ID   KLK1_HUMAN              Reviewed;         262 AA.
AC   P06870; Q66US9; Q86U61; Q8TCV8; Q9BS53; Q9NQU4; Q9UD19; Q9UMJ1;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 2.
DT   24-JAN-2024, entry version 220.
DE   RecName: Full=Kallikrein-1;
DE            EC=3.4.21.35;
DE   AltName: Full=Kidney/pancreas/salivary gland kallikrein;
DE   AltName: Full=Tissue kallikrein;
DE   Flags: Precursor;
GN   Name=KLK1;
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] (ISOFORM 1), AND VARIANTS GLN-145 AND GLU-186.
RC   TISSUE=Pancreas;
RX   PubMed=3004571; DOI=10.1021/bi00348a030;
RA   Fukushima D., Kitamura N., Nakanishi S.;
RT   "Nucleotide sequence of cloned cDNA for human pancreatic kallikrein.";
RL   Biochemistry 24:8037-8043(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLN-145.
RC   TISSUE=Kidney;
RX   PubMed=2898948; DOI=10.1021/bi00409a003;
RA   Evans B.A., Yun Z.X., Close J.A., Tregear G.W., Kitamura N., Nakanishi S.,
RA   Callen D.F., Baker E., Hyland V.J., Sutherland G.R., Richards R.I.;
RT   "Structure and chromosomal localization of the human renal kallikrein
RT   gene.";
RL   Biochemistry 27:3124-3129(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Salivary gland;
RX   PubMed=2686621; DOI=10.1042/bj2620787;
RA   Angermann A., Bergmann C., Appelhans H.;
RT   "Cloning and expression of human salivary-gland kallikrein in Escherichia
RT   coli.";
RL   Biochem. J. 262:787-793(1989).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=7749372;
RA   Chen L.-M., Murray S.R., Chai K.X., Chao L., Chao J.;
RT   "Molecular cloning and characterization of a novel kallikrein transcript in
RT   colon and its distribution in human tissues.";
RL   Braz. J. Med. Biol. Res. 27:1829-1838(1994).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11006094; DOI=10.1006/bbrc.2000.3448;
RA   Yousef G.M., Chang A., Scorilas A., Diamandis E.P.;
RT   "Genomic organization of the human kallikrein gene family on chromosome
RT   19q13.3-q13.4.";
RL   Biochem. Biophys. Res. Commun. 276:125-133(2000).
RN   [6]
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   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS GLN-145 AND GLU-186.
RA   Li T., Du G., Dai Y.;
RT   "Kallikrein cDNA from the pancreas of a Chinese patient.";
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLN-145.
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLN-145.
RG   SeattleSNPs variation discovery resource;
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [10]
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   [11]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLN-145.
RC   TISSUE=Pancreas;
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   [12]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 18-262 (ISOFORM 1), AND VARIANTS GLN-145 AND
RP   GLU-186.
RC   TISSUE=Kidney;
RX   PubMed=3853975; DOI=10.1089/dna.1985.4.445;
RA   Baker A.R., Shine J.;
RT   "Human kidney kallikrein: cDNA cloning and sequence analysis.";
RL   DNA 4:445-450(1985).
RN   [13]
RP   PROTEIN SEQUENCE OF 25-262 (ISOFORM 1), AND GLYCOSYLATION AT SER-93;
RP   ASN-102; SER-104; ASN-108; ASN-165 AND SER-167.
RC   TISSUE=Urine;
RX   PubMed=3163150;
RA   Kellermann J., Lottspeich F., Geiger R., Deutzmann R.;
RT   "Human urinary kallikrein -- amino acid sequence and carbohydrate
RT   attachment sites.";
RL   Protein Seq. Data Anal. 1:177-182(1988).
RN   [14]
RP   PROTEIN SEQUENCE OF 25-262 (ISOFORM 1).
RC   TISSUE=Urine;
RX   PubMed=2666327; DOI=10.1111/j.1399-3011.1989.tb01277.x;
RA   Lu H.S., Lin F.-K., Chao L., Chao J.;
RT   "Human urinary kallikrein. Complete amino acid sequence and sites of
RT   glycosylation.";
RL   Int. J. Pept. Protein Res. 33:237-249(1989).
RN   [15]
RP   PROTEIN SEQUENCE OF 25-55 (ISOFORM 1).
