EGFB2_MOUSE
ID EGFB2_MOUSE Reviewed; 261 AA.
AC P36368; P00754;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 25-MAY-2022, entry version 147.
DE RecName: Full=Epidermal growth factor-binding protein type B;
DE Short=EGF-BP B;
DE EC=3.4.21.119;
DE AltName: Full=Glandular kallikrein K13;
DE Short=mGK-13;
DE AltName: Full=Prorenin-converting enzyme 1;
DE Short=PRECE-1;
DE AltName: Full=Tissue kallikrein 13;
DE Flags: Precursor;
GN Name=Egfbp2; Synonyms=Egfbp-2, Klk-13, Klk13;
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 [GENOMIC DNA].
RC STRAIN=BALB/cJ; TISSUE=Salivary gland;
RX PubMed=3322387; DOI=10.1021/bi00395a026;
RA Drinkwater C.C., Evans B.A., Richards R.I.;
RT "Mouse glandular kallikrein genes: identification and characterization of
RT the genes encoding the epidermal growth factor binding proteins.";
RL Biochemistry 26:6750-6756(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ICR; TISSUE=Submandibular gland;
RX PubMed=1918045; DOI=10.1016/s0021-9258(18)54995-4;
RA Kim W.S., Nakayama K., Nakagawa T., Kawamura Y., Haraguchi K., Murakami K.;
RT "Mouse submandibular gland prorenin-converting enzyme is a member of
RT glandular kallikrein family.";
RL J. Biol. Chem. 266:19283-19287(1991).
RN [3]
RP PROTEIN SEQUENCE OF 17-54, AND NUCLEOTIDE SEQUENCE OF 70-122.
RX PubMed=3036794; DOI=10.1016/s0021-9258(18)47521-7;
RA Evans B.A., Drinkwater C.C., Richards R.I.;
RT "Mouse glandular kallikrein genes. Structure and partial sequence analysis
RT of the kallikrein gene locus.";
RL J. Biol. Chem. 262:8027-8034(1987).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX PubMed=9232643; DOI=10.1002/pro.5560060706;
RA Timm D.E.;
RT "The crystal structure of the mouse glandular kallikrein-13 (prorenin
RT converting enzyme).";
RL Protein Sci. 6:1418-1425(1997).
CC -!- FUNCTION: Cleaves REN2 at a dibasic site to yield mature renin.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes mouse Ren2 protein (a species of prorenin present
CC in the submandibular gland) on the carboxy side of the arginine
CC residue at the Lys-Arg-|- pair in the N-terminus, to yield mature
CC renin.; EC=3.4.21.119;
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; M17982; AAA37680.1; -; Genomic_DNA.
DR EMBL; M17980; AAA37680.1; JOINED; Genomic_DNA.
DR EMBL; M17981; AAA37680.1; JOINED; Genomic_DNA.
DR EMBL; X58628; CAA41482.1; -; mRNA.
DR EMBL; M18612; AAA39354.1; -; Genomic_DNA.
DR PIR; A41020; A41020.
DR RefSeq; NP_034245.3; NM_010115.6.
DR PDB; 1AO5; X-ray; 2.60 A; A/B=25-261.
DR PDBsum; 1AO5; -.
DR AlphaFoldDB; P36368; -.
DR SMR; P36368; -.
DR MEROPS; S01.173; -.
DR GlyGen; P36368; 2 sites.
DR iPTMnet; P36368; -.
DR PhosphoSitePlus; P36368; -.
DR MaxQB; P36368; -.
DR PRIDE; P36368; -.
DR ProteomicsDB; 277557; -.
DR DNASU; 13647; -.
DR GeneID; 13647; -.
DR KEGG; mmu:13647; -.
DR CTD; 13647; -.
DR MGI; MGI:95292; Egfbp2.
DR InParanoid; P36368; -.
DR PhylomeDB; P36368; -.
DR BRENDA; 3.4.21.119; 3474.
DR BioGRID-ORCS; 13647; 2 hits in 12 CRISPR screens.
DR EvolutionaryTrace; P36368; -.
DR PRO; PR:P36368; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P36368; protein.
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; IDA:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0030141; C:secretory granule; IBA:GO_Central.
DR GO; GO:0004175; F:endopeptidase activity; ISO:MGI.
DR GO; GO:0008233; F:peptidase activity; IDA:MGI.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
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; IDA:MGI.
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 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.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hydrolase; Protease; Reference proteome; Serine protease; Signal; Zymogen.
FT SIGNAL 1..16
FT /evidence="ECO:0000269|PubMed:3036794"
FT PROPEP 17..24
FT /note="Activation peptide"
FT /id="PRO_0000027983"
FT CHAIN 25..261
FT /note="Epidermal growth factor-binding protein type B"
FT /id="PRO_0000027984"
FT DOMAIN 25..258
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
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 CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 31..173
FT DISULFID 50..66
FT DISULFID 152..219
FT DISULFID 184..198
FT DISULFID 209..234
FT CONFLICT 119
FT /note="N -> D (in Ref. 1)"
FT /evidence="ECO:0000305"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:1AO5"
FT STRAND 47..56
FT /evidence="ECO:0007829|PDB:1AO5"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:1AO5"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:1AO5"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:1AO5"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:1AO5"
FT HELIX 103..107
FT /evidence="ECO:0007829|PDB:1AO5"
FT STRAND 122..128
FT /evidence="ECO:0007829|PDB:1AO5"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:1AO5"
FT STRAND 151..157
FT /evidence="ECO:0007829|PDB:1AO5"
FT STRAND 172..179
FT /evidence="ECO:0007829|PDB:1AO5"
FT HELIX 181..187
FT /evidence="ECO:0007829|PDB:1AO5"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:1AO5"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:1AO5"
FT STRAND 222..229
FT /evidence="ECO:0007829|PDB:1AO5"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:1AO5"
FT HELIX 246..249
FT /evidence="ECO:0007829|PDB:1AO5"
FT HELIX 250..259
FT /evidence="ECO:0007829|PDB:1AO5"
SQ SEQUENCE 261 AA; 28689 MW; C2854D057877F602 CRC64;
MWFLILFLAL SLGGIDAAPP LQSRVVGGFN CKKNSQPWQV AVYYQKEHIC GGVLLDRNWV
LTAAHCYVDQ YEVWLGKNKL FQEEPSAQHR LVSKSFPHPG FNMSLLMLQT IPPGADFSND
LMLLRLSKPA DITDVVKPIA LPTKEPKPGS KCLASGWGSI TPTRWQKPDD LQCVFITLLP
NENCAKVYLQ KVTDVMLCAG EMGGGKDTCR DDSGGPLICD GILQGTTSYG PVPCGKPGVP
AIYTNLIKFN SWIKDTMMKN A
