ID KLK8_HUMAN Reviewed; 260 AA. AC O60259; Q5V9X1; Q5V9X2; Q8IW69; Q9HCB3; Q9NR68; Q9NR69; Q9UIL9; AC Q9UQ47; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 16-JAN-2019, entry version 168. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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 RT human 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., RA Moss P., Paeper B., Wang K.; RT "Sequencing and expression analysis of the serine protease gene RT cluster 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 RT splice 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, RT ovasin, 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 RT bicistronic 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., RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., RA Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale RT effort to identify novel human secreted and transmembrane proteins: a RT bioinformatics 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., RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M., RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., RA 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., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA 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 RT project: 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., RA Shiosaka S., Fahnestock M.; RT "Expression of the kallikrein gene family in normal and Alzheimer's RT disease 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 RT and 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 RP BIOPHYSICOCHEMICAL 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 RT of 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 RT inhibitor."; RL J. Invest. Dermatol. 129:1656-1665(2009). CC -!- FUNCTION: Serine protease which is capable of degrading a number CC of proteins such as casein, fibrinogen, kininogen, fibronectin and CC collagen type IV. Also cleaves L1CAM in response to increased CC neural activity. Induces neurite outgrowth and fasciculation of CC cultured hippocampal neurons. Plays a role in the formation and CC maturation of orphan and small synaptic boutons in the Schaffer- CC collateral pathway, regulates Schaffer-collateral long-term CC potentiation in the hippocampus and is required for memory CC acquisition and synaptic plasticity. Involved in skin desquamation CC and keratinocyte proliferation. Plays a role in the secondary CC phase of pathogenesis following spinal cord injury. CC {ECO:0000269|PubMed:16337200}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Cleavage of amide substrates following the basic amino CC acids Arg or Lys at the P1 position, with a preference for Arg CC over Lys.; EC=3.4.21.118; CC Evidence={ECO:0000269|PubMed:16337200}; CC -!- ACTIVITY REGULATION: Inhibited by a range of serine protease CC inhibitors including antipain, aprotinin, leupeptin, benzamidine CC and soybean 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 CC {ECO:0000269|PubMed:16337200}; CC KM=0.10 mM for Boc-Leu-Lys-Arg-MCA CC {ECO:0000269|PubMed:16337200}; CC KM=0.10 mM for Boc-Val-Leu-Lys-MCA CC {ECO:0000269|PubMed:16337200}; CC KM=0.07 mM for Boc-Phe-Ser-Arg-MCA CC {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 Q7Z3S9:NOTCH2NLA; NbExp=5; IntAct=EBI-3915857, EBI-945833; CC Q8IUH5:ZDHHC17; NbExp=3; IntAct=EBI-3915857, EBI-524753; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17761692}. CC Cytoplasm {ECO:0000269|PubMed:17761692}. Note=Shows a cytoplasmic CC distribution in 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 Note=Produced as a result of a human-specific mutation which is CC not found in other primates.; 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. CC Detected in salivary gland, uterus, thymus, breast, testis and CC kidney but not in spleen, liver, lung or normal ovarian tissue. CC Displays an 11.5-fold increase in Alzheimer disease hippocampus CC compared to controls and is overexpressed in some ovarian CC carcinomas. Expressed at low levels in normal skin while high CC levels are found in psoriasis vulgaris, seborrheic keratosis, CC lichen planus and squamous cell carcinoma skin samples. Expressed CC 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 CC and tumor cytosol of advanced stage ovarian cancer patients and CC may serve as a marker of ovarian cancer. CC -!- SIMILARITY: Belongs to the peptidase S1 family. Kallikrein CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology CC and Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/KLK8ID41088ch19q13.html"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- 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 UniGene; Hs.104570; -. 