KLK11_HUMAN
ID KLK11_HUMAN Reviewed; 282 AA.
AC Q9UBX7; O75837; Q0WXX5; Q8IXD7; Q9NS65;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Kallikrein-11;
DE Short=hK11;
DE EC=3.4.21.-;
DE AltName: Full=Hippostasin;
DE AltName: Full=Serine protease 20;
DE AltName: Full=Trypsin-like protease;
DE Contains:
DE RecName: Full=Kallikrein-11 inactive chain 1;
DE Contains:
DE RecName: Full=Kallikrein-11 inactive chain 2;
DE Flags: Precursor;
GN Name=KLK11; Synonyms=PRSS20, TLSP; ORFNames=UNQ649/PRO1279;
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 [MRNA] (ISOFORM 2).
RC TISSUE=Hippocampus;
RX PubMed=9765601; DOI=10.1016/s0167-4781(98)00116-x;
RA Yoshida S., Taniguchi M., Suemoto T., Oka T., He X.P., Shiosaka S.;
RT "cDNA cloning and expression of a novel serine protease, TLSP.";
RL Biochim. Biophys. Acta 1399:225-228(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Hippocampus, and Prostate;
RX PubMed=10872828; DOI=10.1006/bbrc.2000.2761;
RA Mitsui S., Yamada T., Okui A., Kominami K., Uemura H., Yamaguchi N.;
RT "A novel isoform of a kallikrein-like protease, TLSP/hippostasin, (PRSS20),
RT is expressed in the human brain and prostate.";
RL Biochem. Biophys. Res. Commun. 272:205-211(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX PubMed=10662548; DOI=10.1006/geno.1999.6072;
RA Yousef G.M., Scorilas A., Diamandis E.P.;
RT "Genomic organization, mapping, tissue expression, and hormonal regulation
RT of trypsin-like serine protease (TLSP PRSS20), a new member of the human
RT kallikrein gene family.";
RL Genomics 63:88-96(2000).
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 [MRNA] (ISOFORM 3).
RX PubMed=12539228; DOI=10.1002/pros.10191;
RA Nakamura T., Mitsui S., Okui A., Miki T., Yamaguchi N.;
RT "Molecular cloning and expression of a variant form of hippostasin/KLK11 in
RT prostate.";
RL Prostate 54:299-305(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
RP ALTERNATIVE SPLICING.
RX PubMed=16911518; DOI=10.1111/j.1742-4658.2006.05372.x;
RA Mitsui S., Nakamura T., Okui A., Kominami K., Uemura H., Yamaguchi N.;
RT "Multiple promoters regulate tissue-specific alternative splicing of the
RT human kallikrein gene, KLK11/hippostasin.";
RL FEBS J. 273:3678-3686(2006).
RN [7]
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 [8]
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 [11]
RP FUNCTION, PROTEOLYTIC PROCESSING, AND TISSUE SPECIFICITY.
RX PubMed=16467084; DOI=10.1158/1078-0432.ccr-05-1696;
RA Luo L.Y., Shan S.J., Elliott M.B., Soosaipillai A., Diamandis E.P.;
RT "Purification and characterization of human kallikrein 11, a candidate
RT prostate and ovarian cancer biomarker, from seminal plasma.";
RL Clin. Cancer Res. 12:742-750(2006).
CC -!- FUNCTION: Possible multifunctional protease. Efficiently cleaves 'bz-
CC Phe-Arg-4-methylcoumaryl-7-amide', a kallikrein substrate, and weakly
CC cleaves other substrates for kallikrein and trypsin. Cleaves synthetic
CC peptides after arginine but not lysine residues.
CC {ECO:0000269|PubMed:10872828, ECO:0000269|PubMed:16467084}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Secreted.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Golgi apparatus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=2;
CC IsoId=Q9UBX7-2; Sequence=Displayed;
CC Name=1;
CC IsoId=Q9UBX7-1; Sequence=VSP_005402;
CC Name=3;
CC IsoId=Q9UBX7-3; Sequence=VSP_043326;
CC Name=4;
CC IsoId=Q9UBX7-4; Sequence=VSP_005402, VSP_043326;
CC -!- TISSUE SPECIFICITY: Expressed in brain, skin and prostate. Isoform 1 is
CC expressed preferentially in brain. Isoform 2 is expressed in prostate.
