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 27-MAR-2024, entry version 176. 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}. 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; 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. DR RefSeq; XP_011525387.1; XM_011527085.2. 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; 187. DR IntAct; Q9H2R5; 7. DR MINT; Q9H2R5; -. DR STRING; 9606.ENSP00000469315; -. DR MEROPS; S01.081; -. DR GlyCosmos; Q9H2R5; 2 sites, No reported glycans. 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; 9606-ENSP00000469315; -. DR PeptideAtlas; Q9H2R5; -. DR ProteomicsDB; 80579; -. [Q9H2R5-1] DR Antibodypedia; 18915; 275 antibodies from 28 providers. DR DNASU; 55554; -. DR Ensembl; ENST00000326856.8; ENSP00000314783.4; ENSG00000174562.14. [Q9H2R5-5] DR Ensembl; ENST00000598239.6; ENSP00000469315.1; ENSG00000174562.14. [Q9H2R5-1] DR Ensembl; ENST00000695965.1; ENSP00000512291.1; ENSG00000174562.14. [Q9H2R5-4] DR Ensembl; ENST00000695998.1; ENSP00000512319.1; ENSG00000174562.14. [Q9H2R5-5] 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 AGR; HGNC:20453; -. DR CTD; 55554; -. DR DisGeNET; 55554; -. DR GeneCards; KLK15; -. DR HGNC; HGNC:20453; KLK15. DR HPA; ENSG00000174562; Tissue enhanced (intestine, salivary gland, testis). 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; IISDASC; -. DR OrthoDB; 4629979at2759; -. DR PhylomeDB; Q9H2R5; -. DR TreeFam; TF331065; -. DR BRENDA; 3.4.21.35; 2681. DR PathwayCommons; Q9H2R5; -. DR SignaLink; Q9H2R5; -. DR BioGRID-ORCS; 55554; 14 hits in 1149 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 77 other cell types or tissues. DR ExpressionAtlas; Q9H2R5; baseline and differential. 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; Trypsin-like serine proteases; 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 PANTHER; PTHR24271:SF60; KALLIKREIN-15; 1. DR PANTHER; PTHR24271; KALLIKREIN-RELATED; 1. DR Pfam; PF00089; Trypsin; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR SMART; SM00020; Tryp_SPc; 1. DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1. DR PROSITE; PS50240; TRYPSIN_DOM; 1. DR PROSITE; PS00134; TRYPSIN_HIS; 1. DR Genevisible; Q9H2R5; HS. 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 //