KLK10_HUMAN
ID KLK10_HUMAN Reviewed; 276 AA.
AC O43240; A6NC12; Q53YL3; Q99920; Q9GZW9;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 3.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Kallikrein-10;
DE EC=3.4.21.-;
DE AltName: Full=Normal epithelial cell-specific 1;
DE AltName: Full=Protease serine-like 1;
DE Flags: Precursor;
GN Name=KLK10; Synonyms=NES1, PRSSL1;
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], AND VARIANTS ALA-50 AND PRO-149.
RC TISSUE=Epithelium;
RX PubMed=8764136;
RA Liu X.-L., Wazer D.E., Watanabe K., Band V.;
RT "Identification of a novel serine protease-like gene, the expression of
RT which is down-regulated during breast cancer progression.";
RL Cancer Res. 56:3371-3379(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ALA-50 AND PRO-149.
RX PubMed=9647736; DOI=10.1006/bbrc.1998.8793;
RA Luo L.-Y., Herbrick J.A., Scherer S.W., Beatty B., Squire J.,
RA Diamandis E.P.;
RT "Structural characterization and mapping of the normal epithelial cell-
RT specific 1 gene.";
RL Biochem. Biophys. Res. Commun. 247:580-586(1998).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16103744; DOI=10.1159/000087377;
RA Yousef G.M., White N.M.A., Michael I.P., Cho J.C.-K., Robb J.D.,
RA Kurlender L., Khan S., Diamandis E.P.;
RT "Identification of new splice variants and differential expression of the
RT human kallikrein 10 gene, a candidate cancer biomarker.";
RL Tumor Biol. 26:227-235(2005).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ALA-50 AND PRO-149.
RC TISSUE=Uterus;
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 [7]
RP CHARACTERIZATION.
RX PubMed=9809976;
RA Goyal J., Smith K.M., Cowan J.M., Wazer D.E., Lee S.W., Band V.;
RT "The role for NES1 serine protease as a novel tumor suppressor.";
RL Cancer Res. 58:4782-4786(1998).
CC -!- FUNCTION: Has a tumor-suppressor role for NES1 in breast and prostate
CC cancer.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in breast, ovary and prostate.
CC -!- DEVELOPMENTAL STAGE: Down-regulated during breast cancer progression.
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/KLK10ID41076ch19q13.html";
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DR EMBL; AF024605; AAB81602.1; -; mRNA.
DR EMBL; AF055481; AAC14266.1; -; Genomic_DNA.
DR EMBL; AF243527; AAG33363.1; -; Genomic_DNA.
DR EMBL; AY561635; AAS66976.1; -; mRNA.
DR EMBL; AC011473; AAG23256.1; -; Genomic_DNA.
DR EMBL; BC002710; AAH02710.1; -; mRNA.
DR CCDS; CCDS12817.1; -.
DR RefSeq; NP_001070968.1; NM_001077500.1.
DR RefSeq; NP_002767.2; NM_002776.4.
DR RefSeq; NP_665895.1; NM_145888.2.
DR RefSeq; XP_005259118.1; XM_005259061.3.
DR RefSeq; XP_005259119.1; XM_005259062.3.
DR RefSeq; XP_006723350.1; XM_006723287.3.
DR RefSeq; XP_006723352.1; XM_006723289.3.
DR RefSeq; XP_016882482.1; XM_017026993.1.
DR PDB; 5LPE; X-ray; 2.65 A; A/B=43-276.
DR PDB; 5LPF; X-ray; 2.70 A; A/B=43-276.
DR PDBsum; 5LPE; -.
DR PDBsum; 5LPF; -.
DR AlphaFoldDB; O43240; -.
DR SMR; O43240; -.
DR BioGRID; 111636; 209.
DR IntAct; O43240; 16.
DR STRING; 9606.ENSP00000311746; -.
DR MEROPS; C06.001; -.
DR MEROPS; S01.246; -.
DR GlyGen; O43240; 1 site.
DR iPTMnet; O43240; -.
DR PhosphoSitePlus; O43240; -.
DR BioMuta; KLK10; -.
DR EPD; O43240; -.
DR MassIVE; O43240; -.
DR MaxQB; O43240; -.
DR PaxDb; O43240; -.
DR PeptideAtlas; O43240; -.
DR PRIDE; O43240; -.
DR ProteomicsDB; 48821; -.
DR Antibodypedia; 1705; 365 antibodies from 30 providers.
DR DNASU; 5655; -.
DR Ensembl; ENST00000309958.7; ENSP00000311746.2; ENSG00000129451.12.
