K1KB3_MOUSE
ID K1KB3_MOUSE Reviewed; 261 AA.
AC P00756; A2RTW1;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Kallikrein 1-related peptidase b3;
DE EC=3.4.21.35;
DE AltName: Full=7S nerve growth factor gamma chain;
DE AltName: Full=Gamma-NGF;
DE AltName: Full=Glandular kallikrein K3;
DE Short=mGK-3;
DE AltName: Full=Tissue kallikrein-3;
DE Contains:
DE RecName: Full=Nerve growth factor gamma chain 1;
DE Contains:
DE RecName: Full=Nerve growth factor gamma chain 2;
DE Flags: Precursor;
GN Name=Klk1b3; Synonyms=Klk-3, Klk3, Ngfg;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6548955; DOI=10.1089/dna.1984.3.387;
RA Ullrich A., Gray A., Wood W.I., Hayflick J., Seeburg P.H.;
RT "Isolation of a cDNA clone coding for the gamma-subunit of mouse nerve
RT growth factor using a high-stringency selection procedure.";
RL DNA 3:387-392(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3848399; DOI=10.1002/j.1460-2075.1985.tb02327.x;
RA Evans B.A., Richards R.I.;
RT "Genes for the alpha and gamma subunits of mouse nerve growth factor are
RT contiguous.";
RL EMBO J. 4:133-138(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 25-261.
RC TISSUE=Submandibular gland;
RX PubMed=7263706; DOI=10.1016/s0021-9258(19)52522-4;
RA Thomas K.A., Baglan N.C., Bradshaw R.A.;
RT "The amino acid sequence of the gamma-subunit of mouse submaxillary gland 7
RT S nerve growth factor.";
RL J. Biol. Chem. 256:9156-9166(1981).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) OF 7S COMPLEX.
RC STRAIN=Swiss Webster; TISSUE=Submandibular gland;
RX PubMed=9351801; DOI=10.1016/s0969-2126(97)00280-3;
RA Bax B., Blundell T.L., Murray-Rust J., McDonald N.Q.;
RT "Structure of mouse 7S NGF: a complex of nerve growth factor with four
RT binding proteins.";
RL Structure 5:1275-1285(1997).
CC -!- FUNCTION: 7S NGF alpha chain stabilizes the 7S complex. The beta dimer
CC promotes neurite growth. The gamma chain is an arginine-specific
CC protease; it may also have plasminogen activator activity, as well as
CC mitogenic activity for chick embryo fibroblasts.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage of Arg-|-Xaa bonds in small molecule
CC substrates. Highly selective action to release kallidin (lysyl-
CC bradykinin) from kininogen involves hydrolysis of Met-|-Xaa or Leu-|-
CC Xaa.; EC=3.4.21.35;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 2 Zn(2+) ions per 7S complex. The Zn(2+) ions are bound at
CC the alpha-gamma interfaces.;
CC -!- SUBUNIT: 7S nerve growth factor is composed of two alpha chains, a beta
CC dimer composed of identical chains, and two gamma chains.
CC -!- MISCELLANEOUS: This precursor is cleaved into segments to produce the
CC active form of the gamma chain, which occurs naturally as combinations
CC of either two or three segments held together by disulfide bonds: B1
CC and A, or B1, C and B2.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Kallikrein subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; X01389; CAA25645.1; -; mRNA.
DR EMBL; X01798; CAA25928.1; -; Genomic_DNA.
DR EMBL; X01799; CAA25930.1; -; Genomic_DNA.
DR EMBL; BC132657; AAI32658.1; -; mRNA.
DR EMBL; BC132659; AAI32660.1; -; mRNA.
DR CCDS; CCDS21199.1; -.
DR PIR; A91005; NGMSG.
DR RefSeq; NP_032719.1; NM_008693.2.
DR PDB; 1SGF; X-ray; 3.15 A; G/Z=25-261.
DR PDBsum; 1SGF; -.
DR AlphaFoldDB; P00756; -.
DR SMR; P00756; -.
DR STRING; 10090.ENSMUSP00000082577; -.
DR MEROPS; S01.170; -.
DR TCDB; 8.A.131.1.5; the transmembrane protease serine 3 (tmprss3) family.
DR GlyGen; P00756; 2 sites.
DR iPTMnet; P00756; -.
DR MaxQB; P00756; -.
DR PaxDb; P00756; -.
DR PeptideAtlas; P00756; -.
DR PRIDE; P00756; -.
DR ProteomicsDB; 269166; -.
DR DNASU; 18050; -.
DR Ensembl; ENSMUST00000085450; ENSMUSP00000082577; ENSMUSG00000066515.
DR GeneID; 18050; -.
DR KEGG; mmu:18050; -.
DR UCSC; uc009gol.2; mouse.
