyake Y.
J. Biochem. 111:643-648(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-41.
Tissue: Submandibular gland.
[4]"Mouse glandular kallikrein genes. Structure and partial sequence analysis of the kallikrein gene locus."
Evans B.A., Drinkwater C.C., Richards R.I.
J. Biol. Chem. 262:8027-8034(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 17-54 AND 70-120.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M17979, M17977, M17978 Genomic DNA. Translation: AAA37682.1. Sequence problems.
M18598 Genomic DNA. Translation: AAA39361.1.
M18618 Genomic DNA. Translation: AAA39362.1.
CCDSCCDS21196.1.
PIRA29746.
RefSeqNP_034244.1. NM_010114.1.
UniGeneMm.5193.

3D structure databases

ProteinModelPortalP15948.
SMRP15948. Positions 25-259.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000076733.

Protein family/group databases

MEROPSS01.039.

Proteomic databases

MaxQBP15948.
PaxDbP15948.
PRIDEP15948.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000077528; ENSMUSP00000076733; ENSMUSG00000060177.
GeneID13646.
KEGGmmu:13646.
UCSCuc009goi.1. mouse.

Organism-specific databases

CTD13646.
MGIMGI:95291. Klk1b22.

Phylogenomic databases

eggNOGCOG5640.
HOGENOMHOG000251820.
HOVERGENHBG013304.
InParanoidP15948.
KOK01325.
OMACVNINIL.
OrthoDBEOG75B84T.
PhylomeDBP15948.
TreeFamTF331065.

Gene expression databases

BgeeP15948.
CleanExMM_KLK1B22.
GenevestigatorP15948.

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

NextBio284362.
PROP15948.
SOURCESearch...

Entry information

Entry nameK1B22_MOUSE
AccessionPrimary (citable) accession number: P15948
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: July 9, 2014
This is version 114 of the entry and version 1 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot