KLK8_HUMAN
ID KLK8_HUMAN Reviewed; 260 AA.
AC O60259; Q5V9X1; Q5V9X2; Q8IW69; Q9HCB3; Q9NR68; Q9NR69; Q9UIL9; Q9UQ47;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Kallikrein-8;
DE Short=hK8;
DE EC=3.4.21.118;
DE AltName: Full=Neuropsin;
DE Short=NP;
DE AltName: Full=Ovasin;
DE AltName: Full=Serine protease 19;
DE AltName: Full=Serine protease TADG-14;
DE AltName: Full=Tumor-associated differentially expressed gene 14 protein;
DE Flags: Precursor;
GN Name=KLK8; Synonyms=NRPN, PRSS19, TADG14; ORFNames=UNQ283/PRO322;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RC TISSUE=Hippocampus;
RX PubMed=9714609; DOI=10.1016/s0378-1119(98)00232-7;
RA Yoshida S., Taniguchi M., Hirata A., Shiosaka S.;
RT "Sequence analysis and expression of human neuropsin cDNA and gene.";
RL Gene 213:9-16(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Ovary;
RX PubMed=10485494;
RA Underwood L.J., Tanimoto H., Wang Y., Shigemasa K., Parmley T.H.,
RA O'Brien T.J.;
RT "Cloning of tumor-associated differentially expressed gene-14, a novel
RT serine protease overexpressed by ovarian carcinoma.";
RL Cancer Res. 59:4435-4439(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
RX PubMed=10102990; DOI=10.1046/j.1432-1327.1999.00213.x;
RA Mitsui S., Tsuruoka N., Yamashiro K., Nakazato H., Yamaguchi N.;
RT "A novel form of human neuropsin, a brain-related serine protease, is
RT generated by alternative splicing and is expressed preferentially in human
RT adult brain.";
RL Eur. J. Biochem. 260:627-634(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11054574; DOI=10.1016/s0378-1119(00)00382-6;
RA Gan L., Lee I., Smith R., Argonza-Barrett R., Lei H., McCuaig J., Moss P.,
RA Paeper B., Wang K.;
RT "Sequencing and expression analysis of the serine protease gene cluster
RT located in chromosome 19q13 region.";
RL Gene 257:119-130(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 3 AND 4), AND TISSUE
RP SPECIFICITY.
RX PubMed=11309326;
RA Magklara A., Scorilas A., Katsaros D., Massobrio M., Yousef G.M.,
RA Fracchioli S., Danese S., Diamandis E.P.;
RT "The human KLK8 (neuropsin/ovasin) gene: identification of two novel splice
RT variants and its prognostic value in ovarian cancer.";
RL Clin. Cancer Res. 7:806-811(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RA Gan L., Gelinas R., Gown A.M., Moss P., Smith R., Wang K.;
RT "Molecular cloning and characterization of a novel serine protease, ovasin,
RT a potential molecular marker for ovarian carcinomas.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA Michael I.P., Diamandis E.P.;
RT "Human kallikrein 8 and human kallikrein 9 are organized as a bicistronic
RT operon.";
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [12]
RP PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
RX PubMed=15282331; DOI=10.1093/molbev/msh220;
RA Li Y., Qian Y.-P., Yu X.-J., Wang Y.-Q., Dong D.-G., Sun W., Ma R.-M.,
RA Su B.;
RT "Recent origin of a hominoid-specific splice form of neuropsin, a gene
RT involved in learning and memory.";
RL Mol. Biol. Evol. 21:2111-2115(2004).
RN [13]
RP TISSUE SPECIFICITY.
RX PubMed=11522960; DOI=10.1097/00001756-200108280-00031;
RA Shimizu-Okabe C., Yousef G.M., Diamandis E.P., Yoshida S., Shiosaka S.,
RA Fahnestock M.;
RT "Expression of the kallikrein gene family in normal and Alzheimer's disease
RT brain.";
RL NeuroReport 12:2747-2751(2001).
