KLK11_MOUSE
ID KLK11_MOUSE Reviewed; 276 AA.
AC Q9QYN3; Q9QYN4;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Kallikrein-11;
DE EC=3.4.21.-;
DE AltName: Full=Hippostasin;
DE AltName: Full=Serine protease 20;
DE Flags: Precursor;
GN Name=Klk11; Synonyms=Prss20;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RC TISSUE=Brain, and Prostate;
RX PubMed=11072088; DOI=10.1016/s0167-4781(00)00206-2;
RA Mitsui S., Okui A., Kominami K., Uemura H., Yamagushi N.;
RT "cDNA cloning and tissue-specific splicing variants of mouse
RT hippostasin/TLSP (PRSS20).";
RL Biochim. Biophys. Acta 1494:206-210(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2;
CC IsoId=Q9QYN3-1; Sequence=Displayed;
CC Name=1;
CC IsoId=Q9QYN3-2; Sequence=VSP_017318;
CC -!- TISSUE SPECIFICITY: Expressed in brain and prostate (isoform 1) and
CC prostate (isoform 2). {ECO:0000269|PubMed:11072088}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Kallikrein subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; AB016226; BAA88825.1; -; mRNA.
DR EMBL; AB016227; BAA36955.1; -; mRNA.
DR EMBL; AK009360; BAB26241.2; -; mRNA.
DR EMBL; AK009720; BAB26461.2; -; mRNA.
DR CCDS; CCDS39935.1; -. [Q9QYN3-2]
DR CCDS; CCDS52227.1; -. [Q9QYN3-1]
DR RefSeq; NP_001170844.1; NM_001177373.1. [Q9QYN3-1]
DR RefSeq; NP_064358.1; NM_019974.2. [Q9QYN3-2]
DR AlphaFoldDB; Q9QYN3; -.
DR SMR; Q9QYN3; -.
DR BioGRID; 208046; 2.
DR STRING; 10090.ENSMUSP00000079101; -.
DR MEROPS; S01.257; -.
DR GlyGen; Q9QYN3; 4 sites.
DR iPTMnet; Q9QYN3; -.
DR PhosphoSitePlus; Q9QYN3; -.
DR PaxDb; Q9QYN3; -.
DR PRIDE; Q9QYN3; -.
DR ProteomicsDB; 264778; -. [Q9QYN3-1]
DR ProteomicsDB; 264779; -. [Q9QYN3-2]
DR Antibodypedia; 18965; 359 antibodies from 32 providers.
DR DNASU; 56538; -.
DR Ensembl; ENSMUST00000080211; ENSMUSP00000079101; ENSMUSG00000067616. [Q9QYN3-1]
DR Ensembl; ENSMUST00000171458; ENSMUSP00000132721; ENSMUSG00000067616. [Q9QYN3-2]
DR GeneID; 56538; -.
DR KEGG; mmu:56538; -.
DR UCSC; uc009gnm.1; mouse. [Q9QYN3-1]
DR CTD; 11012; -.
DR MGI; MGI:1929977; Klk11.
DR VEuPathDB; HostDB:ENSMUSG00000067616; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT01020000230389; -.
DR HOGENOM; CLU_006842_1_1_1; -.
DR InParanoid; Q9QYN3; -.
DR OMA; ATISIPH; -.
DR PhylomeDB; Q9QYN3; -.
DR TreeFam; TF331065; -.
DR BioGRID-ORCS; 56538; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Klk11; mouse.
DR PRO; PR:Q9QYN3; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9QYN3; protein.
DR Bgee; ENSMUSG00000067616; Expressed in lip and 27 other tissues.
DR ExpressionAtlas; Q9QYN3; baseline and differential.
DR Genevisible; Q9QYN3; MM.
DR GO; GO:0005576; C:extracellular region; IDA:MGI.
DR GO; GO:0030141; C:secretory granule; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
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 2: Evidence at transcript level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..44
FT /evidence="ECO:0000255"
FT PROPEP 45..47
FT /note="Activation peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000224185"
FT CHAIN 48..276
FT /note="Kallikrein-11"
FT /id="PRO_0000224186"
FT DOMAIN 48..274
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 88
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 136
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 229
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 54..189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 73..89
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 168..235
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 200..214
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 225..250
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT VAR_SEQ 1..27
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:11072088"
FT /id="VSP_017318"
SQ SEQUENCE 276 AA; 30754 MW; 90BDC03A8AB178D6 CRC64;
MRRLKSDWKL STETREPGAR PALLQARMIL RLIALALVTG HVGGETRIIK GYECRPHSQP
WQVALFQKTR LLCGATLIAP KWLLTAAHCR KPHYVILLGE HNLEKTDGCE QRRMATESFP
HPDFNNSLPN KDHRNDIMLV KMSSPVFFTR AVQPLTLSPH CVAAGTSCLI SGWGTTSSPQ
LRLPHSLRCA NVSIIEHKEC EKAYPGNITD TMLCASVRKE GKDSCQGDSG GPLVCNGSLQ
GIISWGQDPC AVTRKPGVYT KVCKYFNWIH EVMRNN
