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 24-JAN-2024, entry version 200. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 GlyCosmos; P00756; 1 site, No reported glycans. DR GlyGen; P00756; 2 sites. DR iPTMnet; P00756; -. DR MaxQB; P00756; -. DR PaxDb; 10090-ENSMUSP00000082577; -. DR PeptideAtlas; P00756; -. DR ProteomicsDB; 269166; -. DR DNASU; 18050; -. DR Ensembl; ENSMUST00000085450.4; ENSMUSP00000082577.3; ENSMUSG00000066515.4. DR GeneID; 18050; -. DR KEGG; mmu:18050; -. DR UCSC; uc009gol.2; mouse. DR AGR; MGI:97322; -. 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; FLEYDYS; -. DR OrthoDB; 4629979at2759; -. DR PhylomeDB; P00756; -. DR TreeFam; TF331065; -. DR BRENDA; 3.4.21.77; 3474. DR BioGRID-ORCS; 18050; 4 hits in 79 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 epiblast cell in embryo and 25 other cell types or tissues. DR ExpressionAtlas; P00756; baseline and differential. 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; Trypsin-like serine proteases; 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 PANTHER; PTHR24271:SF47; KALLIKREIN-1; 1. DR PANTHER; PTHR24271; KALLIKREIN-RELATED; 1. DR Pfam; PF00089; Trypsin; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR SMART; SM00020; Tryp_SPc; 1. DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1. DR PROSITE; PS50240; TRYPSIN_DOM; 1. DR PROSITE; PS00134; TRYPSIN_HIS; 1. DR PROSITE; PS00135; TRYPSIN_SER; 1. DR Genevisible; P00756; MM. 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 //