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Kallikrein-4 (EC 3.4.21.-) (Enamel matrix serine proteinase 1) (Kallikrein-like protein 1) (KLK-L1) (Prostase) (Serine protease 17)

 KLK4_HUMAN              Reviewed;         254 AA.
Q9Y5K2; Q4VB16; Q96RU5; Q9GZL6; Q9UBJ6;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 2.
27-SEP-2017, entry version 152.
RecName: Full=Kallikrein-4;
EC=3.4.21.-;
AltName: Full=Enamel matrix serine proteinase 1;
AltName: Full=Kallikrein-like protein 1;
Short=KLK-L1;
AltName: Full=Prostase;
AltName: Full=Serine protease 17;
Flags: Precursor;
Name=KLK4; Synonyms=EMSP1, PRSS17, PSTS;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
PubMed=10077646; DOI=10.1073/pnas.96.6.3114;
Nelson P.S., Gan L., Ferguson C., Moss P., Gelinas R., Hood L.,
Wang K.;
"Molecular cloning and characterization of prostase, an androgen-
regulated serine protease with prostate-restricted expression.";
Proc. Natl. Acad. Sci. U.S.A. 96:3114-3119(1999).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLN-197.
PubMed=10485467;
Yousef G.M., Obiezu C.V., Luo L.-Y., Black M.H., Diamandis E.P.;
"Prostase/KLK-L1 is a new member of the human kallikrein gene family,
is expressed in prostate and breast tissues, and is hormonally
regulated.";
Cancer Res. 59:4252-4256(1999).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLN-197.
PubMed=10438493; DOI=10.1074/jbc.274.33.23210;
Stephenson S.A., Verity K., Ashworth L.K., Clements J.A.;
"Localization of a new prostate-specific antigen-related serine
protease gene, KLK4, is evidence for an expanded human kallikrein gene
family cluster on chromosome 19q13.3-13.4.";
J. Biol. Chem. 274:23210-23214(1999).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=11054574; DOI=10.1016/S0378-1119(00)00382-6;
Gan L., Lee I., Smith R., Argonza-Barrett R., Lei H., McCuaig J.,
Moss P., Paeper B., Wang K.;
"Sequencing and expression analysis of the serine protease gene
cluster located in chromosome 19q13 region.";
Gene 257:119-130(2000).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION, AND VARIANT
GLN-197.
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).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANT GLN-197, AND
ALTERNATIVE SPLICING.
TISSUE=Prostatic carcinoma;
PubMed=11506707; DOI=10.1089/104454901750361497;
Korkmaz K.S., Korkmaz C.G., Pretlow T.G., Saatcioglu F.;
"Distinctly different gene structure of KLK4/KLK-L1/prostase/ARM1
compared with other members of the kallikrein family: intracellular
localization, alternative cDNA forms, and Regulation by multiple
hormones.";
DNA Cell Biol. 20:435-445(2001).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
GLN-197.
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).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 22-254 (ISOFORM 1), AND VARIANT GLN-197.
Simmer J.P., Ryu O.H., Qian Q., Zhang C., Cao X., Sun X., Hu C.-C.;
"Cloning and characterization of a cDNA encoding human EMSP1.";
(In) Goldberg M. (eds.);
Chemistry and biology of mineralized tissues, pp.1-1, American Academy
of Orthopaedic Surgeons, Vittel (2000).
[10]
PROTEIN SEQUENCE OF 31-35, X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF
31-253, ACTIVE SITE, ZINC-BINDING SITES, DISULFIDE BONDS, AND VARIANT
GLN-197.
PubMed=16950394; DOI=10.1016/j.jmb.2006.08.003;
Debela M., Magdolen V., Grimminger V., Sommerhoff C.,
Messerschmidt A., Huber R., Friedrich R., Bode W., Goettig P.;
"Crystal structures of human tissue kallikrein 4: activity modulation
by a specific zinc binding site.";
J. Mol. Biol. 362:1094-1107(2006).
[11]
FUNCTION, INVOLVEMENT IN AI2A1, AND VARIANT ALA-22.
