Kallikrein 1-related peptidase b3 precursor

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Reviewed, UniProtKB/Swiss-Prot P00756 (K1KB3_MOUSE)

Last modified June 16, 2009. Version 98. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Kallikrein 1-related peptidase b3
    EC=3.4.21.35
Alternative name(s):
    Glandular kallikrein K3
      Short name=mGK-3
    Tissue kallikrein-3
    7S nerve growth factor gamma chain
    Gamma-NGF
Cleaved into the following 2 chains:
    1- Recommended name:
            Nerve growth factor gamma chain 1
    2- Recommended name:
            Nerve growth factor gamma chain 2

Gene names

Name:	Klk1b3
Synonyms:	Klk-3, Klk3, Ngfg

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length	261 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	7S NGF alpha chain stabilizes the 7S complex. The beta dimer promotes neurite growth. The gamma chain is an arginine-specific protease; it may also have plasminogen activator activity, as well as mitogenic activity for chick embryo fibroblasts.
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.
Cofactor	Binds 2 zinc ions per 7S complex. The zinc ions are bound at the alpha-gamma interfaces.
Subunit structure	7S nerve growth factor is composed of two alpha chains, a beta dimer composed of identical chains, and two gamma chains.
Miscellaneous	This precursor is cleaved into segments to produce the active form of the gamma chain, which occurs naturally as combinations of either two or three segments held together by disulfide bonds: B1 and A, or B1, C and B2.
Sequence similarities	Belongs to the peptidase S1 family. Kallikrein subfamily. Contains 1 peptidase S1 domain.

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Ontologies

Keywords
Domain	Signal
Ligand	Metal-binding Zinc
Molecular function	Growth factor Hydrolase Protease Serine protease
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro
Molecular function	growth factor activity Inferred from electronic annotation. Source: UniProtKB-KW receptor signaling protein activity Inferred from direct assay. Source: MGI serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 18

Probable

Propeptide

19 – 24

Activation peptide Ref.3

PRO_0000027968

Chain

25 – 261

237

Kallikrein 1-related peptidase b3

PRO_0000027969

Chain

25 – 107

Nerve growth factor gamma chain 1

PRO_0000027970

Chain

112 – 261

150

Nerve growth factor gamma chain 2

PRO_0000027971

Regions

Domain

25 – 258

234

Peptidase S1

Region

25 – 107

Segment B1

Region

112 – 261

150

Segment A

Region

112 – 164

Segment C

Region

165 – 261

Segment B2

Sites

Active site

Charge relay system

Active site

120

Charge relay system

Active site

213

Charge relay system

Metal binding

231

Zinc

Metal binding

236

Zinc

Amino acid modifications

Glycosylation

102

N-linked (GlcNAc...) Ref.3

Disulfide bond

Disulfide bond

Disulfide bond

Disulfide bond

Disulfide bond

Experimental info

Sequence conflict

108 – 111

Missing Ref.2

Secondary structure

261

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P00756-1 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 4870748E174AF7C8
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FASTA

261

28,998

        10         20         30         40         50         60 
MWFLILFLAL SLGGIDAAPP VQSRIVGGFK CEKNSQPWHV AVYRYTQYLC GGVLLDPNWV 

        70         80         90        100        110        120 
LTAAHCYDDN YKVWLGKNNL FKDEPSAQHR FVSKAIPHPG FNMSLMRKHI RFLEYDYSND 

       130        140        150        160        170        180 
LMLLRLSKPA DITDTVKPIT LPTEEPKLGS TCLASGWGSI TPTKFQFTDD LYCVNLKLLP 

       190        200        210        220        230        240 
NEDCAKAHIE KVTDAMLCAG EMDGGKDTCK GDSGGPLICD GVLQGITSWG HTPCGEPDMP 

       250        260 
GVYTKLNKFT SWIKDTMAKN P

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References

[1]	"Isolation of a cDNA clone coding for the gamma-subunit of mouse nerve growth factor using a high-stringency selection procedure." Ullrich A., Gray A., Wood W.I., Hayflick J., Seeburg P.H. DNA 3:387-392(1984) [PubMed: 6548955] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Genes for the alpha and gamma subunits of mouse nerve growth factor are contiguous." Evans B.A., Richards R.I. EMBO J. 4:133-138(1985) [PubMed: 3848399] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The amino acid sequence of the gamma-subunit of mouse submaxillary gland 7 S nerve growth factor." Thomas K.A., Baglan N.C., Bradshaw R.A. J. Biol. Chem. 256:9156-9166(1981) [PubMed: 7263706] [Abstract] Cited for: PROTEIN SEQUENCE OF 25-261. Tissue: Submandibular gland.
[4]	"Structure of mouse 7S NGF: a complex of nerve growth factor with four binding proteins." Bax B., Blundell T.L., Murray-Rust J., McDonald N.Q. Structure 5:1275-1285(1997) [PubMed: 9351801] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) OF 7S COMPLEX. Strain: Swiss Webster. Tissue: Submandibular gland.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

X01389 mRNA. Translation: CAA25645.1.
X01798 Genomic DNA. Translation: CAA25928.1.
X01799 Genomic DNA. Translation: CAA25930.1.

IPI

IPI00134582.

PIR

NGMSG. A91005.

RefSeq

NP_032719.1.

UniGene

Mm.439740

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1SGF	X-ray	3.15	G/Z	25-261	[»]

ModBase

Search...

Protein family/group databases

MEROPS

S01.170.

Genome annotation databases

Ensembl

ENSMUSG00000066515. Mus musculus. [Contig view]

GeneID

18050.

KEGG

mmu:18050.

Organism-specific databases

MGI

MGI:97322. Klk1b3.

Phylogenomic databases

HOVERGEN

P00756.

OMA

P00756. YEDEPFA.

Enzyme and pathway databases

BRENDA

3.4.21.35. 244.
3.4.21.77. 244.

Gene expression databases

ArrayExpress

P00756.

Bgee

P00756.

CleanEx

MM_KLK1B3.

GermOnline

ENSMUSG00000066515. Mus musculus.

Family and domain databases

InterPro

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]

PROSITE

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

ProtoNet

Search...

Other Resources

NextBio

293179.

SOURCE

Search...

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Entry information

Entry name

K1KB3_MOUSE

Accession

Primary (citable) accession number: P00756

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	June 16, 2009
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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