DR Ensembl; ENST00000358789.8; ENSP00000351640.2; ENSG00000129451.12.
DR Ensembl; ENST00000391805.5; ENSP00000375681.1; ENSG00000129451.12.
DR GeneID; 5655; -.
DR KEGG; hsa:5655; -.
DR MANE-Select; ENST00000358789.8; ENSP00000351640.2; NM_145888.3; NP_665895.1.
DR UCSC; uc002puy.4; human.
DR CTD; 5655; -.
DR DisGeNET; 5655; -.
DR GeneCards; KLK10; -.
DR HGNC; HGNC:6358; KLK10.
DR HPA; ENSG00000129451; Group enriched (esophagus, vagina).
DR MIM; 602673; gene.
DR neXtProt; NX_O43240; -.
DR OpenTargets; ENSG00000129451; -.
DR PharmGKB; PA30147; -.
DR VEuPathDB; HostDB:ENSG00000129451; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00930000151066; -.
DR HOGENOM; CLU_006842_1_1_1; -.
DR InParanoid; O43240; -.
DR OMA; NNKPLWA; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; O43240; -.
DR TreeFam; TF331065; -.
DR BRENDA; 3.4.21.B41; 2681.
DR PathwayCommons; O43240; -.
DR SignaLink; O43240; -.
DR BioGRID-ORCS; 5655; 10 hits in 1071 CRISPR screens.
DR ChiTaRS; KLK10; human.
DR GeneWiki; KLK10; -.
DR GenomeRNAi; 5655; -.
DR Pharos; O43240; Tbio.
DR PRO; PR:O43240; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O43240; protein.
DR Bgee; ENSG00000129451; Expressed in lower esophagus mucosa and 113 other tissues.
DR ExpressionAtlas; O43240; baseline and differential.
DR Genevisible; O43240; HS.
DR GO; GO:0005576; C:extracellular region; TAS:ProtInc.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
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 3D-structure; Cell cycle; Disulfide bond; Glycoprotein; Hydrolase;
KW Protease; Reference proteome; Secreted; Serine protease; Signal;
KW Tumor suppressor.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..276
FT /note="Kallikrein-10"
FT /id="PRO_0000027953"
FT DOMAIN 47..274
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 86
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 137
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 229
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 52..162
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 71..87
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 169..235
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 201..215
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 225..250
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID ?..263
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT VARIANT 50
FT /note="S -> A (in dbSNP:rs3745535)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:8764136, ECO:0000269|PubMed:9647736"
FT /id="VAR_027979"
FT VARIANT 149
FT /note="L -> P (in dbSNP:rs2075690)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:8764136, ECO:0000269|PubMed:9647736"
FT /id="VAR_027980"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:5LPE"
FT STRAND 68..77
FT /evidence="ECO:0007829|PDB:5LPE"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:5LPE"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:5LPE"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:5LPE"
FT STRAND 107..117
FT /evidence="ECO:0007829|PDB:5LPE"
FT STRAND 139..145
FT /evidence="ECO:0007829|PDB:5LPE"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:5LPE"
FT STRAND 168..173
FT /evidence="ECO:0007829|PDB:5LPE"
FT STRAND 189..195
FT /evidence="ECO:0007829|PDB:5LPE"
FT TURN 198..200
FT /evidence="ECO:0007829|PDB:5LPE"
FT HELIX 201..204
FT /evidence="ECO:0007829|PDB:5LPE"
FT STRAND 211..218
FT /evidence="ECO:0007829|PDB:5LPE"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:5LPE"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:5LPE"
FT STRAND 238..245
FT /evidence="ECO:0007829|PDB:5LPE"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:5LPF"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:5LPE"
FT STRAND 257..261
FT /evidence="ECO:0007829|PDB:5LPE"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:5LPE"
FT HELIX 266..272
FT /evidence="ECO:0007829|PDB:5LPE"
SQ SEQUENCE 276 AA; 30170 MW; 4CFB32E0AF686E96 CRC64;
MRAPHLHLSA ASGARALAKL LPLLMAQLWA AEAALLPQND TRLDPEAYGS PCARGSQPWQ
VSLFNGLSFH CAGVLVDQSW VLTAAHCGNK PLWARVGDDH LLLLQGEQLR RTTRSVVHPK
YHQGSGPILP RRTDEHDLML LKLARPVVLG PRVRALQLPY RCAQPGDQCQ VAGWGTTAAR
RVKYNKGLTC SSITILSPKE CEVFYPGVVT NNMICAGLDR GQDPCQSDSG GPLVCDETLQ
GILSWGVYPC GSAQHPAVYT QICKYMSWIN KVIRSN