RC   TISSUE=Urine;
RX   PubMed=393608;
RA   Lottspeich F., Geiger R., Henschen A., Kutzbach C.;
RT   "N-terminal amino acid sequence of human urinary kallikrein homology with
RT   other serine proteases.";
RL   Hoppe-Seyler's Z. Physiol. Chem. 360:1947-1950(1979).
RN   [16]
RP   PROTEIN SEQUENCE OF 28-47 (ISOFORM 1).
RC   TISSUE=Urine;
RX   PubMed=3635530; DOI=10.1093/oxfordjournals.jbchem.a135563;
RA   Takahashi S., Irie A., Katayama Y., Ito K., Miyake Y.;
RT   "N-terminal amino acid sequence of human urinary prokallikrein.";
RL   J. Biochem. 99:989-992(1986).
RN   [17]
RP   CLEAVES N.MENINGITIDIS NHBA (MICROBIAL INFECTION).
RX   PubMed=31369555; DOI=10.1371/journal.pone.0203234;
RA   Pantano E., Marchi S., Biagini M., Di Fede M., Nardi Dei V.,
RA   Rossi Paccani S., Pizza M., Cartocci E.;
RT   "NHBA is processed by kallikrein from human saliva.";
RL   PLoS ONE 14:e0203234-e0203234(2019).
RN   [18]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 25-262, GLYCOSYLATION AT ASN-108,
RP   AND DISULFIDE BONDS.
RX   PubMed=15651049; DOI=10.1002/prot.20368;
RA   Laxmikanthan G., Blaber S.I., Bernett M.J., Scarisbrick I.A., Juliano M.A.,
RA   Blaber M.;
RT   "1.70 A X-ray structure of human apo kallikrein 1: structural changes upon
RT   peptide inhibitor/substrate binding.";
RL   Proteins 58:802-814(2005).
RN   [19]
RP   CHARACTERIZATION OF VARIANTS HIS-77 AND GLN-145, AND POLYMORPHISM.
RX   PubMed=11912256; DOI=10.1681/asn.v134968;
RA   Slim R., Torremocha F., Moreau T., Pizard A., Hunt S.C., Vuagnat A.,
RA   Williams G.H., Gauthier F., Jeunemaitre X., Alhenc-Gelas F.;
RT   "Loss-of-function polymorphism of the human kallikrein gene with reduced
RT   urinary kallikrein activity.";
RL   J. Am. Soc. Nephrol. 13:968-976(2002).
RN   [20]
RP   POLYMORPHISM.
RX   PubMed=15765151; DOI=10.1172/jci23669;
RA   Azizi M., Boutouyrie P., Bissery A., Agharazii M., Verbeke F., Stern N.,
RA   Bura-Riviere A., Laurent S., Alhenc-Gelas F., Jeunemaitre X.;
RT   "Arterial and renal consequences of partial genetic deficiency in tissue
RT   kallikrein activity in humans.";
RL   J. Clin. Invest. 115:780-787(2005).
CC   -!- FUNCTION: Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in
CC       kininogen to release Lys-bradykinin.
CC   -!- FUNCTION: (Microbial infection) Cleaves Neisseria meningitidis NHBA in
CC       saliva; Neisseria is an obligate commensal of the nasopharyngeal
CC       mucosa. {ECO:0000269|PubMed:31369555}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage of Arg-|-Xaa bonds in small molecule
CC         substrates. Highly selective action to release kallidin (lysyl-
CC         bradykinin) from kininogen involves hydrolysis of Met-|-Xaa or Leu-|-
CC         Xaa.; EC=3.4.21.35;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P06870-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P06870-2; Sequence=VSP_037483;
CC   -!- TISSUE SPECIFICITY: Isoform 2 is expressed in pancreas, salivary
CC       glands, kidney, colon, prostate gland, testis, spleen and the colon
CC       adenocarcinoma cell line T84. {ECO:0000269|PubMed:7749372}.
CC   -!- PTM: The O-linked polysaccharides on Ser-93, Ser-104 and Ser-167 are
CC       probably the mucin type linked to GalNAc. In PubMed:3163150, GalNAc was
CC       detected with the corresponding peptides but not located.
CC       {ECO:0000269|PubMed:15651049, ECO:0000269|PubMed:3163150}.
