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Kallikrein-4 (EC 3.4.21.-) (Enamel matrix serine proteinase 1) (Kallikrein-like protein 1) (Serine protease 17)

 KLK4_MOUSE              Reviewed;         255 AA.
Q9Z0M1; Q9JIS2;
13-APR-2016, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
23-MAY-2018, entry version 135.
RecName: Full=Kallikrein-4 {ECO:0000250|UniProtKB:Q9Y5K2};
EC=3.4.21.- {ECO:0000255|PROSITE-ProRule:PRU00274};
AltName: Full=Enamel matrix serine proteinase 1 {ECO:0000303|PubMed:10690663};
AltName: Full=Kallikrein-like protein 1 {ECO:0000250|UniProtKB:Q9Y5K2};
AltName: Full=Serine protease 17 {ECO:0000303|PubMed:10863090};
Flags: Precursor;
Name=Klk4 {ECO:0000312|MGI:MGI:1861379};
Synonyms=EMSP1 {ECO:0000303|PubMed:10690663},
KLK-L1 {ECO:0000312|MGI:MGI:1861379},
Prss17 {ECO:0000303|PubMed:10863090};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1] {ECO:0000312|EMBL:AAF85937.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DEVELOPMENTAL STAGE.
STRAIN=129/SvJ {ECO:0000312|EMBL:AAF85937.1};
PubMed=10863090; DOI=10.1016/S0378-1119(00)00203-1;
Hu J.C.-C., Zhang C., Sun X., Yang Y., Cao X., Ryu O., Simmer J.P.;
"Characterization of the mouse and human PRSS17 genes, their
relationship to other serine proteases, and the expression of PRSS17
in developing mouse incisors.";
Gene 251:1-8(2000).
[2] {ECO:0000312|EMBL:AAC98894.1}
NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
STRAIN=Swiss Webster {ECO:0000312|EMBL:AAC98894.1};
TISSUE=Ameloblast {ECO:0000312|EMBL:AAC98894.1};
PubMed=10690663; DOI=10.1177/00220345000790011301;
Hu J.C.-C., Ryu O.H., Chen J.J., Uchida T., Wakida K., Murakami C.,
Jiang H., Qian Q., Zhang C., Ottmers V., Bartlett J.D., Simmer J.P.;
"Localization of EMSP1 expression during tooth formation and cloning
of mouse cDNA.";
J. Dent. Res. 79:70-76(2000).
[3] {ECO:0000312|Proteomes:UP000000589}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4] {ECO:0000312|Proteomes:UP000000589}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5] {ECO:0000312|EMBL:AAI00717.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6] {ECO:0000305}
FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
PubMed=19578120; DOI=10.1074/jbc.M109.013623;
Simmer J.P., Hu Y., Lertlam R., Yamakoshi Y., Hu J.C.;
"Hypomaturation enamel defects in Klk4 knockout/LacZ knockin mice.";
J. Biol. Chem. 284:19110-19121(2009).
[7] {ECO:0000305}
GLYCOSYLATION.
PubMed=22243251; DOI=10.1111/j.1600-0722.2011.00863.x;
Yamakoshi Y., Yamakoshi F., Hu J.C., Simmer J.P.;
"Characterization of kallikrein-related peptidase 4 glycosylations.";
Eur. J. Oral Sci. 119:234-240(2011).
-!- FUNCTION: Has a major role in enamel formation. Required during
the maturation stage of tooth development for clearance of enamel
proteins and normal structural patterning of the crystalline
matrix. {ECO:0000269|PubMed:19578120}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
-!- DEVELOPMENTAL STAGE: In developing teeth, expressed in ameloblasts
during transition and maturation stages (PubMed:10863090,
PubMed:10690663, PubMed:19578120). Expressed weakly in
odontoblasts (PubMed:10863090). Not detected in odontoblasts
(PubMed:19578120). Detected in the epithelium surrounding the
erupted first molar (PubMed:10690663).
{ECO:0000269|PubMed:10690663, ECO:0000269|PubMed:10863090,
ECO:0000269|PubMed:19578120}.
-!- PTM: N-glycosylated. The N-glycan structures are of complex
diantennary or triantennary type, which may be further modified
with up to 2 sialic acid residues. {ECO:0000269|PubMed:22243251}.
