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Kallikrein-8 (hK8) (EC 3.4.21.118) (Neuropsin) (NP) (Ovasin) (Serine protease 19) (Serine protease TADG-14) (Tumor-associated differentially expressed gene 14 protein)

 KLK8_HUMAN              Reviewed;         260 AA.
O60259; Q5V9X1; Q5V9X2; Q8IW69; Q9HCB3; Q9NR68; Q9NR69; Q9UIL9;
Q9UQ47;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
01-AUG-1998, sequence version 1.
27-SEP-2017, entry version 159.
RecName: Full=Kallikrein-8;
Short=hK8;
EC=3.4.21.118;
AltName: Full=Neuropsin;
Short=NP;
AltName: Full=Ovasin;
AltName: Full=Serine protease 19;
AltName: Full=Serine protease TADG-14;
AltName: Full=Tumor-associated differentially expressed gene 14 protein;
Flags: Precursor;
Name=KLK8; Synonyms=NRPN, PRSS19, TADG14; ORFNames=UNQ283/PRO322;
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).
TISSUE=Hippocampus;
PubMed=9714609; DOI=10.1016/S0378-1119(98)00232-7;
Yoshida S., Taniguchi M., Hirata A., Shiosaka S.;
"Sequence analysis and expression of human neuropsin cDNA and gene.";
Gene 213:9-16(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Ovary;
PubMed=10485494;
Underwood L.J., Tanimoto H., Wang Y., Shigemasa K., Parmley T.H.,
O'Brien T.J.;
"Cloning of tumor-associated differentially expressed gene-14, a novel
serine protease overexpressed by ovarian carcinoma.";
Cancer Res. 59:4435-4439(1999).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain;
PubMed=10102990; DOI=10.1046/j.1432-1327.1999.00213.x;
Mitsui S., Tsuruoka N., Yamashiro K., Nakazato H., Yamaguchi N.;
"A novel form of human neuropsin, a brain-related serine protease, is
generated by alternative splicing and is expressed preferentially in
human adult brain.";
Eur. J. Biochem. 260:627-634(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] (ISOFORMS 3 AND 4), AND TISSUE
SPECIFICITY.
PubMed=11309326;
Magklara A., Scorilas A., Katsaros D., Massobrio M., Yousef G.M.,
Fracchioli S., Danese S., Diamandis E.P.;
"The human KLK8 (neuropsin/ovasin) gene: identification of two novel
splice variants and its prognostic value in ovarian cancer.";
Clin. Cancer Res. 7:806-811(2001).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
Gan L., Gelinas R., Gown A.M., Moss P., Smith R., Wang K.;
"Molecular cloning and characterization of a novel serine protease,
ovasin, a potential molecular marker for ovarian carcinomas.";
Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Michael I.P., Diamandis E.P.;
"Human kallikrein 8 and human kallikrein 9 are organized as a
bicistronic operon.";
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[9]
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).
[10]
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.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
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).
[12]
PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
PubMed=15282331; DOI=10.1093/molbev/msh220;
Li Y., Qian Y.-P., Yu X.-J., Wang Y.-Q., Dong D.-G., Sun W., Ma R.-M.,
Su B.;
"Recent origin of a hominoid-specific splice form of neuropsin, a gene
involved in learning and memory.";
Mol. Biol. Evol. 21:2111-2115(2004).
[13]
TISSUE SPECIFICITY.
PubMed=11522960; DOI=10.1097/00001756-200108280-00031;
Shimizu-Okabe C., Yousef G.M., Diamandis E.P., Yoshida S.,
Shiosaka S., Fahnestock M.;
"Expression of the kallikrein gene family in normal and Alzheimer's
disease brain.";
NeuroReport 12:2747-2751(2001).
[14]
TISSUE SPECIFICITY.
PubMed=12147714; DOI=10.1136/mp.55.4.235;
Kuwae K., Matsumoto-Miyai K., Yoshida S., Sadayama T., Yoshikawa K.,
Hosokawa K., Shiosaka S.;
"Epidermal expression of serine protease, neuropsin (KLK8) in normal
and pathological skin samples.";
Mol. Pathol. 55:235-241(2002).
[15]
USE AS A MARKER FOR OVARIAN CANCER.
PubMed=12782581;
Kishi T., Grass L., Soosaipillai A., Scorilas A., Harbeck N.,
Schmalfeldt B., Dorn J., Mysliwiec M., Schmitt M., Diamandis E.P.;
"Human kallikrein 8, a novel biomarker for ovarian carcinoma.";
Cancer Res. 63:2771-2774(2003).
[16]
FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, AND
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=16337200; DOI=10.1016/j.febslet.2005.11.039;
Rajapakse S., Ogiwara K., Takano N., Moriyama A., Takahashi T.;
"Biochemical characterization of human kallikrein 8 and its possible
involvement in the degradation of extracellular matrix proteins.";
FEBS Lett. 579:6879-6884(2005).