PubMed=15235027; DOI=10.1136/jmg.2003.017657;
Hart P.S., Hart T.C., Michalec M.D., Ryu O.H., Simmons D., Hong S.,
Wright J.T.;
"Mutation in kallikrein 4 causes autosomal recessive hypomaturation
amelogenesis imperfecta.";
J. Med. Genet. 41:545-549(2004).
-!- FUNCTION: Has a major role in enamel formation (PubMed:15235027).
Required during the maturation stage of tooth development for
clearance of enamel proteins and normal structural patterning of
the crystalline matrix (By similarity).
{ECO:0000250|UniProtKB:Q9Z0M1, ECO:0000269|PubMed:15235027}.
-!- INTERACTION:
Q06418:TYRO3; NbExp=3; IntAct=EBI-10224152, EBI-3951628;
-!- SUBCELLULAR LOCATION: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9Y5K2-1; Sequence=Displayed;
Name=2;
IsoId=Q9Y5K2-2; Sequence=VSP_056629, VSP_056630;
-!- TISSUE SPECIFICITY: Expressed in prostate.
-!- 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:0000250|UniProtKB:Q9Z0M1}.
-!- DISEASE: Amelogenesis imperfecta, hypomaturation type, 2A1 (AI2A1)
[MIM:204700]: A defect of enamel formation. The disorder involves
both primary and secondary dentitions. The teeth have a shiny agar
jelly appearance and the enamel is softer than normal. Brown
pigment is present in middle layers of enamel.
{ECO:0000269|PubMed:15235027}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the peptidase S1 family. Kallikrein
subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/KLK4ID41084ch19q13.html";
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EMBL; AF113140; AAD21580.1; -; mRNA.
EMBL; AF113141; AAD21581.1; -; Genomic_DNA.
EMBL; AF135023; AAD26424.2; -; Genomic_DNA.
EMBL; AF148532; AAD38019.1; -; Genomic_DNA.
EMBL; AF243527; AAG33357.1; -; Genomic_DNA.
EMBL; AF228497; AAF70620.1; -; Genomic_DNA.
EMBL; AF259969; AAF81227.1; -; mRNA.
EMBL; AF259971; AAK71706.1; -; mRNA.
EMBL; AC037199; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC069325; AAH69325.1; -; mRNA.
EMBL; BC069403; AAH69403.1; -; mRNA.
EMBL; BC069429; AAH69429.1; -; mRNA.
EMBL; BC069489; AAH69489.1; -; mRNA.
EMBL; BC096175; AAH96175.1; -; mRNA.
EMBL; BC096178; AAH96178.1; -; mRNA.
EMBL; AF126401; AAG43246.1; -; mRNA.
CCDS; CCDS12809.1; -. [Q9Y5K2-1]
RefSeq; NP_001289890.1; NM_001302961.1.
RefSeq; NP_004908.4; NM_004917.4.
UniGene; Hs.218366; -.
PDB; 2BDG; X-ray; 1.95 A; A/B=31-247.
PDB; 2BDH; X-ray; 3.00 A; A/B/C/D=31-247.
PDB; 2BDI; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=31-247.
PDB; 4K1E; X-ray; 1.30 A; A=31-253.
PDB; 4K8Y; X-ray; 1.00 A; A=31-253.
PDB; 4KEL; X-ray; 1.15 A; A=31-253.
PDB; 4KGA; X-ray; 2.32 A; A/B=31-253.
PDBsum; 2BDG; -.
PDBsum; 2BDH; -.
PDBsum; 2BDI; -.
PDBsum; 4K1E; -.
PDBsum; 4K8Y; -.
PDBsum; 4KEL; -.
PDBsum; 4KGA; -.
ProteinModelPortal; Q9Y5K2; -.
SMR; Q9Y5K2; -.