CC   -!- POLYMORPHISM: Genetic variations in KLK1 are the cause of a decreased
CC       in urinary kallikrein activity [MIM:615953]. The His-77 mutation
CC       dramatically reduces the activity of the enzyme in the urine. There is
CC       a 50 to 60% reduction in urinary kallikrein activity in His-77
CC       individuals, but renal and hormonal adaptation to dietary changes in
CC       sodium and potassium are unaffected. However, in studies of brachial
CC       artery function, His-77 individuals consistently exhibited an increase
CC       in wall shear stress and a paradoxical reduction in artery diameter and
CC       lumen compared to Arg-77 individuals. This partial genetic deficiency
CC       in kallikrein activity is associated with a form of arterial
CC       dysfunction involving inappropriate inward remodeling of the brachial
CC       artery despite a chronic increase in shear stress.
CC       {ECO:0000269|PubMed:11912256, ECO:0000269|PubMed:15765151}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Kallikrein subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Kallikrein entry;
CC       URL="https://en.wikipedia.org/wiki/Kallikrein";
CC   -!- WEB RESOURCE: Name=SeattleSNPs;
CC       URL="http://pga.gs.washington.edu/data/klk1/";
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DR   EMBL; M25629; AAA36136.1; -; mRNA.
DR   EMBL; M33109; AAA59455.1; -; Genomic_DNA.
DR   EMBL; M33105; AAA59455.1; JOINED; Genomic_DNA.
DR   EMBL; M33106; AAA59455.1; JOINED; Genomic_DNA.
DR   EMBL; M33107; AAA59455.1; JOINED; Genomic_DNA.
DR   EMBL; M33108; AAA59455.1; JOINED; Genomic_DNA.
DR   EMBL; X13561; CAA31912.1; -; mRNA.
DR   EMBL; AF277050; AAF86333.1; -; Genomic_DNA.
DR   EMBL; AF243527; AAG33353.1; -; Genomic_DNA.
DR   EMBL; AY703451; AAU12569.1; -; mRNA.
DR   EMBL; BT007253; AAP35917.1; -; mRNA.
DR   EMBL; AY094609; AAM11874.1; -; Genomic_DNA.
DR   EMBL; AC010325; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC005313; AAH05313.1; -; mRNA.
DR   EMBL; M12706; AAA59201.1; -; mRNA.
DR   CCDS; CCDS12804.1; -. [P06870-1]
DR   PIR; A24696; KQHU.
DR   PIR; B24696; B24696.
DR   RefSeq; NP_002248.1; NM_002257.3. [P06870-1]
DR   PDB; 1SPJ; X-ray; 1.70 A; A=25-262.
DR   PDBsum; 1SPJ; -.
DR   AlphaFoldDB; P06870; -.
DR   SMR; P06870; -.
DR   BioGRID; 110016; 48.
DR   STRING; 9606.ENSP00000301420; -.
DR   BindingDB; P06870; -.
DR   ChEMBL; CHEMBL2319; -.
DR   DrugBank; DB01370; Aluminium.
DR   DrugBank; DB14517; Aluminium phosphate.
DR   DrugBank; DB14518; Aluminum acetate.
DR   DrugBank; DB06728; Aniline.
DR   DrugBank; DB06692; Aprotinin.
DR   DrugBank; DB03127; Benzamidine.
DR   DrugBank; DB06245; Lanoteplase.
DR   DrugBank; DB12598; Nafamostat.
DR   DrugCentral; P06870; -.
DR   GuidetoPHARMACOLOGY; 2865; -.
DR   MEROPS; S01.160; -.
DR   GlyConnect; 172; 15 N-Linked glycans.
DR   GlyCosmos; P06870; 6 sites, 28 glycans.
DR   GlyGen; P06870; 7 sites, 28 N-linked glycans (4 sites).
DR   iPTMnet; P06870; -.
DR   PhosphoSitePlus; P06870; -.
DR   BioMuta; KLK1; -.
DR   DMDM; 269849612; -.
DR   jPOST; P06870; -.
DR   MassIVE; P06870; -.
DR   PaxDb; 9606-ENSP00000301420; -.
DR   PeptideAtlas; P06870; -.
DR   PRIDE; P06870; -.
DR   ProteomicsDB; 51938; -. [P06870-1]
DR   ProteomicsDB; 51939; -. [P06870-2]
DR   Antibodypedia; 32372; 468 antibodies from 37 providers.
DR   DNASU; 3816; -.
DR   Ensembl; ENST00000301420.3; ENSP00000301420.1; ENSG00000167748.11. [P06870-1]
DR   GeneID; 3816; -.
