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Kallikrein-6 (EC 3.4.21.-) (Neurosin) (Protease M) (SP59) (Serine protease 18) (Serine protease 9) (Zyme)

 KLK6_HUMAN              Reviewed;         244 AA.
Q92876; A6NJA1; A8MW09; Q6H301;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
27-SEP-2017, entry version 158.
RecName: Full=Kallikrein-6;
EC=3.4.21.-;
AltName: Full=Neurosin;
AltName: Full=Protease M;
AltName: Full=SP59;
AltName: Full=Serine protease 18;
AltName: Full=Serine protease 9;
AltName: Full=Zyme;
Flags: Precursor;
Name=KLK6; Synonyms=PRSS18, PRSS9;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8898378;
Anisowicz A., Sotiropoulou G., Stenman G., Mok S.C., Sager R.;
"A novel protease homolog differentially expressed in breast and
ovarian cancer.";
Mol. Med. 2:624-636(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Colon;
PubMed=9003450; DOI=10.1016/S0167-4781(96)00187-X;
Yamashiro K., Tsuruoka N., Kodama S., Tsujimoto M., Yamamura Y.,
Tanaka T., Nakazato H., Yamaguchi N.;
"Molecular cloning of a novel trypsin-like serine protease (neurosin)
preferentially expressed in brain.";
Biochim. Biophys. Acta 1350:11-14(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=9312124; DOI=10.1074/jbc.272.40.25135;
Little S.P., Dixon E.P., Norris F., Buckley W., Becker G.W.,
Johnson M., Dobbins J.R., Wyrick T., Miller J.R., Mackellar W.,
Hepburn D., Corvalan J., McClure D., Liu X., Stephenson D.,
Clemens J., Johnstone E.M.;
"Zyme, a novel and potentially amyloidogenic enzyme cDNA isolated from
Alzheimer's disease brain.";
J. Biol. Chem. 272:25135-25142(1997).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10610719; DOI=10.1006/geno.1999.6012;
Yousef G.M., Luo L.Y., Scherer S.W., Sotiropoulou G., Diamandis E.P.;
"Molecular characterization of Zyme/protease M/neurosin(PRSS9), a
hormonally regulated kallikrein-like serine protease.";
Genomics 62:251-259(1999).
[5]
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).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
TISSUE=Testis;
PubMed=15207701; DOI=10.1016/j.bbrc.2004.04.205;
Pampalakis G., Kurlender L., Diamandis E.P., Sotiropoulou G.;
"Cloning and characterization of novel isoforms of the human
kallikrein 6 gene.";
Biochem. Biophys. Res. Commun. 320:54-61(2004).
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
PubMed=16800739; DOI=10.1515/BC.2006.097;
Pampalakis G., Sotiropoulou G.;
"Multiple mechanisms underlie the aberrant expression of the human
kallikrein 6 gene in breast cancer.";
Biol. Chem. 387:773-782(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[10]
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).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Colon;
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).
[13]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=11018688; DOI=10.1016/S0009-9120(00)00145-4;
Diamandis E.P., Yousef G.M., Soosaipillai A.R., Grass L., Porter A.,
Little S., Sotiropoulou G.;
"Immunofluorometric assay of human kallikrein 6 (zyme/protease
M/neurosin) and preliminary clinical applications.";
Clin. Biochem. 33:369-375(2000).
[14]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=10997858; DOI=10.1046/j.1440-1819.2000.00731.x;
Ogawa K., Yamada T., Tsujioka Y., Taguchi J., Takahashi M., Tsuboi Y.,
Fujino Y., Nakajima M., Yamamoto T., Akatsu H., Mitsui S.,
Yamaguchi N.;
"Localization of a novel type trypsin-like serine protease, neurosin,
in brain tissues of Alzheimer's disease and Parkinson's disease.";
Psychiatry Clin. Neurosci. 54:419-426(2000).
[15]
TISSUE SPECIFICITY.
PubMed=11668196; DOI=10.1177/002215540104901111;
Petraki C.D., Karavana V.N., Skoufogiannis P.T., Little S.P.,
Howarth D.J.C., Yousef G.M., Diamandis E.P.;
"The spectrum of human kallikrein 6 (zyme/protease M/neurosin)
expression in human tissues as assessed by immunohistochemistry.";
J. Histochem. Cytochem. 49:1431-1441(2001).
[16]
FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND
AUTOCATALYTIC CLEAVAGE.