[17]
ALTERNATIVE SPLICING (ISOFORM 2).
PubMed=17487847; DOI=10.1002/humu.20547;
Lu Z.-X., Peng J., Su B.;
"A human-specific mutation leads to the origin of a novel splice form
of neuropsin (KLK8), a gene involved in learning and memory.";
Hum. Mutat. 28:978-984(2007).
[18]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=17761692; DOI=10.1093/jb/mvm156;
Scott F.L., Sun J., Whisstock J.C., Kato K., Bird P.I.;
"SerpinB6 is an inhibitor of kallikrein-8 in keratinocytes.";
J. Biochem. 142:435-442(2007).
[19]
INTERACTION WITH SPINK9.
PubMed=19194479; DOI=10.1038/jid.2008.448;
Brattsand M., Stefansson K., Hubiche T., Nilsson S.K., Egelrud T.;
"SPINK9: a selective, skin-specific Kazal-type serine protease
inhibitor.";
J. Invest. Dermatol. 129:1656-1665(2009).
-!- FUNCTION: Serine protease which is capable of degrading a number
of proteins such as casein, fibrinogen, kininogen, fibronectin and
collagen type IV. Also cleaves L1CAM in response to increased
neural activity. Induces neurite outgrowth and fasciculation of
cultured hippocampal neurons. Plays a role in the formation and
maturation of orphan and small synaptic boutons in the Schaffer-
collateral pathway, regulates Schaffer-collateral long-term
potentiation in the hippocampus and is required for memory
acquisition and synaptic plasticity. Involved in skin desquamation
and keratinocyte proliferation. Plays a role in the secondary
phase of pathogenesis following spinal cord injury.
{ECO:0000269|PubMed:16337200}.
-!- CATALYTIC ACTIVITY: Cleavage of amide substrates following the
basic amino acids Arg or Lys at the P1 position, with a preference
for Arg over Lys. {ECO:0000269|PubMed:16337200}.
-!- ENZYME REGULATION: Inhibited by a range of serine protease
inhibitors including antipain, aprotinin, leupeptin, benzamidine
and soybean trypsin inhibitor. {ECO:0000269|PubMed:16337200}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.07 mM for Pro-Phe-Arg-MCA {ECO:0000269|PubMed:16337200};
KM=0.07 mM for Z-Val-Val-Arg-MCA {ECO:0000269|PubMed:16337200};
KM=0.07 mM for Boc-Val-Pro-Arg-MCA
{ECO:0000269|PubMed:16337200};
KM=0.10 mM for Boc-Leu-Lys-Arg-MCA
{ECO:0000269|PubMed:16337200};
KM=0.10 mM for Boc-Val-Leu-Lys-MCA
{ECO:0000269|PubMed:16337200};
KM=0.07 mM for Boc-Phe-Ser-Arg-MCA
{ECO:0000269|PubMed:16337200};
Vmax=7.1 umol/min/mg enzyme toward Pro-Phe-Arg-MCA
{ECO:0000269|PubMed:16337200};
Vmax=5.4 umol/min/mg enzyme toward Z-Val-Val-Arg-MCA
{ECO:0000269|PubMed:16337200};
Vmax=3.9 umol/min/mg enzyme toward Boc-Val-Pro-Arg-MCA
{ECO:0000269|PubMed:16337200};
Vmax=2.6 umol/min/mg enzyme toward Boc-Leu-Lys-Arg-MCA
{ECO:0000269|PubMed:16337200};
Vmax=1.9 umol/min/mg enzyme toward Boc-Val-Leu-Lys-MCA
{ECO:0000269|PubMed:16337200};
Vmax=1.6 umol/min/mg enzyme toward Boc-Phe-Ser-Arg-MCA
{ECO:0000269|PubMed:16337200};
pH dependence:
Optimum pH is 8.5. Active from pH 7-10.
{ECO:0000269|PubMed:16337200};
-!- SUBUNIT: Interacts with SPINK9. {ECO:0000269|PubMed:19194479}.
-!- INTERACTION:
Q7Z3S9:NOTCH2NL; NbExp=5; IntAct=EBI-3915857, EBI-945833;
Q8IUH5:ZDHHC17; NbExp=3; IntAct=EBI-3915857, EBI-524753;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17761692}.
Cytoplasm {ECO:0000269|PubMed:17761692}. Note=Shows a cytoplasmic
distribution in the keratinocytes.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=O60259-1; Sequence=Displayed;
Name=2;
IsoId=O60259-2; Sequence=VSP_005401;
Note=Produced as a result of a human-specific mutation which is
not found in other primates.;
Name=3;
IsoId=O60259-3; Sequence=VSP_030350;
Name=4;
IsoId=O60259-4; Sequence=VSP_030351, VSP_030352;
-!- TISSUE SPECIFICITY: Isoform 1 is predominantly expressed in the
pancreas. Isoform 2 is expressed in adult brain and hippocampus.