DR   KEGG; hsa:3816; -.
DR   MANE-Select; ENST00000301420.3; ENSP00000301420.1; NM_002257.4; NP_002248.1.
DR   UCSC; uc002ptk.3; human. [P06870-1]
DR   AGR; HGNC:6357; -.
DR   CTD; 3816; -.
DR   DisGeNET; 3816; -.
DR   GeneCards; KLK1; -.
DR   HGNC; HGNC:6357; KLK1.
DR   HPA; ENSG00000167748; Group enriched (pancreas, salivary gland).
DR   MalaCards; KLK1; -.
DR   MIM; 147910; gene.
DR   MIM; 615953; phenotype.
DR   neXtProt; NX_P06870; -.
DR   OpenTargets; ENSG00000167748; -.
DR   PharmGKB; PA224; -.
DR   VEuPathDB; HostDB:ENSG00000167748; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   GeneTree; ENSGT01020000230389; -.
DR   HOGENOM; CLU_006842_1_1_1; -.
DR   InParanoid; P06870; -.
DR   OMA; FMLCAGQ; -.
DR   OrthoDB; 4629979at2759; -.
DR   PhylomeDB; P06870; -.
DR   TreeFam; TF331065; -.
DR   BRENDA; 3.4.21.35; 2681.
DR   PathwayCommons; P06870; -.
DR   Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   SignaLink; P06870; -.
DR   BioGRID-ORCS; 3816; 6 hits in 1157 CRISPR screens.
DR   ChiTaRS; KLK1; human.
DR   EvolutionaryTrace; P06870; -.
DR   GeneWiki; KLK1; -.
DR   GenomeRNAi; 3816; -.
DR   Pharos; P06870; Tchem.
DR   PRO; PR:P06870; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; P06870; Protein.
DR   Bgee; ENSG00000167748; Expressed in body of pancreas and 134 other cell types or tissues.
DR   ExpressionAtlas; P06870; baseline and differential.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0030141; C:secretory granule; IBA:GO_Central.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; TAS:ProtInc.
DR   GO; GO:0003073; P:regulation of systemic arterial blood pressure; IBA:GO_Central.
DR   GO; GO:0031638; P:zymogen activation; IBA:GO_Central.
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   InterPro; IPR033116; TRYPSIN_SER.
DR   PANTHER; PTHR24271:SF47; KALLIKREIN-1; 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   PROSITE; PS00135; TRYPSIN_SER; 1.
DR   Genevisible; P06870; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW   Serine protease; Signal; Zymogen.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000305"
FT   PROPEP          19..24
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000027923"
FT   CHAIN           25..262
FT                   /note="Kallikrein-1"
FT                   /id="PRO_0000027924"
FT   DOMAIN          25..259
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        65
FT                   /note="Charge relay system"
FT   ACT_SITE        120
FT                   /note="Charge relay system"
FT   ACT_SITE        214
FT                   /note="Charge relay system"
FT   CARBOHYD        93
FT                   /note="O-linked (GalNAc...) serine"
FT                   /evidence="ECO:0000269|PubMed:3163150"
FT   CARBOHYD        102
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:3163150"
FT   CARBOHYD        104
FT                   /note="O-linked (GalNAc...) serine"
FT                   /evidence="ECO:0000269|PubMed:3163150"
FT   CARBOHYD        108
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:15651049,
FT                   ECO:0000269|PubMed:3163150"
FT   CARBOHYD        165
FT                   /note="N-linked (GlcNAc...) asparagine; partial"
FT                   /evidence="ECO:0000269|PubMed:3163150"
FT   CARBOHYD        167
FT                   /note="O-linked (GalNAc...) serine"
FT                   /evidence="ECO:0000269|PubMed:3163150"
FT   DISULFID        31..174
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT                   ECO:0000269|PubMed:15651049"
FT   DISULFID        50..66
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT                   ECO:0000269|PubMed:15651049"
FT   DISULFID        153..220
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT                   ECO:0000269|PubMed:15651049"
FT   DISULFID        185..199
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT                   ECO:0000269|PubMed:15651049"
FT   DISULFID        210..235
