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P00756

- K1KB3_MOUSE

UniProt

P00756 - K1KB3_MOUSE

Protein

Kallikrein 1-related peptidase b3

Gene

Klk1b3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    Functioni

    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 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.

    Cofactori

    Binds 2 zinc ions per 7S complex. The zinc ions are bound at the alpha-gamma interfaces.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei65 – 651Charge relay system
    Active sitei120 – 1201Charge relay system
    Active sitei213 – 2131Charge relay system
    Metal bindingi231 – 2311Zinc
    Metal bindingi236 – 2361Zinc

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. receptor signaling protein activity Source: MGI
    3. serine-type endopeptidase activity Source: InterPro

    GO - Biological processi

    1. intracellular signal transduction Source: GOC

    Keywords - Molecular functioni

    Growth factor, Hydrolase, Protease, Serine protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BRENDAi3.4.21.77. 3474.
    ReactomeiREACT_199000. Activation of Matrix Metalloproteinases.

    Protein family/group databases

    MEROPSiS01.170.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Kallikrein 1-related peptidase b3 (EC:3.4.21.35)
    Alternative name(s):
    7S nerve growth factor gamma chain
    Gamma-NGF
    Glandular kallikrein K3
    Short name:
    mGK-3
    Tissue kallikrein-3
    Cleaved into the following 2 chains:
    Gene namesi
    Name:Klk1b3
    Synonyms:Klk-3, Klk3, Ngfg
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:97322. Klk1b3.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818CuratedAdd
    BLAST
    Propeptidei19 – 246Activation peptide1 PublicationPRO_0000027968
    Chaini25 – 261237Kallikrein 1-related peptidase b3PRO_0000027969Add
    BLAST
    Chaini25 – 10783Nerve growth factor gamma chain 1PRO_0000027970Add
    BLAST
    Chaini112 – 261150Nerve growth factor gamma chain 2PRO_0000027971Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi31 ↔ 173
    Disulfide bondi50 ↔ 66
    Glycosylationi102 – 1021N-linked (GlcNAc...)1 Publication
    Disulfide bondi152 ↔ 219
    Disulfide bondi184 ↔ 198
    Disulfide bondi209 ↔ 234

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    MaxQBiP00756.
    PaxDbiP00756.
    PRIDEiP00756.

    Expressioni

    Gene expression databases

    ArrayExpressiP00756.
    BgeeiP00756.
    CleanExiMM_KLK1B3.
    GenevestigatoriP00756.

    Interactioni

    Subunit structurei

    7S nerve growth factor is composed of two alpha chains, a beta dimer composed of identical chains, and two gamma chains.

    Structurei

    Secondary structure

    1
    261
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi33 – 353
    Beta strandi39 – 446
    Beta strandi47 – 5610
    Beta strandi59 – 624
    Helixi64 – 663
    Beta strandi72 – 765
    Beta strandi88 – 9710
    Helixi103 – 1053
    Beta strandi122 – 1287
    Beta strandi133 – 1353
    Beta strandi151 – 16414
    Beta strandi172 – 1798
    Helixi181 – 1877
    Beta strandi196 – 2005
    Beta strandi202 – 2054
    Beta strandi216 – 2194
    Beta strandi222 – 2298
    Beta strandi241 – 2455
    Helixi246 – 2494
    Helixi250 – 2589

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1SGFX-ray3.15G/Z25-261[»]
    ProteinModelPortaliP00756.
    SMRiP00756. Positions 25-261.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00756.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini25 – 258234Peptidase S1PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni25 – 10783Segment B1Add
    BLAST
    Regioni112 – 261150Segment AAdd
    BLAST
    Regioni112 – 16453Segment CAdd
    BLAST
    Regioni165 – 26197Segment B2Add
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG5640.
    GeneTreeiENSGT00750000117405.
    HOGENOMiHOG000251820.
    HOVERGENiHBG013304.
    InParanoidiA2RTW1.
    KOiK01325.
    OMAiNDECDKA.
    OrthoDBiEOG75B84T.
    PhylomeDBiP00756.
    TreeFamiTF331065.