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 ProteinModelPortal; O60259; -. DR SMR; O60259; -. DR BioGrid; 116371; 17. DR IntAct; O60259; 9. DR BindingDB; O60259; -. DR ChEMBL; CHEMBL4812; -. DR MEROPS; S01.244; -. DR PhosphoSitePlus; O60259; -. DR BioMuta; KLK8; -. DR EPD; O60259; -. DR PeptideAtlas; O60259; -. DR PRIDE; O60259; -. DR ProteomicsDB; 49286; -. DR ProteomicsDB; 49287; -. [O60259-2] DR ProteomicsDB; 49288; -. [O60259-3] DR ProteomicsDB; 49289; -. [O60259-4] DR DNASU; 11202; -. DR Ensembl; ENST00000320838; ENSP00000325072; ENSG00000129455. [O60259-4] DR Ensembl; ENST00000347619; ENSP00000341555; ENSG00000129455. [O60259-3] DR Ensembl; ENST00000391806; ENSP00000375682; ENSG00000129455. [O60259-2] DR Ensembl; ENST00000593490; ENSP00000469278; ENSG00000129455. [O60259-4] DR Ensembl; ENST00000600767; ENSP00000472016; ENSG00000129455. [O60259-1] DR GeneID; 11202; -. DR KEGG; hsa:11202; -. DR UCSC; uc002puq.2; human. [O60259-1] DR CTD; 11202; -. DR DisGeNET; 11202; -. DR EuPathDB; HostDB:ENSG00000129455.15; -. DR GeneCards; KLK8; -. DR HGNC; HGNC:6369; KLK8. DR HPA; CAB019393; -. DR HPA; HPA035761; -. DR MIM; 605644; gene. DR neXtProt; NX_O60259; -. DR OpenTargets; ENSG00000129455; -. DR PharmGKB; PA30158; -. DR GeneTree; ENSGT00940000153679; -. DR HOVERGEN; HBG013304; -. DR InParanoid; O60259; -. DR KO; K08650; -. DR OMA; TKLYAEN; -. DR OrthoDB; 1314811at2759; -. DR PhylomeDB; O60259; -. DR TreeFam; TF331065; -. DR BRENDA; 3.4.21.118; 2681. DR Reactome; R-HSA-6809371; Formation of the cornified envelope. DR GeneWiki; KLK8; -. DR GenomeRNAi; 11202; -. DR PRO; PR:O60259; -. DR Proteomes; UP000005640; Chromosome 19. DR Bgee; ENSG00000129455; Expressed in 105 organ(s), highest expression level in lower esophagus mucosa. 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:0050807; P:regulation of synapse organization; ISS:UniProtKB. DR GO; GO:0009611; P:response to wounding; ISS:UniProtKB. DR GO; GO:0050808; P:synapse organization; IEA:Ensembl. DR CDD; cd00190; Tryp_SPc; 1. DR InterPro; IPR009003; Peptidase_S1_PA. 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; Complete proteome; Cytoplasm; KW Disulfide bond; Glycoprotein; Hydrolase; Polymorphism; Protease; KW Reference proteome; Secreted; Serine protease; Signal; Zymogen. FT SIGNAL 1 28 {ECO:0000255}. FT PROPEP 29 32 {ECO:0000250}. FT /FTId=PRO_0000027946. FT CHAIN 33 260 Kallikrein-8. FT /FTId=PRO_0000027947. FT DOMAIN 33 257 Peptidase S1. {ECO:0000255|PROSITE- FT ProRule:PRU00274}. FT ACT_SITE 73 73 Charge relay system. {ECO:0000250}. FT ACT_SITE 120 120 Charge relay system. {ECO:0000250}. FT ACT_SITE 212 212 Charge relay system. {ECO:0000250}. FT CARBOHYD 110 110 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 39 173 {ECO:0000255|PROSITE-ProRule:PRU00274}. FT DISULFID 58 74 {ECO:0000255|PROSITE-ProRule:PRU00274}. FT DISULFID 145 246 {ECO:0000255|PROSITE-ProRule:PRU00274}. FT DISULFID 152 218 {ECO:0000255|PROSITE-ProRule:PRU00274}. FT DISULFID 184 198 {ECO:0000255|PROSITE-ProRule:PRU00274}. FT DISULFID 208 233 {ECO:0000255|PROSITE-ProRule:PRU00274}. FT VAR_SEQ 23 23 A -> AACGSLDLLTKLYAENLPCVHLNPQWPSQPSHCPRG FT WRSNPLPPAA (in isoform 2). FT {ECO:0000303|PubMed:10102990}. FT /FTId=VSP_005401. FT VAR_SEQ 24 164 Missing (in isoform 3). FT {ECO:0000303|Ref.7}. FT /FTId=VSP_030350. FT VAR_SEQ 25 32 HSRAQEDK -> RFWRPPGV (in isoform 4). FT {ECO:0000305}. FT /FTId=VSP_030351. FT VAR_SEQ 33 260 Missing (in isoform 4). {ECO:0000305}. FT /FTId=VSP_030352. FT VARIANT 154 154 V -> I (in dbSNP:rs16988799). FT /FTId=VAR_051855. FT CONFLICT 195 195 G -> V (in Ref. 11; AAH40887). FT {ECO:0000305}. FT STRAND 47 54 {ECO:0000244|PDB:5MS4}. FT STRAND 56 64 {ECO:0000244|PDB:5MS4}. FT STRAND 67 70 {ECO:0000244|PDB:5MS4}. FT HELIX 72 74 {ECO:0000244|PDB:5MS4}. FT STRAND 80 84 {ECO:0000244|PDB:5MS4}. FT STRAND 86 90 {ECO:0000244|PDB:5MS4}. FT STRAND 96 105 {ECO:0000244|PDB:5MS4}. FT STRAND 111 113 {ECO:0000244|PDB:5MS3}. FT STRAND 122 128 {ECO:0000244|PDB:5MS4}. FT STRAND 133 136 {ECO:0000244|PDB:5MS4}. FT STRAND 151 158 {ECO:0000244|PDB:5MS4}. FT STRAND 160 164 {ECO:0000244|PDB:5MS4}. FT STRAND 172 178 {ECO:0000244|PDB:5MS4}. FT HELIX 181 187 {ECO:0000244|PDB:5MS4}. FT TURN 189 191 {ECO:0000244|PDB:5MS4}. FT STRAND 196 200 {ECO:0000244|PDB:5MS4}. FT STRAND 215 228 {ECO:0000244|PDB:5MS4}. FT STRAND 231 234 {ECO:0000244|PDB:5MS3}. FT STRAND 236 238 {ECO:0000244|PDB:5MS4}. FT STRAND 240 244 {ECO:0000244|PDB:5MS4}. FT HELIX 245 247 {ECO:0000244|PDB:5MS4}. FT HELIX 249 257 {ECO:0000244|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 //