RN [14]
RP TISSUE SPECIFICITY.
RX PubMed=12147714; DOI=10.1136/mp.55.4.235;
RA Kuwae K., Matsumoto-Miyai K., Yoshida S., Sadayama T., Yoshikawa K.,
RA Hosokawa K., Shiosaka S.;
RT "Epidermal expression of serine protease, neuropsin (KLK8) in normal and
RT pathological skin samples.";
RL Mol. Pathol. 55:235-241(2002).
RN [15]
RP USE AS A MARKER FOR OVARIAN CANCER.
RX PubMed=12782581;
RA Kishi T., Grass L., Soosaipillai A., Scorilas A., Harbeck N.,
RA Schmalfeldt B., Dorn J., Mysliwiec M., Schmitt M., Diamandis E.P.;
RT "Human kallikrein 8, a novel biomarker for ovarian carcinoma.";
RL Cancer Res. 63:2771-2774(2003).
RN [16]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=16337200; DOI=10.1016/j.febslet.2005.11.039;
RA Rajapakse S., Ogiwara K., Takano N., Moriyama A., Takahashi T.;
RT "Biochemical characterization of human kallikrein 8 and its possible
RT involvement in the degradation of extracellular matrix proteins.";
RL FEBS Lett. 579:6879-6884(2005).
RN [17]
RP ALTERNATIVE SPLICING (ISOFORM 2).
RX PubMed=17487847; DOI=10.1002/humu.20547;
RA Lu Z.-X., Peng J., Su B.;
RT "A human-specific mutation leads to the origin of a novel splice form of
RT neuropsin (KLK8), a gene involved in learning and memory.";
RL Hum. Mutat. 28:978-984(2007).
RN [18]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17761692; DOI=10.1093/jb/mvm156;
RA Scott F.L., Sun J., Whisstock J.C., Kato K., Bird P.I.;
RT "SerpinB6 is an inhibitor of kallikrein-8 in keratinocytes.";
RL J. Biochem. 142:435-442(2007).
RN [19]
RP INTERACTION WITH SPINK9.
RX PubMed=19194479; DOI=10.1038/jid.2008.448;
RA Brattsand M., Stefansson K., Hubiche T., Nilsson S.K., Egelrud T.;
RT "SPINK9: a selective, skin-specific Kazal-type serine protease inhibitor.";
RL J. Invest. Dermatol. 129:1656-1665(2009).
CC -!- FUNCTION: Serine protease which is capable of degrading a number of
CC proteins such as casein, fibrinogen, kininogen, fibronectin and
CC collagen type IV. Also cleaves L1CAM in response to increased neural
CC activity. Induces neurite outgrowth and fasciculation of cultured
CC hippocampal neurons. Plays a role in the formation and maturation of
CC orphan and small synaptic boutons in the Schaffer-collateral pathway,
CC regulates Schaffer-collateral long-term potentiation in the hippocampus
CC and is required for memory acquisition and synaptic plasticity.