BioGrid; 114982; 4.
IntAct; Q9Y5K2; 1.
STRING; 9606.ENSP00000326159; -.
BindingDB; Q9Y5K2; -.
ChEMBL; CHEMBL4446; -.
GuidetoPHARMACOLOGY; 2374; -.
MEROPS; S01.251; -.
PhosphoSitePlus; Q9Y5K2; -.
BioMuta; KLK4; -.
DMDM; 317373372; -.
EPD; Q9Y5K2; -.
PaxDb; Q9Y5K2; -.
PeptideAtlas; Q9Y5K2; -.
PRIDE; Q9Y5K2; -.
DNASU; 9622; -.
Ensembl; ENST00000431178; ENSP00000399448; ENSG00000167749. [Q9Y5K2-2]
GeneID; 9622; -.
KEGG; hsa:9622; -.
UCSC; uc002pty.2; human. [Q9Y5K2-1]
CTD; 9622; -.
DisGeNET; 9622; -.
EuPathDB; HostDB:ENSG00000167749.11; -.
GeneCards; KLK4; -.
H-InvDB; HIX0039968; -.
HGNC; HGNC:6365; KLK4.
HPA; HPA051839; -.
MalaCards; KLK4; -.
MIM; 204700; phenotype.
MIM; 603767; gene.
neXtProt; NX_Q9Y5K2; -.
OpenTargets; ENSG00000167749; -.
Orphanet; 100033; Hypomaturation amelogenesis imperfecta.
PharmGKB; PA30154; -.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00760000118862; -.
HOGENOM; HOG000251820; -.
HOVERGEN; HBG013304; -.
InParanoid; Q9Y5K2; -.
KO; K08666; -.
PhylomeDB; Q9Y5K2; -.
TreeFam; TF331065; -.
BRENDA; 3.4.21.B12; 2681.
ChiTaRS; KLK4; human.
EvolutionaryTrace; Q9Y5K2; -.
GeneWiki; KLK4; -.
GenomeRNAi; 9622; -.
PRO; PR:Q9Y5K2; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000167749; -.
CleanEx; HS_KLK4; -.
ExpressionAtlas; Q9Y5K2; baseline and differential.
Genevisible; Q9Y5K2; HS.
GO; GO:0005576; C:extracellular region; TAS:ProtInc.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0008236; F:serine-type peptidase activity; TAS:ProtInc.
GO; GO:0097186; P:amelogenesis; IMP:UniProtKB.
GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
GO; GO:0006508; P:proteolysis; NAS:UniProtKB.
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;
3D-structure; Alternative splicing; Amelogenesis imperfecta;
Biomineralization; Complete proteome; Direct protein sequencing;
Disulfide bond; Glycoprotein; Hydrolase; Metal-binding; Polymorphism;
Protease; Reference proteome; Secreted; Serine protease; Signal; Zinc;
Zymogen.
SIGNAL 1 26 {ECO:0000255}.
PROPEP 27 30 {ECO:0000305|PubMed:16950394}.
/FTId=PRO_0000027937.
CHAIN 31 254 Kallikrein-4.
/FTId=PRO_0000027938.
DOMAIN 31 252 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 71 71 Charge relay system.
{ECO:0000269|PubMed:16950394}.
ACT_SITE 116 116 Charge relay system.
{ECO:0000269|PubMed:16950394}.
ACT_SITE 207 207 Charge relay system.
{ECO:0000269|PubMed:16950394}.
METAL 40 40 Zinc. {ECO:0000269|PubMed:16950394}.
METAL 91 91 Zinc. {ECO:0000269|PubMed:16950394}.
CARBOHYD 169 169 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 37 167 {ECO:0000255|PROSITE-ProRule:PRU00274,
ECO:0000269|PubMed:16950394}.
DISULFID 56 72 {ECO:0000255|PROSITE-ProRule:PRU00274,
ECO:0000269|PubMed:16950394}.