PubMed=12878203; DOI=10.1016/S0006-291X(03)01271-3;
Magklara A., Mellati A.A., Wasney G.A., Little S.P., Sotiropoulou G.,
Becker G.W., Diamandis E.P.;
"Characterization of the enzymatic activity of human kallikrein 6:
autoactivation, substrate specificity, and regulation by inhibitors.";
Biochem. Biophys. Res. Commun. 307:948-955(2003).
[17]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=12928483; DOI=10.1093/hmg/ddg283;
Iwata A., Maruyama M., Akagi T., Hashikawa T., Kanazawa I., Tsuji S.,
Nukina N.;
"Alpha-synuclein degradation by serine protease neurosin: implication
for pathogenesis of synucleinopathies.";
Hum. Mol. Genet. 12:2625-2635(2003).
[18]
FUNCTION.
PubMed=15557757; DOI=10.1159/000081102;
Ghosh M.C., Grass L., Soosaipillai A., Sotiropoulou G.,
Diamandis E.P.;
"Human kallikrein 6 degrades extracellular matrix proteins and may
enhance the metastatic potential of tumour cells.";
Tumor Biol. 25:193-199(2004).
[19]
FUNCTION, AND INDUCTION.
PubMed=16987227; DOI=10.1111/j.1460-9568.2006.05021.x;
Scarisbrick I.A., Sabharwal P., Cruz H., Larsen N., Vandell A.G.,
Blaber S.I., Ameenuddin S., Papke L.M., Fehlings M.G., Reeves R.K.,
Blaber M., Windebank A.J., Rodriguez M.;
"Dynamic role of kallikrein 6 in traumatic spinal cord injury.";
Eur. J. Neurosci. 24:1457-1469(2006).
[20]
FUNCTION, AND ENZYME REGULATION.
PubMed=16321973; DOI=10.1074/jbc.M510096200;
Angelo P.F., Lima A.R., Alves F.M., Blaber S.I., Scarisbrick I.A.,
Blaber M., Juliano L., Juliano M.A.;
"Substrate specificity of human kallikrein 6: salt and
glycosaminoglycan activation effects.";
J. Biol. Chem. 281:3116-3126(2006).
[21]
AUTOCATALYTIC CLEAVAGE.
PubMed=17417874; DOI=10.1021/bi6025006;
Blaber S.I., Yoon H., Scarisbrick I.A., Juliano M.A., Blaber M.;
"The autolytic regulation of human kallikrein-related peptidase 6.";
Biochemistry 46:5209-5217(2007).
[22]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 21-243, AUTOCATALYTIC
CLEAVAGE, ACTIVE SITES, AND DISULFIDE BONDS.
PubMed=12016211; DOI=10.1074/jbc.M201534200;
Gomis-Rueth F.X., Bayes A., Sotiropoulou G., Pampalakis G.,
Tsetsenis T., Villegas V., Aviles F.X., Coll M.;
"The structure of human prokallikrein 6 reveals a novel activation
mechanism for the kallikrein family.";
J. Biol. Chem. 277:27273-27281(2002).
[23]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 22-244, PROTEIN SEQUENCE OF
22-25, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AUTOCATALYTIC
CLEAVAGE, DISULFIDE BONDS, AND MASS SPECTROMETRY.
PubMed=11983703; DOI=10.1074/jbc.M202392200;
Bernett M.J., Blaber S.I., Scarisbrick I.A., Dhanarajan P.,
Thompson S.M., Blaber M.;
"Crystal structure and biochemical characterization of human
kallikrein 6 reveals that a trypsin-like kallikrein is expressed in
the central nervous system.";
J. Biol. Chem. 277:24562-24570(2002).
-!- FUNCTION: Serine protease which exhibits a preference for Arg over
Lys in the substrate P1 position and for Ser or Pro in the P2
position. Shows activity against amyloid precursor protein, myelin
basic protein, gelatin, casein and extracellular matrix proteins
such as fibronectin, laminin, vitronectin and collagen. Degrades
alpha-synuclein and prevents its polymerization, indicating that
it may be involved in the pathogenesis of Parkinson disease and
other synucleinopathies. May be involved in regulation of axon
outgrowth following spinal cord injury. Tumor cells treated with a
neutralizing KLK6 antibody migrate less than control cells,
suggesting a role in invasion and metastasis.
{ECO:0000269|PubMed:11983703, ECO:0000269|PubMed:12878203,
ECO:0000269|PubMed:12928483, ECO:0000269|PubMed:15557757,
ECO:0000269|PubMed:16321973, ECO:0000269|PubMed:16987227}.