CC Involved in skin desquamation and keratinocyte proliferation. Plays a
CC role in the secondary phase of pathogenesis following spinal cord
CC injury. {ECO:0000269|PubMed:16337200}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of amide substrates following the basic amino acids
CC Arg or Lys at the P1 position, with a preference for Arg over Lys.;
CC EC=3.4.21.118; Evidence={ECO:0000269|PubMed:16337200};
CC -!- ACTIVITY REGULATION: Inhibited by a range of serine protease inhibitors
CC including antipain, aprotinin, leupeptin, benzamidine and soybean
CC trypsin inhibitor. {ECO:0000269|PubMed:16337200}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.07 mM for Pro-Phe-Arg-MCA {ECO:0000269|PubMed:16337200};
CC KM=0.07 mM for Z-Val-Val-Arg-MCA {ECO:0000269|PubMed:16337200};
CC KM=0.07 mM for Boc-Val-Pro-Arg-MCA {ECO:0000269|PubMed:16337200};
CC KM=0.10 mM for Boc-Leu-Lys-Arg-MCA {ECO:0000269|PubMed:16337200};
CC KM=0.10 mM for Boc-Val-Leu-Lys-MCA {ECO:0000269|PubMed:16337200};
CC KM=0.07 mM for Boc-Phe-Ser-Arg-MCA {ECO:0000269|PubMed:16337200};
CC Vmax=7.1 umol/min/mg enzyme toward Pro-Phe-Arg-MCA
CC {ECO:0000269|PubMed:16337200};
CC Vmax=5.4 umol/min/mg enzyme toward Z-Val-Val-Arg-MCA
CC {ECO:0000269|PubMed:16337200};
CC Vmax=3.9 umol/min/mg enzyme toward Boc-Val-Pro-Arg-MCA
CC {ECO:0000269|PubMed:16337200};
CC Vmax=2.6 umol/min/mg enzyme toward Boc-Leu-Lys-Arg-MCA
CC {ECO:0000269|PubMed:16337200};
CC Vmax=1.9 umol/min/mg enzyme toward Boc-Val-Leu-Lys-MCA
CC {ECO:0000269|PubMed:16337200};
CC Vmax=1.6 umol/min/mg enzyme toward Boc-Phe-Ser-Arg-MCA
CC {ECO:0000269|PubMed:16337200};
CC pH dependence:
CC Optimum pH is 8.5. Active from pH 7-10.
CC {ECO:0000269|PubMed:16337200};
CC -!- SUBUNIT: Interacts with SPINK9. {ECO:0000269|PubMed:19194479}.
CC -!- INTERACTION:
CC O60259; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-3915857, EBI-3867333;
CC O60259; P42858: HTT; NbExp=3; IntAct=EBI-3915857, EBI-466029;
CC O60259; Q92876: KLK6; NbExp=3; IntAct=EBI-3915857, EBI-2432309;
CC O60259; Q15323: KRT31; NbExp=3; IntAct=EBI-3915857, EBI-948001;
CC O60259; O76011: KRT34; NbExp=3; IntAct=EBI-3915857, EBI-1047093;
CC O60259; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-3915857, EBI-11959885;
CC O60259; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-3915857, EBI-10171774;
CC O60259; P26371: KRTAP5-9; NbExp=3; IntAct=EBI-3915857, EBI-3958099;
CC O60259; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-3915857, EBI-945833;
CC O60259; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-3915857, EBI-22310682;
CC O60259; P50454: SERPINH1; NbExp=3; IntAct=EBI-3915857, EBI-350723;
CC O60259; P37173: TGFBR2; NbExp=3; IntAct=EBI-3915857, EBI-296151;
CC O60259; Q8IUH5: ZDHHC17; NbExp=3; IntAct=EBI-3915857, EBI-524753;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17761692}. Cytoplasm
CC {ECO:0000269|PubMed:17761692}. Note=Shows a cytoplasmic distribution in
CC the keratinocytes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=O60259-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O60259-2; Sequence=VSP_005401;
CC Name=3;
CC IsoId=O60259-3; Sequence=VSP_030350;
CC Name=4;
CC IsoId=O60259-4; Sequence=VSP_030351, VSP_030352;
CC -!- TISSUE SPECIFICITY: Isoform 1 is predominantly expressed in the
CC pancreas. Isoform 2 is expressed in adult brain and hippocampus.
CC Isoform 1 and isoform 2 are found in fetal brain and placenta. Detected
CC in salivary gland, uterus, thymus, breast, testis and kidney but not in
CC spleen, liver, lung or normal ovarian tissue. Displays an 11.5-fold
CC increase in Alzheimer disease hippocampus compared to controls and is
CC overexpressed in some ovarian carcinomas. Expressed at low levels in
CC normal skin while high levels are found in psoriasis vulgaris,
CC seborrheic keratosis, lichen planus and squamous cell carcinoma skin
CC samples. Expressed in the keratinocytes. {ECO:0000269|PubMed:11309326,
CC ECO:0000269|PubMed:11522960, ECO:0000269|PubMed:12147714,
CC ECO:0000269|PubMed:17761692}.