    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.

    P00756-1 [UniParc]FASTAAdd to Basket

    « Hide

    MWFLILFLAL SLGGIDAAPP VQSRIVGGFK CEKNSQPWHV AVYRYTQYLC    50
    GGVLLDPNWV LTAAHCYDDN YKVWLGKNNL FKDEPSAQHR FVSKAIPHPG 100
    FNMSLMRKHI RFLEYDYSND LMLLRLSKPA DITDTVKPIT LPTEEPKLGS 150
    TCLASGWGSI TPTKFQFTDD LYCVNLKLLP NEDCAKAHIE KVTDAMLCAG 200
    EMDGGKDTCK GDSGGPLICD GVLQGITSWG HTPCGEPDMP GVYTKLNKFT 250
    SWIKDTMAKN P 261
    Length:261
    Mass (Da):28,998
    Last modified:July 21, 1986 - v1
    Checksum:i4870748E174AF7C8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti108 – 1114Missing(PubMed:3848399)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X01389 mRNA. Translation: CAA25645.1.
    X01798 Genomic DNA. Translation: CAA25928.1.
    X01799 Genomic DNA. Translation: CAA25930.1.
    BC132657 mRNA. Translation: AAI32658.1.
    BC132659 mRNA. Translation: AAI32660.1.
    CCDSiCCDS21199.1.
    PIRiA91005. NGMSG.
    RefSeqiNP_032719.1. NM_008693.2.
    UniGeneiMm.439740.

    Genome annotation databases

    EnsembliENSMUST00000085450; ENSMUSP00000082577; ENSMUSG00000066515.
    GeneIDi18050.
    KEGGimmu:18050.
    UCSCiuc009gol.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X01389 mRNA. Translation: CAA25645.1 .
    X01798 Genomic DNA. Translation: CAA25928.1 .
    X01799 Genomic DNA. Translation: CAA25930.1 .
    BC132657 mRNA. Translation: AAI32658.1 .
    BC132659 mRNA. Translation: AAI32660.1 .
    CCDSi CCDS21199.1.
    PIRi A91005. NGMSG.
    RefSeqi NP_032719.1. NM_008693.2.
    UniGenei Mm.439740.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1SGF X-ray 3.15 G/Z 25-261 [» ]
    ProteinModelPortali P00756.
    SMRi P00756. Positions 25-261.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi S01.170.

    Proteomic databases

    MaxQBi P00756.
    PaxDbi P00756.
    PRIDEi P00756.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000085450 ; ENSMUSP00000082577 ; ENSMUSG00000066515 .
    GeneIDi 18050.
    KEGGi mmu:18050.
    UCSCi uc009gol.2. mouse.

    Organism-specific databases

    CTDi 18050.
    MGIi MGI:97322. Klk1b3.

    Phylogenomic databases

    eggNOGi COG5640.
    GeneTreei ENSGT00750000117405.
    HOGENOMi HOG000251820.
    HOVERGENi HBG013304.
    InParanoidi A2RTW1.
    KOi K01325.
    OMAi NDECDKA.
    OrthoDBi EOG75B84T.
    PhylomeDBi P00756.
    TreeFami TF331065.

    Enzyme and pathway databases

    BRENDAi 3.4.21.77. 3474.
    Reactomei REACT_199000. Activation of Matrix Metalloproteinases.

    Miscellaneous databases

    EvolutionaryTracei P00756.
    NextBioi 293179.
    PROi P00756.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P00756.
    Bgeei P00756.
    CleanExi MM_KLK1B3.
    Genevestigatori P00756.

    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. "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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    4. "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] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 25-261.
      Tissue: Submandibular gland.
    5. "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] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) OF 7S COMPLEX.
      Strain: Swiss Webster.
      Tissue: Submandibular gland.

    Entry informationi

    Entry nameiK1KB3_MOUSE
    AccessioniPrimary (citable) accession number: P00756
    Secondary accession number(s): A2RTW1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 142 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    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.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. Peptidase families
      Classification of peptidase families and list of entries
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3