KLK13_HUMAN
ID KLK13_HUMAN Reviewed; 277 AA.
AC Q9UKR3; A7UNK6; Q86VI8; Q9Y433;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Kallikrein-13;
DE EC=3.4.21.-;
DE AltName: Full=Kallikrein-like protein 4;
DE Short=KLK-L4;
DE Flags: Precursor;
GN Name=KLK13; Synonyms=KLKL4;
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].
RX PubMed=10766816; DOI=10.1074/jbc.275.16.11891;
RA Yousef G.M., Chang A., Diamandis E.P.;
RT "Identification and characterization of KLK-L4, a new kallikrein-like gene
RT that appears to be down-regulated in breast cancer tissues.";
RL J. Biol. Chem. 275:11891-11898(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING.
RC TISSUE=Skin;
RX PubMed=12925213; DOI=10.1046/j.1523-1747.2003.12363.x;
RA Komatsu N., Takata M., Otsuki N., Toyama T., Ohka R., Takehara K.,
RA Saijoh K.;
RT "Expression and localization of tissue kallikrein mRNAs in human epidermis
RT and appendages.";
RL J. Invest. Dermatol. 121:542-549(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=17922479; DOI=10.1002/gepi.20185;
RA Andres A.M., Clark A.G., Shimmin L., Boerwinkle E., Sing C.F., Hixson J.E.;
RT "Understanding the accuracy of statistical haplotype inference with
RT sequence data of known phase.";
RL Genet. Epidemiol. 31:659-671(2007).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-169 (ISOFORM 1).
RC TISSUE=Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UKR3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UKR3-2; Sequence=VSP_056631;
CC -!- TISSUE SPECIFICITY: Expressed in prostate, breast, testis and salivary
CC gland.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Kallikrein subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; AF135024; AAD26425.2; -; Genomic_DNA.
DR EMBL; AB108823; BAC75825.1; -; mRNA.
DR EMBL; EU091477; ABU63130.1; -; Genomic_DNA.
DR EMBL; AC011473; AAG23259.1; -; Genomic_DNA.
DR EMBL; CH471135; EAW71979.1; -; Genomic_DNA.
DR EMBL; BC069334; AAH69334.1; -; mRNA.
DR EMBL; BC069543; AAH69543.1; -; mRNA.
DR EMBL; AL050220; CAB43320.2; -; mRNA.
DR CCDS; CCDS12822.1; -. [Q9UKR3-1]
DR CCDS; CCDS86794.1; -. [Q9UKR3-2]
DR PIR; T08808; T08808.
DR RefSeq; NP_001335107.1; NM_001348178.1. [Q9UKR3-2]
DR RefSeq; NP_056411.1; NM_015596.2. [Q9UKR3-1]
DR AlphaFoldDB; Q9UKR3; -.
DR SMR; Q9UKR3; -.
DR BioGRID; 117538; 17.
DR IntAct; Q9UKR3; 1.
DR STRING; 9606.ENSP00000470555; -.
DR BindingDB; Q9UKR3; -.
DR ChEMBL; CHEMBL4863; -.
DR MEROPS; S01.306; -.
DR GlyGen; Q9UKR3; 2 sites.
DR iPTMnet; Q9UKR3; -.
DR PhosphoSitePlus; Q9UKR3; -.
DR BioMuta; KLK13; -.
DR DMDM; 9296990; -.
DR MassIVE; Q9UKR3; -.
DR PaxDb; Q9UKR3; -.
DR PeptideAtlas; Q9UKR3; -.
DR PRIDE; Q9UKR3; -.
DR ProteomicsDB; 70027; -.
DR ProteomicsDB; 84840; -. [Q9UKR3-1]
DR Antibodypedia; 18982; 281 antibodies from 31 providers.
DR DNASU; 26085; -.
DR Ensembl; ENST00000335422.3; ENSP00000334079.3; ENSG00000167759.13. [Q9UKR3-2]
DR Ensembl; ENST00000595793.6; ENSP00000470555.1; ENSG00000167759.13. [Q9UKR3-1]
DR GeneID; 26085; -.
DR KEGG; hsa:26085; -.
DR MANE-Select; ENST00000595793.6; ENSP00000470555.1; NM_015596.3; NP_056411.1.
DR UCSC; uc002pvn.4; human. [Q9UKR3-1]
DR CTD; 26085; -.
DR DisGeNET; 26085; -.
DR GeneCards; KLK13; -.
DR HGNC; HGNC:6361; KLK13.
DR HPA; ENSG00000167759; Tissue enriched (esophagus).
DR MIM; 605505; gene.
DR neXtProt; NX_Q9UKR3; -.
DR OpenTargets; ENSG00000167759; -.
DR PharmGKB; PA30150; -.
DR VEuPathDB; HostDB:ENSG00000167759; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT01030000234551; -.
DR HOGENOM; CLU_006842_13_2_1; -.
DR InParanoid; Q9UKR3; -.
DR OMA; TNHIRVL; -.
DR PhylomeDB; Q9UKR3; -.
DR TreeFam; TF331065; -.
DR BRENDA; 3.4.21.119; 2681.
DR PathwayCommons; Q9UKR3; -.
DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-HSA-6809371; Formation of the cornified envelope.
DR SignaLink; Q9UKR3; -.
DR BioGRID-ORCS; 26085; 13 hits in 1073 CRISPR screens.
DR ChiTaRS; KLK13; human.
DR GeneWiki; KLK13; -.
DR GenomeRNAi; 26085; -.
DR Pharos; Q9UKR3; Tchem.
DR PRO; PR:Q9UKR3; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9UKR3; protein.
DR Bgee; ENSG00000167759; Expressed in lower esophagus mucosa and 114 other tissues.
DR ExpressionAtlas; Q9UKR3; baseline and differential.
DR Genevisible; Q9UKR3; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0030141; C:secretory granule; IBA:GO_Central.
DR GO; GO:0016787; F:hydrolase activity; IDA:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; NAS:UniProtKB.
DR GO; GO:0016485; P:protein processing; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; NAS:UniProtKB.
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 2: Evidence at transcript level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Secreted; Serine protease; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..277
FT /note="Kallikrein-13"
FT /id="PRO_0000027957"
FT DOMAIN 36..263
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 76
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 124
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 218
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 42..178
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 61..77
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 157..224
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 189..203
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 214..239
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT VAR_SEQ 18..169
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12925213"
FT /id="VSP_056631"
FT VARIANT 109
FT /note="H -> Y (in dbSNP:rs34089525)"
FT /id="VAR_051857"
SQ SEQUENCE 277 AA; 30570 MW; BA8A9E8DCFB5D542 CRC64;
MWPLALVIAS LTLALSGGVS QESSKVLNTN GTSGFLPGGY TCFPHSQPWQ AALLVQGRLL
CGGVLVHPKW VLTAAHCLKE GLKVYLGKHA LGRVEAGEQV REVVHSIPHP EYRRSPTHLN
HDHDIMLLEL QSPVQLTGYI QTLPLSHNNR LTPGTTCRVS GWGTTTSPQV NYPKTLQCAN
IQLRSDEECR QVYPGKITDN MLCAGTKEGG KDSCEGDSGG PLVCNRTLYG IVSWGDFPCG
QPDRPGVYTR VSRYVLWIRE TIRKYETQQQ KWLKGPQ