CC -!- MISCELLANEOUS: Expressed at high levels in serum, ascites fluid and
CC tumor cytosol of advanced stage ovarian cancer patients and may serve
CC as a marker of ovarian cancer.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced as a result of a human-specific
CC mutation which is not found in other primates. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Kallikrein subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/KLK8ID41088ch19q13.html";
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DR EMBL; AB009849; BAA28673.1; -; mRNA.
DR EMBL; AB012761; BAA28676.1; -; Genomic_DNA.
DR EMBL; AF055982; AAD56050.1; -; mRNA.
DR EMBL; AB008390; BAA82665.1; -; mRNA.
DR EMBL; AB008927; BAA82666.1; -; mRNA.
DR EMBL; AB010780; BAA88684.1; -; Genomic_DNA.
DR EMBL; AF243527; AAG33361.1; -; Genomic_DNA.
DR EMBL; AF251125; AAF79144.1; -; Genomic_DNA.
DR EMBL; AF251125; AAF79145.1; -; Genomic_DNA.
DR EMBL; AF095742; AAD25979.1; -; mRNA.
DR EMBL; AF095743; AAD29574.1; -; Genomic_DNA.
DR EMBL; DQ267420; ABB83339.1; -; mRNA.
DR EMBL; AY359036; AAQ89395.1; -; mRNA.
DR EMBL; AC011473; AAG23254.1; -; Genomic_DNA.
DR EMBL; AC011483; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471135; EAW71962.1; -; Genomic_DNA.
DR EMBL; BC040887; AAH40887.1; -; mRNA.
DR EMBL; AY563055; AAT76913.1; -; Genomic_DNA.
DR EMBL; AY563055; AAT76914.1; -; Genomic_DNA.
DR EMBL; AY563056; AAT76915.1; -; Genomic_DNA.
DR EMBL; AY563056; AAT76916.1; -; Genomic_DNA.
DR EMBL; AY563057; AAT76917.1; -; Genomic_DNA.
DR EMBL; AY563057; AAT76918.1; -; Genomic_DNA.
DR EMBL; AY563058; AAT76919.1; -; Genomic_DNA.
DR EMBL; AY563058; AAT76920.1; -; Genomic_DNA.
DR EMBL; AY563059; AAT76921.1; -; Genomic_DNA.
DR EMBL; AY563059; AAT76922.1; -; Genomic_DNA.
DR EMBL; AY563060; AAT76923.1; -; Genomic_DNA.
DR EMBL; AY563060; AAT76924.1; -; Genomic_DNA.
DR EMBL; AY563061; AAT76925.1; -; Genomic_DNA.
DR EMBL; AY563061; AAT76926.1; -; Genomic_DNA.
DR EMBL; AY563062; AAT76927.1; -; Genomic_DNA.
DR EMBL; AY563062; AAT76928.1; -; Genomic_DNA.
DR EMBL; AY563063; AAT76929.1; -; Genomic_DNA.
DR EMBL; AY563063; AAT76930.1; -; Genomic_DNA.
DR EMBL; AY563064; AAT76931.1; -; Genomic_DNA.
DR EMBL; AY563064; AAT76932.1; -; Genomic_DNA.
DR EMBL; AY563065; AAT76933.1; -; Genomic_DNA.
DR EMBL; AY563065; AAT76934.1; -; Genomic_DNA.
DR EMBL; AY563066; AAT76935.1; -; Genomic_DNA.
DR EMBL; AY563066; AAT76936.1; -; Genomic_DNA.
DR EMBL; AY563067; AAT76937.1; -; Genomic_DNA.
DR EMBL; AY563067; AAT76938.1; -; Genomic_DNA.
