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P36368 (EGFB2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
Epidermal growth factor-binding protein type B

Short name=EGF-BP B
EC=3.4.21.119
Alternative name(s):
Glandular kallikrein K13
Short name=mGK-13
Prorenin-converting enzyme 1
Short name=PRECE-1
Tissue kallikrein 13
Gene names
Name:Egfbp2
Synonyms:Egfbp-2, Klk-13, Klk13
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length261 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cleaves REN2 at a dibasic site to yield mature renin.

Catalytic activity

Hydrolyzes mouse Ren2 protein (a species of prorenin present in the submandibular gland) on the carboxy side of the arginine residue at the Lys-Arg-|- pair in the N-terminus, to yield mature renin.

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 – 1818 Probable
Propeptide19 – 246Activation peptide
PRO_0000027983
Chain25 – 261237Epidermal growth factor-binding protein type B
PRO_0000027984

Regions

Domain25 – 258234Peptidase S1

Sites

Active site651Charge relay system
Active site1201Charge relay system
Active site2131Charge relay system

Amino acid modifications

Glycosylation1021N-linked (GlcNAc...)
Disulfide bond31 ↔ 173
Disulfide bond50 ↔ 66
Disulfide bond152 ↔ 219
Disulfide bond184 ↔ 198
Disulfide bond209 ↔ 234

Experimental info

Sequence conflict1191N → D Ref.1

Secondary structure

.................................... 261
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P36368 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: C2854D057877F602

FASTA26128,689
        10         20         30         40         50         60 
MWFLILFLAL SLGGIDAAPP LQSRVVGGFN CKKNSQPWQV AVYYQKEHIC GGVLLDRNWV 

        70         80         90        100        110        120 
LTAAHCYVDQ YEVWLGKNKL FQEEPSAQHR LVSKSFPHPG FNMSLLMLQT IPPGADFSND 

       130        140        150        160        170        180 
LMLLRLSKPA DITDVVKPIA LPTKEPKPGS KCLASGWGSI TPTRWQKPDD LQCVFITLLP 

       190        200        210        220        230        240 
NENCAKVYLQ KVTDVMLCAG EMGGGKDTCR DDSGGPLICD GILQGTTSYG PVPCGKPGVP 

       250        260 
AIYTNLIKFN SWIKDTMMKN A 

« 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]"Mouse submandibular gland prorenin-converting enzyme is a member of glandular kallikrein family."
Kim W.S., Nakayama K., Nakagawa T., Kawamura Y., Haraguchi K., Murakami K.
J. Biol. Chem. 266:19283-19287(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: ICR.
Tissue: Submandibular gland.
[3]"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: PROTEIN SEQUENCE OF 16-54, NUCLEOTIDE SEQUENCE OF 70-122.
[4]"The crystal structure of the mouse glandular kallikrein-13 (prorenin converting enzyme)."
Timm D.E.
Protein Sci. 6:1418-1425(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M17982, M17980, M17981 Genomic DNA. Translation: AAA37680.1.
X58628 mRNA. Translation: CAA41482.1.
M18612 Genomic DNA. Translation: AAA39354.1.
PIRA41020.
RefSeqNP_034245.3. NM_010115.6.
UniGeneMm.439663.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AO5X-ray2.60A/B25-261[»]
ProteinModelPortalP36368.
SMRP36368. Positions 25-261.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteP36368.

Proteomic databases

PaxDbP36368.
PRIDEP36368.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID13647.
KEGGmmu:13647.

Organism-specific databases

CTD13647.
MGIMGI:95292. Egfbp2.

Phylogenomic databases

eggNOGCOG5640.
HOGENOMHOG000251820.
HOVERGENHBG013304.
InParanoidP36368.
KOK09462.
PhylomeDBP36368.

Enzyme and pathway databases

BRENDA3.4.21.119. 3474.

Gene expression databases

GenevestigatorP36368.

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.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP36368.
NextBio290219.
PROP36368.
SOURCESearch...

Entry information

Entry nameEGFB2_MOUSE
AccessionPrimary (citable) accession number: P36368
Secondary accession number(s): P00754
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: June 1, 1994
Last modified: July 9, 2014
This is version 116 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

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