-!- ENZYME REGULATION: Inhibited by a range of serine protease
inhibitors including soybean trypsin inhibitor, benzamidine and
serpins. Activated by a range of glycosaminoglycans including
chondroitin sulfate, dermatan sulfate, heparan sulfate and
heparin. {ECO:0000269|PubMed:12878203,
ECO:0000269|PubMed:16321973}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1562 uM for Tosyl-Gly-Pro-Arg-AMC
{ECO:0000269|PubMed:11983703, ECO:0000269|PubMed:12878203};
KM=777 uM for Tosyl-Gly-Pro-Lys-AMC
{ECO:0000269|PubMed:11983703, ECO:0000269|PubMed:12878203};
KM=0.410 mM for Phe-Ser-Arg-AMC {ECO:0000269|PubMed:11983703,
ECO:0000269|PubMed:12878203};
KM=0.455 mM for Gly-Gly-Arg-AMC {ECO:0000269|PubMed:11983703,
ECO:0000269|PubMed:12878203};
KM=0.335 mM for Asp-Pro-Arg-AMC {ECO:0000269|PubMed:11983703,
ECO:0000269|PubMed:12878203};
KM=0.758 mM for Gln-Gly-Arg-AMC {ECO:0000269|PubMed:11983703,
ECO:0000269|PubMed:12878203};
KM=0.625 mM for Pro-Phe-Arg-AMC {ECO:0000269|PubMed:11983703,
ECO:0000269|PubMed:12878203};
KM=0.271 mM for Val-Pro-Arg-AMC {ECO:0000269|PubMed:11983703,
ECO:0000269|PubMed:12878203};
KM=1.72 mM for Val-Leu-Lys-AMC {ECO:0000269|PubMed:11983703,
ECO:0000269|PubMed:12878203};
-!- SUBCELLULAR LOCATION: Secreted. Nucleus, nucleolus. Cytoplasm.
Mitochondrion. Microsome. Note=In brain, detected in the nucleus
of glial cells and in the nucleus and cytoplasm of neurons.
Detected in the mitochondrial and microsomal fractions of HEK-293
cells and released into the cytoplasm following cell stress.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q92876-1; Sequence=Displayed;
Name=2;
IsoId=Q92876-2; Sequence=VSP_034403;
Name=3;
IsoId=Q92876-3; Sequence=VSP_034404, VSP_034405;
-!- TISSUE SPECIFICITY: In fluids, highest levels found in milk of
lactating women followed by cerebrospinal fluid, nipple aspirate
fluid and breast cyst fluid. Also found in serum, seminal plasma
and some amniotic fluids and breast tumor cytosolic extracts. Not
detected in urine. At the tissue level, highest concentrations
found in glandular tissues such as salivary glands followed by
lung, colon, fallopian tube, placenta, breast, pituitary and
kidney. Not detected in skin, spleen, bone, thyroid, heart,
ureter, liver, muscle, endometrium, testis, pancreas, seminal
vesicle, ovary, adrenals and prostate. In brain, detected in gray
matter neurons (at protein level). Colocalizes with pathological
inclusions such as Lewy bodies and glial cytoplasmic inclusions.
Overexpressed in primary breast tumors but not expressed in
metastatic tumors. {ECO:0000269|PubMed:10997858,
ECO:0000269|PubMed:11018688, ECO:0000269|PubMed:11668196,
ECO:0000269|PubMed:12928483, ECO:0000269|PubMed:16800739}.
-!- INDUCTION: By spinal cord injury. This effect is particularly
prominent in macrophages, microglia and reactive astrocytes.
{ECO:0000269|PubMed:16987227}.
-!- PTM: Inactivated by autolytic cleavage after Arg-80.
-!- MASS SPECTROMETRY: Mass=25866; Method=MALDI; Range=22-244;
Evidence={ECO:0000269|PubMed:11983703};
-!- SIMILARITY: Belongs to the peptidase S1 family. Kallikrein
subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}.
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EMBL; U62801; AAB07113.1; -; mRNA.
EMBL; D78203; BAA11306.1; -; mRNA.
EMBL; AF013988; AAB66483.1; -; mRNA.
EMBL; AF149289; AAD51475.1; -; Genomic_DNA.
EMBL; AF243527; AAG33359.1; -; Genomic_DNA.
EMBL; AY318867; AAP82446.1; -; mRNA.
EMBL; AY318868; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AY318869; AAP82448.1; -; mRNA.
EMBL; AY318870; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; DQ223012; ABB04464.1; -; mRNA.
EMBL; AK314897; BAG37411.1; -; mRNA.
EMBL; BT006852; AAP35498.1; -; mRNA.
EMBL; AC011483; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471135; EAW71953.1; -; Genomic_DNA.
EMBL; CH471135; EAW71954.1; -; Genomic_DNA.
EMBL; BC015525; AAH15525.1; -; mRNA.