DR CTD; 18050; -.
DR MGI; MGI:97322; Klk1b3.
DR VEuPathDB; HostDB:ENSMUSG00000066515; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT01020000230389; -.
DR HOGENOM; CLU_006842_1_1_1; -.
DR InParanoid; P00756; -.
DR OMA; WQVALYH; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; P00756; -.
DR TreeFam; TF331065; -.
DR BRENDA; 3.4.21.77; 3474.
DR Reactome; R-MMU-1592389; Activation of Matrix Metalloproteinases.
DR BioGRID-ORCS; 18050; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Klk1b3; mouse.
DR EvolutionaryTrace; P00756; -.
DR PRO; PR:P00756; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P00756; protein.
DR Bgee; ENSMUSG00000066515; Expressed in spermatid and 23 other tissues.
DR ExpressionAtlas; P00756; baseline and differential.
DR Genevisible; P00756; MM.
DR GO; GO:0001669; C:acrosomal vesicle; ISO:MGI.
DR GO; GO:0045177; C:apical part of cell; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0030141; C:secretory granule; IBA:GO_Central.
DR GO; GO:0004175; F:endopeptidase activity; ISO:MGI.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISO:MGI.
DR GO; GO:0008236; F:serine-type peptidase activity; ISO:MGI.
DR GO; GO:0003073; P:regulation of systemic arterial blood pressure; IBA:GO_Central.
DR GO; GO:0031638; P:zymogen activation; IBA:GO_Central.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Growth factor; Hydrolase; Metal-binding; Protease; Reference proteome;
KW Serine protease; Signal; Zinc; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000305"
FT PROPEP 19..24
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:7263706"
FT /id="PRO_0000027968"
FT CHAIN 25..261
FT /note="Kallikrein 1-related peptidase b3"
FT /id="PRO_0000027969"
FT CHAIN 25..107
FT /note="Nerve growth factor gamma chain 1"
FT /id="PRO_0000027970"
FT CHAIN 112..261
FT /note="Nerve growth factor gamma chain 2"
FT /id="PRO_0000027971"
FT DOMAIN 25..258
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 25..107
FT /note="Segment B1"
FT REGION 112..261
FT /note="Segment A"
FT REGION 112..164
FT /note="Segment C"
FT REGION 165..261
FT /note="Segment B2"
FT ACT_SITE 65
FT /note="Charge relay system"
FT ACT_SITE 120
FT /note="Charge relay system"
FT ACT_SITE 213
FT /note="Charge relay system"
FT BINDING 231
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 236
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:7263706"
FT DISULFID 31..173
FT DISULFID 50..66
FT DISULFID 152..219
FT DISULFID 184..198
FT DISULFID 209..234
FT CONFLICT 108..111
FT /note="Missing (in Ref. 2)"
FT /evidence="ECO:0000305"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:1SGF"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:1SGF"
FT STRAND 47..56
FT /evidence="ECO:0007829|PDB:1SGF"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:1SGF"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:1SGF"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:1SGF"
FT STRAND 88..97
FT /evidence="ECO:0007829|PDB:1SGF"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:1SGF"
FT STRAND 122..128
FT /evidence="ECO:0007829|PDB:1SGF"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:1SGF"
FT STRAND 151..164
FT /evidence="ECO:0007829|PDB:1SGF"
FT STRAND 172..179
FT /evidence="ECO:0007829|PDB:1SGF"
FT HELIX 181..187
FT /evidence="ECO:0007829|PDB:1SGF"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:1SGF"
FT STRAND 202..205
FT /evidence="ECO:0007829|PDB:1SGF"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:1SGF"
FT STRAND 222..229
FT /evidence="ECO:0007829|PDB:1SGF"
FT STRAND 241..245
FT /evidence="ECO:0007829|PDB:1SGF"
FT HELIX 246..249
FT /evidence="ECO:0007829|PDB:1SGF"
FT HELIX 250..258
FT /evidence="ECO:0007829|PDB:1SGF"
SQ SEQUENCE 261 AA; 28998 MW; 4870748E174AF7C8 CRC64;
MWFLILFLAL SLGGIDAAPP VQSRIVGGFK CEKNSQPWHV AVYRYTQYLC GGVLLDPNWV
LTAAHCYDDN YKVWLGKNNL FKDEPSAQHR FVSKAIPHPG FNMSLMRKHI RFLEYDYSND
LMLLRLSKPA DITDTVKPIT LPTEEPKLGS TCLASGWGSI TPTKFQFTDD LYCVNLKLLP
NEDCAKAHIE KVTDAMLCAG EMDGGKDTCK GDSGGPLICD GVLQGITSWG HTPCGEPDMP
GVYTKLNKFT SWIKDTMAKN P