Isoform 1 and isoform 2 are found in fetal brain and placenta.
Detected in salivary gland, uterus, thymus, breast, testis and
kidney but not in spleen, liver, lung or normal ovarian tissue.
Displays an 11.5-fold increase in Alzheimer disease hippocampus
compared to controls and is overexpressed in some ovarian
carcinomas. Expressed at low levels in normal skin while high
levels are found in psoriasis vulgaris, seborrheic keratosis,
lichen planus and squamous cell carcinoma skin samples. Expressed
in the keratinocytes. {ECO:0000269|PubMed:11309326,
ECO:0000269|PubMed:11522960, ECO:0000269|PubMed:12147714,
ECO:0000269|PubMed:17761692}.
-!- MISCELLANEOUS: Expressed at high levels in serum, ascites fluid
and tumor cytosol of advanced stage ovarian cancer patients and
may serve as a marker of ovarian cancer.
-!- 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/KLK8ID41088ch19q13.html";
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EMBL; AB009849; BAA28673.1; -; mRNA.
EMBL; AB012761; BAA28676.1; -; Genomic_DNA.
EMBL; AF055982; AAD56050.1; -; mRNA.
EMBL; AB008390; BAA82665.1; -; mRNA.
EMBL; AB008927; BAA82666.1; -; mRNA.
EMBL; AB010780; BAA88684.1; -; Genomic_DNA.
EMBL; AF243527; AAG33361.1; -; Genomic_DNA.
EMBL; AF251125; AAF79144.1; -; Genomic_DNA.
EMBL; AF251125; AAF79145.1; -; Genomic_DNA.
EMBL; AF095742; AAD25979.1; -; mRNA.
EMBL; AF095743; AAD29574.1; -; Genomic_DNA.
EMBL; DQ267420; ABB83339.1; -; mRNA.
EMBL; AY359036; AAQ89395.1; -; mRNA.
EMBL; AC011473; AAG23254.1; -; Genomic_DNA.
EMBL; AC011483; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471135; EAW71962.1; -; Genomic_DNA.
EMBL; BC040887; AAH40887.1; -; mRNA.
EMBL; AY563055; AAT76913.1; -; Genomic_DNA.
EMBL; AY563055; AAT76914.1; -; Genomic_DNA.
EMBL; AY563056; AAT76915.1; -; Genomic_DNA.
EMBL; AY563056; AAT76916.1; -; Genomic_DNA.
EMBL; AY563057; AAT76917.1; -; Genomic_DNA.
EMBL; AY563057; AAT76918.1; -; Genomic_DNA.
EMBL; AY563058; AAT76919.1; -; Genomic_DNA.
EMBL; AY563058; AAT76920.1; -; Genomic_DNA.
EMBL; AY563059; AAT76921.1; -; Genomic_DNA.
EMBL; AY563059; AAT76922.1; -; Genomic_DNA.
EMBL; AY563060; AAT76923.1; -; Genomic_DNA.
EMBL; AY563060; AAT76924.1; -; Genomic_DNA.
EMBL; AY563061; AAT76925.1; -; Genomic_DNA.
EMBL; AY563061; AAT76926.1; -; Genomic_DNA.
EMBL; AY563062; AAT76927.1; -; Genomic_DNA.
EMBL; AY563062; AAT76928.1; -; Genomic_DNA.
EMBL; AY563063; AAT76929.1; -; Genomic_DNA.
EMBL; AY563063; AAT76930.1; -; Genomic_DNA.
EMBL; AY563064; AAT76931.1; -; Genomic_DNA.
EMBL; AY563064; AAT76932.1; -; Genomic_DNA.
EMBL; AY563065; AAT76933.1; -; Genomic_DNA.
EMBL; AY563065; AAT76934.1; -; Genomic_DNA.
EMBL; AY563066; AAT76935.1; -; Genomic_DNA.
EMBL; AY563066; AAT76936.1; -; Genomic_DNA.
EMBL; AY563067; AAT76937.1; -; Genomic_DNA.
EMBL; AY563067; AAT76938.1; -; Genomic_DNA.
CCDS; CCDS12813.1; -. [O60259-1]
CCDS; CCDS12814.1; -. [O60259-3]
CCDS; CCDS12815.1; -. [O60259-4]
CCDS; CCDS42600.1; -. [O60259-2]
RefSeq; NP_001268360.1; NM_001281431.1.
RefSeq; NP_009127.1; NM_007196.3. [O60259-1]
RefSeq; NP_653088.1; NM_144505.2. [O60259-2]
RefSeq; NP_653089.1; NM_144506.2. [O60259-3]
RefSeq; NP_653090.1; NM_144507.2. [O60259-4]
UniGene; Hs.104570; -.