CCDS; CCDS12811.1; -. [Q92876-1]
CCDS; CCDS42599.1; -. [Q92876-2]
RefSeq; NP_001012982.1; NM_001012964.2. [Q92876-1]
RefSeq; NP_001012983.1; NM_001012965.2. [Q92876-2]
RefSeq; NP_001306877.1; NM_001319948.1. [Q92876-2]
RefSeq; NP_001306878.1; NM_001319949.1. [Q92876-2]
RefSeq; NP_002765.1; NM_002774.3. [Q92876-1]
UniGene; Hs.79361; -.
PDB; 1GVL; X-ray; 1.80 A; A=21-243.
PDB; 1L2E; X-ray; 1.75 A; A=22-244.
PDB; 1LO6; X-ray; 1.56 A; A=22-237.
PDB; 3VFE; X-ray; 1.88 A; A=22-244.
PDB; 4D8N; X-ray; 1.68 A; A=22-244.
PDBsum; 1GVL; -.
PDBsum; 1L2E; -.
PDBsum; 1LO6; -.
PDBsum; 3VFE; -.
PDBsum; 4D8N; -.
ProteinModelPortal; Q92876; -.
SMR; Q92876; -.
BioGrid; 111634; 12.
IntAct; Q92876; 16.
STRING; 9606.ENSP00000309148; -.
BindingDB; Q92876; -.
ChEMBL; CHEMBL4448; -.
DrugBank; DB03127; Benzamidine.
GuidetoPHARMACOLOGY; 2376; -.
MEROPS; S01.236; -.
PhosphoSitePlus; Q92876; -.
UniCarbKB; Q92876; -.
BioMuta; KLK6; -.
DMDM; 3914480; -.
MaxQB; Q92876; -.
PaxDb; Q92876; -.
PeptideAtlas; Q92876; -.
PRIDE; Q92876; -.
DNASU; 5653; -.
Ensembl; ENST00000310157; ENSP00000309148; ENSG00000167755. [Q92876-1]
Ensembl; ENST00000376851; ENSP00000366047; ENSG00000167755. [Q92876-1]
Ensembl; ENST00000391808; ENSP00000375684; ENSG00000167755. [Q92876-2]
Ensembl; ENST00000594641; ENSP00000470482; ENSG00000167755. [Q92876-1]
Ensembl; ENST00000597379; ENSP00000469630; ENSG00000167755. [Q92876-3]
Ensembl; ENST00000599881; ENSP00000471948; ENSG00000167755. [Q92876-3]
GeneID; 5653; -.
KEGG; hsa:5653; -.
UCSC; uc002pui.4; human. [Q92876-1]
CTD; 5653; -.
DisGeNET; 5653; -.
EuPathDB; HostDB:ENSG00000167755.13; -.
GeneCards; KLK6; -.
HGNC; HGNC:6367; KLK6.
HPA; HPA051837; -.
MIM; 602652; gene.
neXtProt; NX_Q92876; -.
OpenTargets; ENSG00000167755; -.
PharmGKB; PA30156; -.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00760000118862; -.
HOGENOM; HOG000251820; -.
HOVERGEN; HBG013304; -.
InParanoid; Q92876; -.
KO; K08667; -.
OMA; AWAEEQN; -.
OrthoDB; EOG091G0G5F; -.
PhylomeDB; Q92876; -.
TreeFam; TF331065; -.
BRENDA; 3.4.21.104; 2681.
BRENDA; 3.4.21.34; 2681.
BRENDA; 3.4.21.B10; 2681.
SABIO-RK; Q92876; -.
ChiTaRS; KLK6; human.
EvolutionaryTrace; Q92876; -.
GeneWiki; KLK6; -.
GenomeRNAi; 5653; -.
PMAP-CutDB; Q92876; -.
PRO; PR:Q92876; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000167755; -.
CleanEx; HS_KLK6; -.
ExpressionAtlas; Q92876; baseline and differential.
Genevisible; Q92876; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0030141; C:secretory granule; IBA:GO_Central.
GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
GO; GO:0042982; P:amyloid precursor protein metabolic process; NAS:UniProtKB.
GO; GO:0007417; P:central nervous system development; NAS:UniProtKB.
GO; GO:0030574; P:collagen catabolic process; NAS:UniProtKB.
GO; GO:0042445; P:hormone metabolic process; NAS:UniProtKB.
GO; GO:0042552; P:myelination; NAS:UniProtKB.
GO; GO:0070997; P:neuron death; IMP:UniProtKB.
GO; GO:0045745; P:positive regulation of G-protein coupled receptor protein signaling pathway; IDA:UniProtKB.