CC Present in seminal plasma at concentrations ranging from 2 to 37
CC microg/mL (at protein level). {ECO:0000269|PubMed:10872828,
CC ECO:0000269|PubMed:16467084}.
CC -!- PTM: About 40% of KLK11 is inactivated by internal cleavage after Arg-
CC 188. This proteolytic inactivation may be effected by plasminogen.
CC {ECO:0000269|PubMed:16467084}.
CC -!- MISCELLANEOUS: [Isoform 3]: Localized in the prostate secretory
CC epithelium. {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/KLK11ID41077ch19q13.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; AB012917; BAA33404.1; -; mRNA.
DR EMBL; AB013730; BAA88713.1; -; mRNA.
DR EMBL; AB041036; BAA96797.1; -; mRNA.
DR EMBL; AF164623; AAD47815.1; -; Genomic_DNA.
DR EMBL; AF243527; AAG33364.1; -; Genomic_DNA.
DR EMBL; AB078780; BAC54105.1; -; mRNA.
DR EMBL; AB261897; BAE95335.1; -; mRNA.
DR EMBL; AB259014; BAF02733.1; -; mRNA.
DR EMBL; AY359014; AAQ89373.1; -; mRNA.
DR EMBL; AC011473; AAG23257.1; -; Genomic_DNA.
DR EMBL; CH471135; EAW71971.1; -; Genomic_DNA.
DR EMBL; BC022068; AAH22068.1; -; mRNA.
DR CCDS; CCDS12818.1; -. [Q9UBX7-2]
DR CCDS; CCDS12819.1; -. [Q9UBX7-1]
DR CCDS; CCDS54297.1; -. [Q9UBX7-4]
DR RefSeq; NP_001129504.1; NM_001136032.2. [Q9UBX7-1]
DR RefSeq; NP_001161077.1; NM_001167605.1. [Q9UBX7-4]
DR RefSeq; NP_006844.1; NM_006853.2. [Q9UBX7-1]
DR RefSeq; NP_659196.1; NM_144947.2. [Q9UBX7-2]
DR RefSeq; XP_011524671.1; XM_011526369.1. [Q9UBX7-3]
DR RefSeq; XP_011524672.1; XM_011526370.2. [Q9UBX7-4]
DR RefSeq; XP_011524673.1; XM_011526371.2. [Q9UBX7-4]
DR RefSeq; XP_011524674.1; XM_011526372.2. [Q9UBX7-4]
DR RefSeq; XP_011524675.1; XM_011526373.1. [Q9UBX7-4]
DR AlphaFoldDB; Q9UBX7; -.
DR SMR; Q9UBX7; -.
DR BioGRID; 116202; 98.
DR IntAct; Q9UBX7; 16.
DR STRING; 9606.ENSP00000473047; -.
DR MEROPS; S01.257; -.
DR GlyGen; Q9UBX7; 4 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q9UBX7; -.
DR PhosphoSitePlus; Q9UBX7; -.
DR BioMuta; KLK11; -.
DR DMDM; 88984315; -.
DR jPOST; Q9UBX7; -.
DR MassIVE; Q9UBX7; -.
DR PaxDb; Q9UBX7; -.
DR PeptideAtlas; Q9UBX7; -.
DR PRIDE; Q9UBX7; -.
DR ProteomicsDB; 84094; -. [Q9UBX7-2]
DR ProteomicsDB; 84095; -. [Q9UBX7-1]
DR ProteomicsDB; 84096; -. [Q9UBX7-3]
DR Antibodypedia; 18965; 359 antibodies from 32 providers.
DR DNASU; 11012; -.
DR Ensembl; ENST00000319720.11; ENSP00000324269.6; ENSG00000167757.14. [Q9UBX7-1]
DR Ensembl; ENST00000391804.7; ENSP00000375680.2; ENSG00000167757.14. [Q9UBX7-4]
DR Ensembl; ENST00000453757.8; ENSP00000413958.2; ENSG00000167757.14. [Q9UBX7-1]
DR Ensembl; ENST00000594768.5; ENSP00000473047.1; ENSG00000167757.14. [Q9UBX7-2]
DR GeneID; 11012; -.
DR KEGG; hsa:11012; -.
