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 13-FEB-2019, entry version 156. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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 RT of 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 RT cell-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., RA Moss P., Paeper B., Wang K.; RT "Sequencing and expression analysis of the serine protease gene RT cluster 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 RT the 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., RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M., RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., RA 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 RP 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 RT project: 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 CC prostate cancer. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. CC -!- TISSUE SPECIFICITY: Expressed in breast, ovary and prostate. CC -!- DEVELOPMENTAL STAGE: Down-regulated during breast cancer CC progression. CC -!- SIMILARITY: Belongs to the peptidase S1 family. Kallikrein CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology CC and Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/KLK10ID41076ch19q13.html"; 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; 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 UniGene; Hs.275464; -. 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 ProteinModelPortal; O43240; -. DR SMR; O43240; -. DR BioGrid; 111636; 17. DR IntAct; O43240; 2. DR STRING; 9606.ENSP00000311746; -. DR MEROPS; S01.246; -. DR iPTMnet; O43240; -. DR PhosphoSitePlus; O43240; -. DR BioMuta; KLK10; -. DR EPD; O43240; -. DR MaxQB; O43240; -. DR PaxDb; O43240; -. DR PeptideAtlas; O43240; -. DR PRIDE; O43240; -. DR ProteomicsDB; 48821; -. DR DNASU; 5655; -. DR Ensembl; ENST00000309958; ENSP00000311746; ENSG00000129451. DR Ensembl; ENST00000358789; ENSP00000351640; ENSG00000129451. DR Ensembl; ENST00000391805; ENSP00000375681; ENSG00000129451. DR GeneID; 5655; -. DR KEGG; hsa:5655; -. DR UCSC; uc002puy.4; human. DR CTD; 5655; -. DR DisGeNET; 5655; -. DR EuPathDB; HostDB:ENSG00000129451.11; -. DR GeneCards; KLK10; -. DR H-InvDB; HIX0015374; -. DR HGNC; HGNC:6358; KLK10. DR HPA; HPA017195; -. DR MIM; 602673; gene. DR neXtProt; NX_O43240; -. DR OpenTargets; ENSG00000129451; -. DR PharmGKB; PA30147; -. DR eggNOG; KOG3627; Eukaryota. DR eggNOG; COG5640; LUCA. DR GeneTree; ENSGT00930000151066; -. DR HOGENOM; HOG000251820; -. DR HOVERGEN; HBG013304; -. DR InParanoid; O43240; -. DR KO; K09619; -. DR OMA; YNRSLSC; -. DR OrthoDB; 1314811at2759; -. DR PhylomeDB; O43240; -. DR TreeFam; TF331065; -. DR BRENDA; 3.4.21.B41; 2681. DR ChiTaRS; KLK10; human. DR GeneWiki; KLK10; -. DR GenomeRNAi; 5655; -. DR PRO; PR:O43240; -. DR Proteomes; UP000005640; Chromosome 19. DR Bgee; ENSG00000129451; Expressed in 119 organ(s), highest expression level in lower esophagus mucosa. 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 CDD; cd00190; Tryp_SPc; 1. DR InterPro; IPR009003; Peptidase_S1_PA. 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; Complete proteome; Disulfide bond; KW Glycoprotein; Hydrolase; Polymorphism; Protease; Reference proteome; KW Secreted; Serine protease; Signal; Tumor suppressor. FT SIGNAL 1 30 {ECO:0000255}. FT CHAIN 31 276 Kallikrein-10. FT /FTId=PRO_0000027953. FT DOMAIN 47 274 Peptidase S1. {ECO:0000255|PROSITE- FT ProRule:PRU00274}. FT ACT_SITE 86 86 Charge relay system. {ECO:0000250}. FT ACT_SITE 137 137 Charge relay system. {ECO:0000250}. FT ACT_SITE 229 229 Charge relay system. {ECO:0000250}. FT CARBOHYD 39 39 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 52 162 {ECO:0000255|PROSITE-ProRule:PRU00274}. FT DISULFID 71 87 {ECO:0000255|PROSITE-ProRule:PRU00274}. FT DISULFID 169 235 {ECO:0000255|PROSITE-ProRule:PRU00274}. FT DISULFID 201 215 {ECO:0000255|PROSITE-ProRule:PRU00274}. FT DISULFID 225 250 {ECO:0000255|PROSITE-ProRule:PRU00274}. FT DISULFID ? 263 {ECO:0000255|PROSITE-ProRule:PRU00274}. FT VARIANT 50 50 S -> A (in dbSNP:rs3745535). FT {ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:8764136, FT ECO:0000269|PubMed:9647736}. FT /FTId=VAR_027979. FT VARIANT 149 149 L -> P (in dbSNP:rs2075690). FT {ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:8764136, FT ECO:0000269|PubMed:9647736}. FT /FTId=VAR_027980. FT STRAND 60 65 {ECO:0000244|PDB:5LPE}. FT STRAND 68 77 {ECO:0000244|PDB:5LPE}. FT STRAND 80 83 {ECO:0000244|PDB:5LPE}. FT HELIX 85 87 {ECO:0000244|PDB:5LPE}. FT STRAND 93 96 {ECO:0000244|PDB:5LPE}. FT STRAND 107 117 {ECO:0000244|PDB:5LPE}. FT STRAND 139 145 {ECO:0000244|PDB:5LPE}. FT STRAND 151 153 {ECO:0000244|PDB:5LPE}. FT STRAND 168 173 {ECO:0000244|PDB:5LPE}. FT STRAND 189 195 {ECO:0000244|PDB:5LPE}. FT TURN 198 200 {ECO:0000244|PDB:5LPE}. FT HELIX 201 204 {ECO:0000244|PDB:5LPE}. FT STRAND 211 218 {ECO:0000244|PDB:5LPE}. FT HELIX 224 226 {ECO:0000244|PDB:5LPE}. FT STRAND 232 235 {ECO:0000244|PDB:5LPE}. FT STRAND 238 245 {ECO:0000244|PDB:5LPE}. FT STRAND 249 251 {ECO:0000244|PDB:5LPF}. FT STRAND 253 255 {ECO:0000244|PDB:5LPE}. FT STRAND 257 261 {ECO:0000244|PDB:5LPE}. FT HELIX 262 264 {ECO:0000244|PDB:5LPE}. FT HELIX 266 272 {ECO:0000244|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 //