GO; GO:0016540; P:protein autoprocessing; NAS:UniProtKB.
GO; GO:0045595; P:regulation of cell differentiation; NAS:UniProtKB.
GO; GO:0010975; P:regulation of neuron projection development; IEA:Ensembl.
GO; GO:0009611; P:response to wounding; NAS:UniProtKB.
GO; GO:0042246; P:tissue regeneration; 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; Autocatalytic cleavage;
Cleavage on pair of basic residues; Complete proteome; Cytoplasm;
Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
Glycoprotein; Hydrolase; Microsome; Mitochondrion; Nucleus;
Polymorphism; Protease; Reference proteome; Secreted; Serine protease;
Signal; Zymogen.
SIGNAL 1 16 {ECO:0000255}.
PROPEP 17 21 Activation peptide. {ECO:0000255}.
/FTId=PRO_0000027940.
CHAIN 22 244 Kallikrein-6.
/FTId=PRO_0000027941.
DOMAIN 22 242 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 62 62 Charge relay system.
{ECO:0000269|PubMed:12016211}.
ACT_SITE 106 106 Charge relay system.
{ECO:0000269|PubMed:12016211}.
ACT_SITE 197 197 Charge relay system.
{ECO:0000269|PubMed:12016211}.
SITE 80 81 Cleavage; by autolysis.
CARBOHYD 134 134 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 28 157
DISULFID 47 63
DISULFID 131 231
DISULFID 138 203
DISULFID 168 182
DISULFID 193 218
VAR_SEQ 1 107 Missing (in isoform 2).
{ECO:0000303|PubMed:15207701}.
/FTId=VSP_034403.
VAR_SEQ 14 40 AWAEEQNKLVHGGPCDKTSHPYQAALY -> GIFRSSWGSI
TFGKGRVPRSRVLLSGL (in isoform 3).
{ECO:0000303|PubMed:15207701}.
/FTId=VSP_034404.
VAR_SEQ 41 244 Missing (in isoform 3).
{ECO:0000303|PubMed:15207701}.
/FTId=VSP_034405.
VARIANT 78 78 R -> W (in dbSNP:rs61469141).
/FTId=VAR_061776.
HELIX 27 29 {ECO:0000244|PDB:1GVL}.
STRAND 36 41 {ECO:0000244|PDB:1LO6}.
STRAND 44 53 {ECO:0000244|PDB:1LO6}.
STRAND 56 59 {ECO:0000244|PDB:1LO6}.
HELIX 61 63 {ECO:0000244|PDB:1LO6}.
STRAND 69 73 {ECO:0000244|PDB:1LO6}.
STRAND 75 77 {ECO:0000244|PDB:1GVL}.
STRAND 85 94 {ECO:0000244|PDB:1LO6}.
TURN 100 102 {ECO:0000244|PDB:1LO6}.
STRAND 108 114 {ECO:0000244|PDB:1LO6}.
STRAND 137 144 {ECO:0000244|PDB:1LO6}.
STRAND 146 149 {ECO:0000244|PDB:1GVL}.
STRAND 156 163 {ECO:0000244|PDB:1LO6}.
HELIX 165 171 {ECO:0000244|PDB:1LO6}.
TURN 173 175 {ECO:0000244|PDB:1LO6}.
STRAND 180 184 {ECO:0000244|PDB:1LO6}.
TURN 186 188 {ECO:0000244|PDB:1LO6}.
TURN 194 198 {ECO:0000244|PDB:1LO6}.
STRAND 200 203 {ECO:0000244|PDB:1LO6}.
STRAND 206 213 {ECO:0000244|PDB:1LO6}.
STRAND 221 223 {ECO:0000244|PDB:1LO6}.
STRAND 225 229 {ECO:0000244|PDB:1LO6}.
HELIX 230 233 {ECO:0000244|PDB:1LO6}.
HELIX 234 237 {ECO:0000244|PDB:1LO6}.
SEQUENCE 244 AA; 26856 MW; AEA03F9145D87AAB CRC64;
MKKLMVVLSL IAAAWAEEQN KLVHGGPCDK TSHPYQAALY TSGHLLCGGV LIHPLWVLTA
AHCKKPNLQV FLGKHNLRQR ESSQEQSSVV RAVIHPDYDA ASHDQDIMLL RLARPAKLSE
LIQPLPLERD CSANTTSCHI LGWGKTADGD FPDTIQCAYI HLVSREECEH AYPGQITQNM
LCAGDEKYGK DSCQGDSGGP LVCGDHLRGL VSWGNIPCGS KEKPGVYTNV CRYTNWIQKT
IQAK


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