DR MANE-Select; ENST00000453757.8; ENSP00000413958.2; NM_001136032.3; NP_001129504.1. [Q9UBX7-1]
DR UCSC; uc002pvb.3; human. [Q9UBX7-2]
DR CTD; 11012; -.
DR DisGeNET; 11012; -.
DR GeneCards; KLK11; -.
DR HGNC; HGNC:6359; KLK11.
DR HPA; ENSG00000167757; Tissue enhanced (esophagus, salivary gland, skin, vagina).
DR MIM; 604434; gene.
DR neXtProt; NX_Q9UBX7; -.
DR OpenTargets; ENSG00000167757; -.
DR PharmGKB; PA30148; -.
DR VEuPathDB; HostDB:ENSG00000167757; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT01020000230389; -.
DR HOGENOM; CLU_006842_1_1_1; -.
DR InParanoid; Q9UBX7; -.
DR OMA; ATISIPH; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q9UBX7; -.
DR TreeFam; TF331065; -.
DR BRENDA; 3.4.21.35; 2681.
DR BRENDA; 3.4.21.B42; 2681.
DR PathwayCommons; Q9UBX7; -.
DR SignaLink; Q9UBX7; -.
DR BioGRID-ORCS; 11012; 13 hits in 1067 CRISPR screens.
DR ChiTaRS; KLK11; human.
DR GeneWiki; KLK11; -.
DR GenomeRNAi; 11012; -.
DR Pharos; Q9UBX7; Tbio.
DR PRO; PR:Q9UBX7; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9UBX7; protein.
DR Bgee; ENSG00000167757; Expressed in lower esophagus mucosa and 127 other tissues.
DR ExpressionAtlas; Q9UBX7; baseline and differential.
DR Genevisible; Q9UBX7; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0030141; C:secretory granule; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0008236; F:serine-type peptidase activity; TAS:ProtInc.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 Alternative splicing; Disulfide bond; Glycoprotein; Golgi apparatus;
KW Hydrolase; Protease; Reference proteome; Secreted; Serine protease; Signal;
KW Zymogen.
FT SIGNAL 1..50
FT /evidence="ECO:0000255"
FT PROPEP 51..53
FT /note="Activation peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000027954"
FT CHAIN 54..282
FT /note="Kallikrein-11"
FT /id="PRO_0000027955"
FT CHAIN 54..188
FT /note="Kallikrein-11 inactive chain 1"
FT /id="PRO_0000302061"
FT CHAIN 189..282
FT /note="Kallikrein-11 inactive chain 2"
FT /id="PRO_0000302062"
FT DOMAIN 53..280
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 94
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 142
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 235
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 60..195
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 79..95
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 167..269
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 174..241
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 206..220
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 231..256
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT VAR_SEQ 1..32
FT /note="Missing (in isoform 1 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10872828,
FT ECO:0000303|PubMed:12975309, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16911518"
FT /id="VSP_005402"
FT VAR_SEQ 98
FT /note="P -> PWVSLTSPTHVSPDLSSSNYCLSHLS (in isoform 3 and
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:12539228"
FT /id="VSP_043326"
FT VARIANT 32
FT /note="A -> T (in dbSNP:rs2288892)"
FT /id="VAR_051856"
FT VARIANT 49
FT /note="G -> E (in dbSNP:rs3745539)"
FT /id="VAR_021943"
FT VARIANT 166
FT /note="R -> C (in dbSNP:rs1048328)"
FT /id="VAR_024296"
SQ SEQUENCE 282 AA; 31059 MW; B442DDE613EE0A17 CRC64;
MQRLRWLRDW KSSGRGLTAA KEPGARSSPL QAMRILQLIL LALATGLVGG ETRIIKGFEC
KPHSQPWQAA LFEKTRLLCG ATLIAPRWLL TAAHCLKPRY IVHLGQHNLQ KEEGCEQTRT
ATESFPHPGF NNSLPNKDHR NDIMLVKMAS PVSITWAVRP LTLSSRCVTA GTSCLISGWG
STSSPQLRLP HTLRCANITI IEHQKCENAY PGNITDTMVC ASVQEGGKDS CQGDSGGPLV
CNQSLQGIIS WGQDPCAITR KPGVYTKVCK YVDWIQETMK NN