DR CCDS; CCDS12813.1; -. [O60259-1]
DR CCDS; CCDS12814.1; -. [O60259-3]
DR CCDS; CCDS12815.1; -. [O60259-4]
DR CCDS; CCDS42600.1; -. [O60259-2]
DR RefSeq; NP_001268360.1; NM_001281431.1.
DR RefSeq; NP_009127.1; NM_007196.3. [O60259-1]
DR RefSeq; NP_653088.1; NM_144505.2. [O60259-2]
DR RefSeq; NP_653089.1; NM_144506.2. [O60259-3]
DR RefSeq; NP_653090.1; NM_144507.2. [O60259-4]
DR PDB; 5MS3; X-ray; 2.30 A; A=33-260.
DR PDB; 5MS4; X-ray; 2.10 A; A/B/C/D=33-260.
DR PDBsum; 5MS3; -.
DR PDBsum; 5MS4; -.
DR AlphaFoldDB; O60259; -.
DR SMR; O60259; -.
DR BioGRID; 116371; 44.
DR IntAct; O60259; 20.
DR BindingDB; O60259; -.
DR ChEMBL; CHEMBL4812; -.
DR GuidetoPHARMACOLOGY; 2378; -.
DR MEROPS; S01.244; -.
DR GlyGen; O60259; 1 site.
DR PhosphoSitePlus; O60259; -.
DR BioMuta; KLK8; -.
DR EPD; O60259; -.
DR MassIVE; O60259; -.
DR PeptideAtlas; O60259; -.
DR PRIDE; O60259; -.
DR ProteomicsDB; 49286; -. [O60259-1]
DR ProteomicsDB; 49287; -. [O60259-2]
DR ProteomicsDB; 49288; -. [O60259-3]
DR Antibodypedia; 32417; 1304 antibodies from 32 providers.
DR DNASU; 11202; -.
DR Ensembl; ENST00000320838.9; ENSP00000325072.5; ENSG00000129455.15. [O60259-4]
DR Ensembl; ENST00000347619.8; ENSP00000341555.3; ENSG00000129455.15. [O60259-3]
DR Ensembl; ENST00000391806.6; ENSP00000375682.1; ENSG00000129455.15. [O60259-2]
DR Ensembl; ENST00000593490.1; ENSP00000469278.1; ENSG00000129455.15. [O60259-4]
DR Ensembl; ENST00000600767.5; ENSP00000472016.1; ENSG00000129455.15. [O60259-1]
DR GeneID; 11202; -.
DR KEGG; hsa:11202; -.
DR UCSC; uc002puq.2; human. [O60259-1]
DR CTD; 11202; -.
DR DisGeNET; 11202; -.
DR GeneCards; KLK8; -.
DR HGNC; HGNC:6369; KLK8.
DR HPA; ENSG00000129455; Group enriched (esophagus, skin, vagina).
DR MIM; 605644; gene.
DR neXtProt; NX_O60259; -.
DR OpenTargets; ENSG00000129455; -.
DR PharmGKB; PA30158; -.
DR VEuPathDB; HostDB:ENSG00000129455; -.
DR GeneTree; ENSGT01020000230389; -.
DR HOGENOM; CLU_006842_1_1_1; -.
DR InParanoid; O60259; -.
DR OMA; GQECKPH; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; O60259; -.
DR TreeFam; TF331065; -.
DR BRENDA; 3.4.21.118; 2681.
DR PathwayCommons; O60259; -.
DR Reactome; R-HSA-6809371; Formation of the cornified envelope.
DR SignaLink; O60259; -.
DR BioGRID-ORCS; 11202; 10 hits in 1066 CRISPR screens.
DR GeneWiki; KLK8; -.
DR GenomeRNAi; 11202; -.
DR Pharos; O60259; Tchem.
DR PRO; PR:O60259; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O60259; protein.
DR Bgee; ENSG00000129455; Expressed in lower esophagus mucosa and 102 other tissues.
DR ExpressionAtlas; O60259; baseline and differential.