-!- DISRUPTION PHENOTYPE: Viable and fertile, when reared on a soft
diet. Tooth morphology is grossly normal but the enamel surface is
fragile and rapidly abraded. Although formation of the enamel
layer is initially normal, the crystallites fail to thicken and
interlock. The enamel proteins enamelin and amelogenin are not
cleared and persist in the matrix during the maturation stage.
{ECO:0000269|PubMed:19578120}.
-!- SIMILARITY: Belongs to the peptidase S1 family. Kallikrein
subfamily. {ECO:0000305}.
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EMBL; AF198031; AAF85937.1; -; Genomic_DNA.
EMBL; AF019979; AAC98894.1; -; mRNA.
EMBL; AC134858; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH466603; EDL22687.1; -; Genomic_DNA.
EMBL; BC100716; AAI00717.1; -; mRNA.
EMBL; BC100717; AAI00718.1; -; mRNA.
EMBL; BC100718; AAI00719.1; -; mRNA.
EMBL; BC100719; AAI00720.1; -; mRNA.
CCDS; CCDS21186.1; -.
RefSeq; NP_064312.1; NM_019928.1.
UniGene; Mm.42080; -.
ProteinModelPortal; Q9Z0M1; -.
SMR; Q9Z0M1; -.
STRING; 10090.ENSMUSP00000007161; -.
MEROPS; S01.251; -.
PhosphoSitePlus; Q9Z0M1; -.
PaxDb; Q9Z0M1; -.
PRIDE; Q9Z0M1; -.
Ensembl; ENSMUST00000007161; ENSMUSP00000007161; ENSMUSG00000006948.
GeneID; 56640; -.
KEGG; mmu:56640; -.
UCSC; uc009gny.1; mouse.
CTD; 9622; -.
MGI; MGI:1861379; Klk4.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00910000144067; -.
HOGENOM; HOG000251820; -.
HOVERGEN; HBG013304; -.
KO; K08666; -.
OMA; NGEDCSP; -.
OrthoDB; EOG091G0DF7; -.
PhylomeDB; Q9Z0M1; -.
TreeFam; TF331065; -.
BRENDA; 3.4.21.B12; 3474.
PRO; PR:Q9Z0M1; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000006948; -.
ExpressionAtlas; Q9Z0M1; baseline and differential.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0097186; P:amelogenesis; IMP:MGI.
GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
GO; GO:0022617; P:extracellular matrix disassembly; IMP:MGI.
GO; GO:0030163; P:protein catabolic process; IMP:MGI.
CDD; cd00190; Tryp_SPc; 1.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
Pfam; PF00089; Trypsin; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
1: Evidence at protein level;
Biomineralization; Complete proteome; Disulfide bond; Glycoprotein;
Hydrolase; Metal-binding; Protease; Reference proteome; Secreted;
Serine protease; Signal; Zinc; Zymogen.
SIGNAL 1 25 {ECO:0000255}.
PROPEP 26 31 {ECO:0000250|UniProtKB:Q9Y5K2}.
/FTId=PRO_0000436024.
CHAIN 32 255 Kallikrein-4. {ECO:0000255}.
/FTId=PRO_5006493980.
DOMAIN 32 253 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 72 72 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
ACT_SITE 117 117 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
ACT_SITE 208 208 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
METAL 41 41 Zinc. {ECO:0000250|UniProtKB:Q9Y5K2}.
METAL 92 92 Zinc. {ECO:0000250|UniProtKB:Q9Y5K2}.
CARBOHYD 124 124 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 170 170 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 57 73 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 149 214 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 179 193 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 204 229 {ECO:0000255|PROSITE-ProRule:PRU00274}.
CONFLICT 15 15 C -> Y (in Ref. 1; AAF85937).
{ECO:0000305}.
CONFLICT 251 251 I -> T (in Ref. 1; AAF85937).
{ECO:0000305}.
SEQUENCE 255 AA; 27488 MW; 6FD2E7DEA0660A2A CRC64;
MMVTARTPWG WFLGCLILEV TGASASSVSS RIIQGQDCSP HSQPWQAALF SEDGFFCSGV
LVHPQWVLSA AHCLQESYIV GLGLHNLKGS QEPGSRMLEA HLSIQHPNFN DPSFANDLML
IKLNESVIES NTIRSIPVAT QCPTPGDTCL VSGWGQLKNG KLPSLLQCVN LSVASEETCR
LLYDPVYHLS MFCAGGGQDQ KDSCNGDSGG PIVCNRSLQG LVSMGQGKCG QPGIPSVYTN
LCKFTNWIQT IIQTN


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