KLK15_HUMAN
ID KLK15_HUMAN Reviewed; 256 AA.
AC Q9H2R5; A0AUY8; Q15358; Q6ISI0; Q9H2R3; Q9H2R4; Q9H2R6; Q9HBG9;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Kallikrein-15;
DE EC=3.4.21.-;
DE AltName: Full=ACO protease;
DE Flags: Precursor;
GN Name=KLK15;
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 [GENOMIC DNA], ALTERNATIVE SPLICING, AND TISSUE
RP SPECIFICITY.
RX PubMed=11010966; DOI=10.1074/jbc.m005432200;
RA Yousef G.M., Scorilas A., Jung K., Ashworth L.K., Diamandis E.P.;
RT "Molecular cloning of the human kallikrein 15 gene (KLK15). Up-regulation
RT in prostate cancer.";
RL J. Biol. Chem. 276:53-61(2001).
RN [2]
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 [3]
RP PRELIMINARY PARTIAL NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=8018728; DOI=10.1016/0167-4781(94)90018-3;
RA Dihanich M.E., Spiess M.;
RT "A novel serine proteinase-like sequence from human brain.";
RL Biochim. Biophys. Acta 1218:225-228(1994).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
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 [6]
RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA Hillman R.T., Green R.E., Brenner S.E.;
RT "An unappreciated role for RNA surveillance.";
RL Genome Biol. 5:R8.1-R8.16(2004).
RN [7]
RP VARIANT [LARGE SCALE ANALYSIS] THR-137.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Protease whose physiological substrate is not yet known.
CC -!- INTERACTION:
CC Q9H2R5; P63172: DYNLT1; NbExp=3; IntAct=EBI-8645371, EBI-1176455;
CC Q9H2R5; Q15654: TRIP6; NbExp=3; IntAct=EBI-8645371, EBI-742327;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q9H2R5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H2R5-2; Sequence=VSP_005405;
CC Name=3;
CC IsoId=Q9H2R5-3; Sequence=VSP_005406, VSP_005407;
CC Name=4;
CC IsoId=Q9H2R5-4; Sequence=VSP_005404;
CC Name=5;
CC IsoId=Q9H2R5-5; Sequence=VSP_054621;
CC -!- TISSUE SPECIFICITY: Highest expression in the thyroid gland. Also
CC expressed in the prostate, salivary, and adrenal glands and in the
CC colon testis and kidney. {ECO:0000269|PubMed:11010966}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Kallikrein subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; AF242195; AAG09469.1; -; Genomic_DNA.
DR EMBL; AF242195; AAG09470.1; -; Genomic_DNA.
DR EMBL; AF242195; AAG09471.1; -; Genomic_DNA.
DR EMBL; AF242195; AAG09472.1; -; Genomic_DNA.
DR EMBL; AF243527; AAG33354.1; -; Genomic_DNA.
DR EMBL; X75363; CAA53145.1; ALT_SEQ; mRNA.
DR EMBL; CH471135; EAW71918.1; -; Genomic_DNA.
DR EMBL; BC069480; AAH69480.1; -; mRNA.
DR EMBL; BC069507; AAH69507.1; -; mRNA.
DR EMBL; BC069518; AAH69518.1; -; mRNA.
DR EMBL; BC126137; AAI26138.1; -; mRNA.
DR EMBL; BC144046; AAI44047.1; -; mRNA.
DR CCDS; CCDS12805.1; -. [Q9H2R5-1]
DR CCDS; CCDS62766.1; -. [Q9H2R5-5]
DR PIR; S45356; S45356.
DR RefSeq; NP_001264010.1; NM_001277081.1. [Q9H2R5-5]
DR RefSeq; NP_001264011.1; NM_001277082.1.
DR RefSeq; NP_059979.2; NM_017509.3. [Q9H2R5-1]
DR RefSeq; XP_006723328.1; XM_006723265.3. [Q9H2R5-1]
DR RefSeq; XP_011525387.1; XM_011527085.2. [Q9H2R5-5]
DR RefSeq; XP_011525389.1; XM_011527087.2. [Q9H2R5-4]
DR RefSeq; XP_011525390.1; XM_011527088.2. [Q9H2R5-3]
DR RefSeq; XP_016882432.1; XM_017026943.1. [Q9H2R5-2]
DR AlphaFoldDB; Q9H2R5; -.
DR SMR; Q9H2R5; -.
DR BioGRID; 120715; 186.
DR IntAct; Q9H2R5; 7.