DISULFID 141 241 {ECO:0000255|PROSITE-ProRule:PRU00274,
ECO:0000269|PubMed:16950394}.
DISULFID 148 213 {ECO:0000255|PROSITE-ProRule:PRU00274,
ECO:0000269|PubMed:16950394}.
DISULFID 178 192 {ECO:0000255|PROSITE-ProRule:PRU00274,
ECO:0000269|PubMed:16950394}.
DISULFID 203 228 {ECO:0000255|PROSITE-ProRule:PRU00274,
ECO:0000269|PubMed:16950394}.
VAR_SEQ 1 49 Missing (in isoform 2).
{ECO:0000303|PubMed:11506707}.
/FTId=VSP_056629.
VAR_SEQ 160 254 Missing (in isoform 2).
{ECO:0000303|PubMed:11506707}.
/FTId=VSP_056630.
VARIANT 22 22 S -> A (in dbSNP:rs1654551).
{ECO:0000269|PubMed:15235027}.
/FTId=VAR_028364.
VARIANT 159 159 G -> D (in dbSNP:rs34626614).
/FTId=VAR_033009.
VARIANT 197 197 H -> Q (in dbSNP:rs2569527).
{ECO:0000269|PubMed:10438493,
ECO:0000269|PubMed:10485467,
ECO:0000269|PubMed:10863090,
ECO:0000269|PubMed:11506707,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:16950394,
ECO:0000269|Ref.9}.
/FTId=VAR_028365.
STRAND 45 50 {ECO:0000244|PDB:4K8Y}.
STRAND 53 62 {ECO:0000244|PDB:4K8Y}.
STRAND 65 68 {ECO:0000244|PDB:4K8Y}.
HELIX 70 72 {ECO:0000244|PDB:4K8Y}.
STRAND 75 82 {ECO:0000244|PDB:4K8Y}.
STRAND 84 86 {ECO:0000244|PDB:4K8Y}.
HELIX 88 90 {ECO:0000244|PDB:4K8Y}.
STRAND 95 99 {ECO:0000244|PDB:4K8Y}.
STRAND 101 104 {ECO:0000244|PDB:4K8Y}.
TURN 106 109 {ECO:0000244|PDB:4K8Y}.
STRAND 118 121 {ECO:0000244|PDB:4K8Y}.
STRAND 130 132 {ECO:0000244|PDB:4KGA}.
STRAND 147 154 {ECO:0000244|PDB:4K8Y}.
STRAND 157 160 {ECO:0000244|PDB:2BDH}.
STRAND 166 172 {ECO:0000244|PDB:4K8Y}.
HELIX 175 182 {ECO:0000244|PDB:4K8Y}.
TURN 183 185 {ECO:0000244|PDB:4K8Y}.
STRAND 190 193 {ECO:0000244|PDB:4K8Y}.
STRAND 210 213 {ECO:0000244|PDB:4K8Y}.
STRAND 216 227 {ECO:0000244|PDB:4K8Y}.
STRAND 235 239 {ECO:0000244|PDB:4K8Y}.
HELIX 240 242 {ECO:0000244|PDB:4K8Y}.
HELIX 244 252 {ECO:0000244|PDB:4K8Y}.
SEQUENCE 254 AA; 27032 MW; 9C5E4722AFF70CB8 CRC64;
MATAGNPWGW FLGYLILGVA GSLVSGSCSQ IINGEDCSPH SQPWQAALVM ENELFCSGVL
VHPQWVLSAA HCFQNSYTIG LGLHSLEADQ EPGSQMVEAS LSVRHPEYNR PLLANDLMLI
KLDESVSESD TIRSISIASQ CPTAGNSCLV SGWGLLANGR MPTVLQCVNV SVVSEEVCSK
LYDPLYHPSM FCAGGGHDQK DSCNGDSGGP LICNGYLQGL VSFGKAPCGQ VGVPGVYTNL
CKFTEWIEKT VQAS


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