KLK1_MOUSE
ID KLK1_MOUSE Reviewed; 261 AA.
AC P15947; Q61855;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2001, sequence version 3.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Kallikrein-1;
DE EC=3.4.21.35;
DE AltName: Full=Glandular kallikrein K1;
DE AltName: Full=KAL-B;
DE AltName: Full=Renal kallikrein;
DE AltName: Full=Tissue kallikrein-6;
DE Short=mGK-6;
DE Flags: Precursor;
GN Name=Klk1; Synonyms=Klk-6, Klk6;
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 [GENOMIC DNA].
RX PubMed=3007510; DOI=10.1016/s0021-9258(19)57247-7;
RA van Leeuwen B.H., Evans B.A., Tregear G.W., Richards R.I.;
RT "Mouse glandular kallikrein genes. Identification, structure, and
RT expression of the renal kallikrein gene.";
RL J. Biol. Chem. 261:5529-5535(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Tada M., Peters J., Takahashi S., Inoue H., Miyake Y.;
RT "Identification of a tissue kallikrein gene, mGK-6, expressed in a mouse
RT neuroendocrine cell line.";
RL Submitted (JUN-1991) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon, Kidney, and Salivary gland;
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 [5]
RP PROTEIN SEQUENCE OF 25-44.
RC TISSUE=Submandibular gland;
RX PubMed=1639762; DOI=10.1093/oxfordjournals.jbchem.a123812;
RA Peters J., Takahashi S., Tada M., Miyake Y.;
RT "mGK-6-derived true tissue kallikrein is synthesized, processed, and
RT targeted through a regulated secretory pathway in mouse pituitary AtT-20
RT cells.";
RL J. Biochem. 111:643-648(1992).
RN [6]
RP PROTEIN SEQUENCE OF 165-174.
RC TISSUE=Submandibular gland;
RX PubMed=2583286; DOI=10.1016/0014-5793(89)81581-9;
RA Murakami K., Ikigai H., Nagumo N., Tomita M., Shimamura T.;
RT "A cytocidal tissue kallikrein isolated from mouse submandibular glands.";
RL FEBS Lett. 257:400-402(1989).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in
CC kininogen to release Lys-bradykinin.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage of Arg-|-Xaa bonds in small molecule
CC substrates. Highly selective action to release kallidin (lysyl-
CC bradykinin) from kininogen involves hydrolysis of Met-|-Xaa or Leu-|-
CC Xaa.; EC=3.4.21.35;
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Kallikrein subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; M13500; AAG11389.1; -; Genomic_DNA.
DR EMBL; M13498; AAG11389.1; JOINED; Genomic_DNA.
DR EMBL; M13499; AAG11389.1; JOINED; Genomic_DNA.
DR EMBL; D10464; BAA01257.1; -; mRNA.
DR EMBL; AK002278; BAB21982.1; -; mRNA.
DR EMBL; BC010754; AAH10754.1; -; mRNA.
DR EMBL; BC027736; AAH27736.1; -; mRNA.
DR EMBL; BC053697; AAH53697.1; -; mRNA.
DR CCDS; CCDS21202.1; -.
DR PIR; A25606; A25606.
DR RefSeq; NP_001307260.1; NM_001320331.1.
DR RefSeq; NP_001307261.1; NM_001320332.1.
DR RefSeq; NP_034769.4; NM_010639.8.
DR AlphaFoldDB; P15947; -.
DR SMR; P15947; -.
DR STRING; 10090.ENSMUSP00000074659; -.
DR MEROPS; S01.167; -.
DR GlyGen; P15947; 1 site.
DR PhosphoSitePlus; P15947; -.
DR jPOST; P15947; -.
DR MaxQB; P15947; -.
DR PaxDb; P15947; -.
DR PeptideAtlas; P15947; -.
DR PRIDE; P15947; -.
DR ProteomicsDB; 263660; -.
DR DNASU; 16612; -.
DR Ensembl; ENSMUST00000075162; ENSMUSP00000074659; ENSMUSG00000063903.
DR GeneID; 16612; -.
DR KEGG; mmu:16612; -.
DR UCSC; uc009goo.1; mouse.
DR CTD; 3816; -.
DR MGI; MGI:102850; Klk1.
DR VEuPathDB; HostDB:ENSMUSG00000063903; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT01020000230389; -.
DR HOGENOM; CLU_006842_1_1_1; -.
DR InParanoid; P15947; -.
DR OMA; ETMSANS; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; P15947; -.
DR TreeFam; TF331065; -.
DR BRENDA; 3.4.21.35; 3474.
DR BRENDA; 3.4.21.B10; 3474.
DR Reactome; R-MMU-1592389; Activation of Matrix Metalloproteinases.
DR BioGRID-ORCS; 16612; 1 hit in 42 CRISPR screens.
DR ChiTaRS; Klk1; mouse.
DR PRO; PR:P15947; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P15947; protein.
DR Bgee; ENSMUSG00000063903; Expressed in submandibular gland and 82 other tissues.
DR ExpressionAtlas; P15947; baseline and differential.
DR Genevisible; P15947; MM.
DR GO; GO:0001669; C:acrosomal vesicle; ISO:MGI.
DR GO; GO:0045177; C:apical part of cell; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0030141; C:secretory granule; IBA:GO_Central.
DR GO; GO:0004175; F:endopeptidase activity; ISO:MGI.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; ISO:MGI.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISO:MGI.
DR GO; GO:0008236; F:serine-type peptidase activity; ISO:MGI.
DR GO; GO:0003073; P:regulation of systemic arterial blood pressure; IBA:GO_Central.
DR GO; GO:0031638; P:zymogen activation; IBA:GO_Central.
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 Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW Protease; Reference proteome; Serine protease; Signal; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000305"
FT PROPEP 19..24
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:1639762"
FT /id="PRO_0000027975"
FT CHAIN 25..261
FT /note="Kallikrein-1"
FT /id="PRO_0000027976"
FT DOMAIN 25..258
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 65
FT /note="Charge relay system"
FT ACT_SITE 120
FT /note="Charge relay system"
FT ACT_SITE 213
FT /note="Charge relay system"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 31..173
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 50..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 152..219
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 184..198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 209..234
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CONFLICT 57
FT /note="A -> V (in Ref. 1; AAG11389)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 261 AA; 28775 MW; 7850DDFDBFFB94B8 CRC64;
MRFLILFLAL SLGGIDAAPP VQSRIVGGFN CEKNSQPWQV AVYRFTKYQC GGILLNANWV
LTAAHCHNDK YQVWLGKNNF LEDEPSAQHR LVSKAIPHPD FNMSLLNEHT PQPEDDYSND
LMLLRLKKPA DITDVVKPID LPTEEPKLGS TCLASGWGSI TPVKYEYPDE LQCVNLKLLP
NEDCAKAHIE KVTDDMLCAG DMDGGKDTCA GDSGGPLICD GVLQGITSWG PSPCGKPNVP
GIYTRVLNFN TWIRETMAEN D