DR MINT; Q9H2R5; -.
DR STRING; 9606.ENSP00000469315; -.
DR MEROPS; S01.081; -.
DR GlyGen; Q9H2R5; 2 sites.
DR iPTMnet; Q9H2R5; -.
DR PhosphoSitePlus; Q9H2R5; -.
DR BioMuta; KLK15; -.
DR DMDM; 18202940; -.
DR jPOST; Q9H2R5; -.
DR MassIVE; Q9H2R5; -.
DR PaxDb; Q9H2R5; -.
DR PeptideAtlas; Q9H2R5; -.
DR PRIDE; Q9H2R5; -.
DR ProteomicsDB; 80579; -. [Q9H2R5-1]
DR Antibodypedia; 18915; 244 antibodies from 28 providers.
DR DNASU; 55554; -.
DR Ensembl; ENST00000326856.8; ENSP00000314783.4; ENSG00000174562.13. [Q9H2R5-5]
DR Ensembl; ENST00000598239.5; ENSP00000469315.1; ENSG00000174562.13. [Q9H2R5-1]
DR GeneID; 55554; -.
DR KEGG; hsa:55554; -.
DR MANE-Select; ENST00000598239.6; ENSP00000469315.1; NM_017509.4; NP_059979.2.
DR UCSC; uc002ptl.4; human. [Q9H2R5-1]
DR CTD; 55554; -.
DR DisGeNET; 55554; -.
DR GeneCards; KLK15; -.
DR HGNC; HGNC:20453; KLK15.
DR HPA; ENSG00000174562; Tissue enhanced (intestine, salivary gland).
DR MIM; 610601; gene.
DR neXtProt; NX_Q9H2R5; -.
DR OpenTargets; ENSG00000174562; -.
DR PharmGKB; PA134977502; -.
DR VEuPathDB; HostDB:ENSG00000174562; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000162074; -.
DR HOGENOM; CLU_006842_1_1_1; -.
DR InParanoid; Q9H2R5; -.
DR OMA; NAWRGDS; -.
DR PhylomeDB; Q9H2R5; -.
DR TreeFam; TF331065; -.
DR BRENDA; 3.4.21.35; 2681.
DR PathwayCommons; Q9H2R5; -.
DR SignaLink; Q9H2R5; -.
DR BioGRID-ORCS; 55554; 12 hits in 1071 CRISPR screens.
DR ChiTaRS; KLK15; human.
DR GeneWiki; KLK15; -.
DR GenomeRNAi; 55554; -.
DR Pharos; Q9H2R5; Tbio.
DR PRO; PR:Q9H2R5; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9H2R5; protein.
DR Bgee; ENSG00000174562; Expressed in vena cava and 76 other tissues.
DR ExpressionAtlas; Q9H2R5; baseline and differential.
DR Genevisible; Q9H2R5; HS.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030141; C:secretory granule; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; NAS:UniProtKB.
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 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.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT PROPEP 17..21
FT /note="Activation peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000027960"
FT CHAIN 22..256
FT /note="Kallikrein-15"
FT /id="PRO_0000027961"
FT DOMAIN 22..254
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 62
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 106
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 209
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 47..63
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 138..215
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 180..194
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 205..230
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT VAR_SEQ 15
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054621"
FT VAR_SEQ 122..256
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_005405"
FT VAR_SEQ 122..206
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_005404"
FT VAR_SEQ 161
FT /note="V -> G (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_005406"
FT VAR_SEQ 162..256
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_005407"
FT VARIANT 134
FT /note="P -> L (in dbSNP:rs3212805)"
FT /id="VAR_020179"
FT VARIANT 137
FT /note="A -> T (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036298"
FT CONFLICT 147..160
FT /note="SHNEPGTAGSPRSQ -> PLSSP (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 256 AA; 28087 MW; B5EBF8D6022786B5 CRC64;
MWLLLTLSFL LASTAAQDGD KLLEGDECAP HSQPWQVALY ERGRFNCGAS LISPHWVLSA
AHCQSRFMRV RLGEHNLRKR DGPEQLRTTS RVIPHPRYEA RSHRNDIMLL RLVQPARLNP
QVRPAVLPTR CPHPGEACVV SGWGLVSHNE PGTAGSPRSQ VSLPDTLHCA NISIISDTSC
DKSYPGRLTN TMVCAGAEGR GAESCEGDSG GPLVCGGILQ GIVSWGDVPC DNTTKPGVYT
KVCHYLEWIR ETMKRN