DR Genevisible; O60259; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0030141; C:secretory granule; IBA:GO_Central.
DR GO; GO:0097180; C:serine protease inhibitor complex; IDA:BHF-UCL.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0008219; P:cell death; ISS:UniProtKB.
DR GO; GO:0043616; P:keratinocyte proliferation; ISS:UniProtKB.
DR GO; GO:0007613; P:memory; ISS:UniProtKB.
DR GO; GO:0048681; P:negative regulation of axon regeneration; ISS:UniProtKB.
DR GO; GO:0031642; P:negative regulation of myelination; ISS:UniProtKB.
DR GO; GO:0048812; P:neuron projection morphogenesis; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0050807; P:regulation of synapse organization; ISS:UniProtKB.
DR GO; GO:0009611; P:response to wounding; ISS:UniProtKB.
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 InterPro; IPR033116; TRYPSIN_SER.
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.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Disulfide bond;
KW Glycoprotein; Hydrolase; Protease; Reference proteome; Secreted;
KW Serine protease; Signal; Zymogen.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT PROPEP 29..32
FT /evidence="ECO:0000250"
FT /id="PRO_0000027946"
FT CHAIN 33..260
FT /note="Kallikrein-8"
FT /id="PRO_0000027947"
FT DOMAIN 33..257
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 73
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 120
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 212
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 39..173
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 58..74
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 145..246
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 152..218
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 184..198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 208..233
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT VAR_SEQ 23
FT /note="A -> AACGSLDLLTKLYAENLPCVHLNPQWPSQPSHCPRGWRSNPLPPAA
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10102990"
FT /id="VSP_005401"
FT VAR_SEQ 24..164
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.7"
FT /id="VSP_030350"
FT VAR_SEQ 25..32
FT /note="HSRAQEDK -> RFWRPPGV (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_030351"
FT VAR_SEQ 33..260
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_030352"
FT VARIANT 154
FT /note="V -> I (in dbSNP:rs16988799)"
FT /id="VAR_051855"
FT CONFLICT 195
FT /note="G -> V (in Ref. 11; AAH40887)"
FT /evidence="ECO:0000305"
FT STRAND 47..54
FT /evidence="ECO:0007829|PDB:5MS4"
FT STRAND 56..64
FT /evidence="ECO:0007829|PDB:5MS4"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:5MS4"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:5MS4"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:5MS4"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:5MS4"
FT STRAND 96..105
FT /evidence="ECO:0007829|PDB:5MS4"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:5MS3"
FT STRAND 122..128
FT /evidence="ECO:0007829|PDB:5MS4"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:5MS4"
FT STRAND 151..158
FT /evidence="ECO:0007829|PDB:5MS4"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:5MS4"
FT STRAND 172..178
FT /evidence="ECO:0007829|PDB:5MS4"
FT HELIX 181..187
FT /evidence="ECO:0007829|PDB:5MS4"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:5MS4"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:5MS4"
FT STRAND 215..228
FT /evidence="ECO:0007829|PDB:5MS4"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:5MS3"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:5MS4"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:5MS4"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:5MS4"
FT HELIX 249..257
FT /evidence="ECO:0007829|PDB:5MS4"
SQ SEQUENCE 260 AA; 28048 MW; EF439E5B8C83E660 CRC64;
MGRPRPRAAK TWMFLLLLGG AWAGHSRAQE DKVLGGHECQ PHSQPWQAAL FQGQQLLCGG
VLVGGNWVLT AAHCKKPKYT VRLGDHSLQN KDGPEQEIPV VQSIPHPCYN SSDVEDHNHD
LMLLQLRDQA SLGSKVKPIS LADHCTQPGQ KCTVSGWGTV TSPRENFPDT LNCAEVKIFP
QKKCEDAYPG QITDGMVCAG SSKGADTCQG DSGGPLVCDG ALQGITSWGS DPCGRSDKPG
VYTNICRYLD WIKKIIGSKG
