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UniProtKB/Swiss-Prot entry Q9Y5K2


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name KLK4_HUMAN
Primary accession number Q9Y5K2
Secondary accession numbers Q4VB16 Q9GZL6 Q9UBJ6
Integrated into Swiss-Prot on December 1, 2000
Sequence was last modified on November 1, 1999 (Sequence version 1)
Annotations were last modified on    May 26, 2009 (Entry version 82)
Name and origin of the protein
Protein name Kallikrein-4 [Precursor]
Synonyms EC 3.4.21.-
Prostase
Kallikrein-like protein 1
KLK-L1
Enamel matrix serine proteinase 1
Serine protease 17
Gene name
Name: KLK4
Synonyms: EMSP1, PRSS17, PSTS
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANT HIS-197.
DOI=10.1073/pnas.96.6.3114; PubMed=10077646 [NCBI, ExPASy, EBI, Israel, Japan]
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].
PubMed=10485467 [NCBI, ExPASy, EBI, Israel, Japan]
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].
DOI=10.1074/jbc.274.33.23210; PubMed=10438493 [NCBI, ExPASy, EBI, Israel, Japan]
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], AND VARIANT HIS-197.
DOI=10.1016/S0378-1119(00)00382-6; PubMed=11054574 [NCBI, ExPASy, EBI, Israel, Japan]
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], AND CHARACTERIZATION.
DOI=10.1016/S0378-1119(00)00203-1; PubMed=10863090 [NCBI, ExPASy, EBI, Israel, Japan]
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].
TISSUE=Prostatic carcinoma;
Korkmaz K.S., Korkmaz C.G., Saatcioglu F.;
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature02399; PubMed=15057824 [NCBI, ExPASy, EBI, Israel, Japan]
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].
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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.
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, AND DISULFIDE BONDS.
DOI=10.1016/j.jmb.2006.08.003; PubMed=16950394 [NCBI, ExPASy, EBI, Israel, Japan]
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]
INVOLVEMENT IN AI2A1, AND VARIANT ALA-22.
DOI=10.1136/jmg.2003.017657; PubMed=15235027 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF113140; AAD21580.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF113141; AAD21581.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF135023; AAD26424.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF148532; AAD38019.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF243527; AAG33357.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF228497; AAF70620.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF259969; AAF81227.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC037199; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
BC069325; AAH69325.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC069403; AAH69403.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC069429; AAH69429.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC069489; AAH69489.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC096175; AAH96175.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC096178; AAH96178.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF126401; AAG43246.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00001559; -.
RefSeq NP_004908.3; -.
UniGene Hs.218366
3D structure databases
PDB
2BDG; X-ray; 1.95 A; A/B=31-253.[ExPASy / RCSB / EBI]
2BDH; X-ray; 3.00 A; A/B/C/D=31-253.[ExPASy / RCSB / EBI]
2BDI; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=31-253.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 2BDG; -.
2BDH; -.
2BDI; -.
ModBase Q9Y5K2.
Organism-specific databases
GeneCards GC19M056101; -.
HGNC HGNC:6365; KLK4.
GenAtlas KLK4.
MIM 204700; phenotype. [NCBI / EBI]
603767; gene. [NCBI / EBI]
Orphanet 88661; Amelogenesis imperfecta.
100033; Amelogenesis imperfecta, hypomaturation type.
PharmGKB PA30154; -.
Gene expression databases
ArrayExpress Q9Y5K2; -.
Bgee Q9Y5K2; -.
CleanEx HS_KLK4; -.
GermOnline ENSG00000167749; Homo sapiens.
Ontologies
GO
GO:0005576; Cellular component: extracellular region (traceable author statement from ProtInc).
GO:0004252; Molecular function: serine-type endopeptidase activity (inferred from electronic annotation from InterPro).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006508; Biological process: proteolysis (non-traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR018114; Peptidase_S1/S6_AS.
IPR001254; Peptidase_S1_S6.
IPR001314; Peptidase_S1A.
Graphical view of domain structure.
Pfam PF00089; Trypsin; 1.
Pfam graphical view of domain structure.
PRINTS PR00722; CHYMOTRYPSIN.
SMART SM00020; Tryp_SPc; 1.
SMART graphical view of domain structure.
PROSITE PS50240; TRYPSIN_DOM; 1.
PS00134; TRYPSIN_HIS; 1.
PS00135; TRYPSIN_SER; 1.
PROSITE graphical view of domain structure (profiles).
Genome annotation databases
Ensembl ENSG00000167749; Homo sapiens. [Contig view]
GeneID 9622; -.
KEGG hsa:9622; -.
Phylogenomic databases
HOGENOM Q9Y5K2; -.
HOVERGEN Q9Y5K2; -.
Other
NextBio 36105; -.
SOURCE KLK4; Homo sapiens.
ProtoNet Q9Y5K2.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Amelogenesis imperfecta; Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase; Metal-binding; Polymorphism; Protease; Secreted; Serine protease; Signal; Zinc; Zymogen.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    26  26     Potential. 
PROPEP   27    30  4     Potential. PRO_0000027937
CHAIN   31   254  224     Kallikrein-4. PRO_0000027938
DOMAIN   31   252  222     Peptidase S1. 
ACT_SITE   71    71        Charge relay system. 
ACT_SITE   116   116        Charge relay system. 
ACT_SITE   207   207        Charge relay system. 
METAL   40    40        Zinc. 
METAL   91    91        Zinc. 
CARBOHYD   169   169        N-linked (GlcNAc...) (Potential). 
DISULFID   37   167         
DISULFID   56    72         
DISULFID   141   241         
DISULFID   148   213         
DISULFID   178   192         
DISULFID   203   228         
VARIANT   22    22  1     S -> A (in dbSNP:rs1654551 [NCBI]). VAR_028364 
VARIANT   159   159  1     G -> D (in dbSNP:rs34626614 [NCBI]). VAR_033009 [3D]
VARIANT   197   197  1     Q -> H (in dbSNP:rs2569527 [NCBI]). VAR_028365 [3D]
STRAND   45    49  5      
STRAND   54    62  9      
STRAND   65    68  4      
HELIX   70    72  3      
STRAND   75    82  8      
STRAND   84    86  3      
HELIX   88    90  3      
STRAND   95   104  10      
TURN   106   109  4      
STRAND   118   124  7      
STRAND   147   153  7      
STRAND   166   172  7      
HELIX   175   181  7      
TURN   183   185  3      
STRAND   190   193  4      
STRAND   210   213  4      
STRAND   216   223  8      
STRAND   235   238  4      
HELIX   240   242  3      
HELIX   244   252  9      
Sequence information
Length: 254 AA [This is the length of the unprocessed precursor] Molecular weight: 27023 Da [This is the MW of the unprocessed precursor] CRC64: 9C475E22B6EE0CB8 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MATAGNPWGW FLGYLILGVA GSLVSGSCSQ IINGEDCSPH SQPWQAALVM ENELFCSGVL 

        70         80         90        100        110        120 
VHPQWVLSAA HCFQNSYTIG LGLHSLEADQ EPGSQMVEAS LSVRHPEYNR PLLANDLMLI 

       130        140        150        160        170        180 
KLDESVSESD TIRSISIASQ CPTAGNSCLV SGWGLLANGR MPTVLQCVNV SVVSEEVCSK 

       190        200        210        220        230        240 
LYDPLYHPSM FCAGGGQDQK DSCNGDSGGP LICNGYLQGL VSFGKAPCGQ VGVPGVYTNL 

       250 
CKFTEWIEKT VQAS 

Q9Y5K2 in FASTA format

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