ProteinModelPortal; O60259; -.
SMR; O60259; -.
BioGrid; 116371; 17.
IntAct; O60259; 9.
BindingDB; O60259; -.
ChEMBL; CHEMBL4812; -.
MEROPS; S01.244; -.
PhosphoSitePlus; O60259; -.
BioMuta; KLK8; -.
PeptideAtlas; O60259; -.
PRIDE; O60259; -.
DNASU; 11202; -.
Ensembl; ENST00000320838; ENSP00000325072; ENSG00000129455. [O60259-4]
Ensembl; ENST00000347619; ENSP00000341555; ENSG00000129455. [O60259-3]
Ensembl; ENST00000391806; ENSP00000375682; ENSG00000129455. [O60259-2]
Ensembl; ENST00000593490; ENSP00000469278; ENSG00000129455. [O60259-4]
Ensembl; ENST00000600767; ENSP00000472016; ENSG00000129455. [O60259-1]
GeneID; 11202; -.
KEGG; hsa:11202; -.
UCSC; uc002puq.2; human. [O60259-1]
CTD; 11202; -.
DisGeNET; 11202; -.
EuPathDB; HostDB:ENSG00000129455.15; -.
GeneCards; KLK8; -.
HGNC; HGNC:6369; KLK8.
HPA; CAB019393; -.
HPA; HPA035761; -.
MIM; 605644; gene.
neXtProt; NX_O60259; -.
OpenTargets; ENSG00000129455; -.
PharmGKB; PA30158; -.
GeneTree; ENSGT00760000118862; -.
HOVERGEN; HBG013304; -.
InParanoid; O60259; -.
KO; K08650; -.
OMA; FPQKKCE; -.
OrthoDB; EOG091G0DF7; -.
PhylomeDB; O60259; -.
TreeFam; TF331065; -.
BRENDA; 3.4.21.118; 2681.
Reactome; R-HSA-6809371; Formation of the cornified envelope.
GeneWiki; KLK8; -.
GenomeRNAi; 11202; -.
PRO; PR:O60259; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000129455; -.
ExpressionAtlas; O60259; baseline and differential.
Genevisible; O60259; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
GO; GO:0008219; P:cell death; ISS:UniProtKB.
GO; GO:0070268; P:cornification; TAS:Reactome.
GO; GO:0043616; P:keratinocyte proliferation; ISS:UniProtKB.
GO; GO:0007613; P:memory; ISS:UniProtKB.
GO; GO:0048681; P:negative regulation of axon regeneration; ISS:UniProtKB.
GO; GO:0031642; P:negative regulation of myelination; ISS:UniProtKB.
GO; GO:0048812; P:neuron projection morphogenesis; ISS:UniProtKB.
GO; GO:0050807; P:regulation of synapse organization; ISS:UniProtKB.
GO; GO:0009611; P:response to wounding; ISS:UniProtKB.
GO; GO:0050808; P:synapse organization; IEA:Ensembl.
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;
Alternative splicing; Complete proteome; Cytoplasm; Disulfide bond;
Glycoprotein; Hydrolase; Polymorphism; Protease; Reference proteome;
Secreted; Serine protease; Signal; Zymogen.
SIGNAL 1 28 {ECO:0000255}.
PROPEP 29 32 {ECO:0000250}.
/FTId=PRO_0000027946.
CHAIN 33 260 Kallikrein-8.
/FTId=PRO_0000027947.
DOMAIN 33 257 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 73 73 Charge relay system. {ECO:0000250}.
ACT_SITE 120 120 Charge relay system. {ECO:0000250}.
ACT_SITE 212 212 Charge relay system. {ECO:0000250}.
CARBOHYD 110 110 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 39 173 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 58 74 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 145 246 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 152 218 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 184 198 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 208 233 {ECO:0000255|PROSITE-ProRule:PRU00274}.
VAR_SEQ 23 23 A -> AACGSLDLLTKLYAENLPCVHLNPQWPSQPSHCPRG
WRSNPLPPAA (in isoform 2).
{ECO:0000303|PubMed:10102990}.
/FTId=VSP_005401.
VAR_SEQ 24 164 Missing (in isoform 3).
{ECO:0000303|Ref.7}.
/FTId=VSP_030350.
VAR_SEQ 25 32 HSRAQEDK -> RFWRPPGV (in isoform 4).
{ECO:0000305}.
/FTId=VSP_030351.
VAR_SEQ 33 260 Missing (in isoform 4). {ECO:0000305}.
/FTId=VSP_030352.
VARIANT 154 154 V -> I (in dbSNP:rs16988799).
/FTId=VAR_051855.
CONFLICT 195 195 G -> V (in Ref. 11; AAH40887).
{ECO:0000305}.
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


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