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT                   ECO:0000269|PubMed:15651049"
FT   VAR_SEQ         1..69
FT                   /note="MWFLVLCLALSLGGTGAAPPIQSRIVGGWECEQHSQPWQAALYHFSTFQCGG
FT                   ILVHRQWVLTAAHCISD -> MLPCPIPFSPSRLLIPPFPSFPS (in isoform
FT                   2)"
FT                   /evidence="ECO:0000303|PubMed:7749372"
FT                   /id="VSP_037483"
FT   VARIANT         77
FT                   /note="R -> H (associated with a significant decrease in
FT                   urinary kallikrein activity; dbSNP:rs5515)"
FT                   /evidence="ECO:0000269|PubMed:11912256"
FT                   /id="VAR_014567"
FT   VARIANT         145
FT                   /note="E -> Q (not associated with changes in urinary
FT                   kallikrein activity; dbSNP:rs5516)"
FT                   /evidence="ECO:0000269|PubMed:11912256,
FT                   ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:2898948,
FT                   ECO:0000269|PubMed:3004571, ECO:0000269|PubMed:3853975,
FT                   ECO:0000269|Ref.7, ECO:0000269|Ref.8, ECO:0000269|Ref.9"
FT                   /id="VAR_006625"
FT   VARIANT         186
FT                   /note="K -> E (in dbSNP:rs5517)"
FT                   /evidence="ECO:0000269|PubMed:3004571,
FT                   ECO:0000269|PubMed:3853975, ECO:0000269|Ref.7"
FT                   /id="VAR_006626"
FT   VARIANT         193
FT                   /note="V -> E (in dbSNP:rs5518)"
FT                   /id="VAR_014568"
FT   CONFLICT        114
FT                   /note="D -> N (in Ref. 7; AAU12569)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        139
FT                   /note="V -> F (in Ref. 7; AAU12569)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        188
FT                   /note="A -> V (in Ref. 8; AAP35917 and 11; AAH05313)"
FT                   /evidence="ECO:0000305"
FT   STRAND          39..44
FT                   /evidence="ECO:0007829|PDB:1SPJ"
FT   STRAND          47..56
FT                   /evidence="ECO:0007829|PDB:1SPJ"
FT   STRAND          59..62
FT                   /evidence="ECO:0007829|PDB:1SPJ"
FT   HELIX           64..66
FT                   /evidence="ECO:0007829|PDB:1SPJ"
FT   STRAND          69..76
FT                   /evidence="ECO:0007829|PDB:1SPJ"
FT   STRAND          88..90
FT                   /evidence="ECO:0007829|PDB:1SPJ"
FT   STRAND          92..97
FT                   /evidence="ECO:0007829|PDB:1SPJ"
FT   HELIX           103..106
FT                   /evidence="ECO:0007829|PDB:1SPJ"
FT   TURN            112..114
FT                   /evidence="ECO:0007829|PDB:1SPJ"
FT   STRAND          122..128
FT                   /evidence="ECO:0007829|PDB:1SPJ"
FT   STRAND          152..159
FT                   /evidence="ECO:0007829|PDB:1SPJ"
FT   STRAND          161..165
FT                   /evidence="ECO:0007829|PDB:1SPJ"
FT   STRAND          173..180
FT                   /evidence="ECO:0007829|PDB:1SPJ"
FT   HELIX           182..188
FT                   /evidence="ECO:0007829|PDB:1SPJ"
FT   STRAND          197..201
FT                   /evidence="ECO:0007829|PDB:1SPJ"
FT   STRAND          206..208
FT                   /evidence="ECO:0007829|PDB:1SPJ"
FT   STRAND          217..220
FT                   /evidence="ECO:0007829|PDB:1SPJ"
FT   STRAND          223..230
FT                   /evidence="ECO:0007829|PDB:1SPJ"
FT   STRAND          242..246
FT                   /evidence="ECO:0007829|PDB:1SPJ"
FT   HELIX           247..250
FT                   /evidence="ECO:0007829|PDB:1SPJ"
FT   HELIX           251..260
FT                   /evidence="ECO:0007829|PDB:1SPJ"
SQ   SEQUENCE   262 AA;  28890 MW;  7D8A715E9E104D60 CRC64;
     MWFLVLCLAL SLGGTGAAPP IQSRIVGGWE CEQHSQPWQA ALYHFSTFQC GGILVHRQWV
     LTAAHCISDN YQLWLGRHNL FDDENTAQFV HVSESFPHPG FNMSLLENHT RQADEDYSHD
     LMLLRLTEPA DTITDAVKVV ELPTEEPEVG STCLASGWGS IEPENFSFPD DLQCVDLKIL
     PNDECKKAHV QKVTDFMLCV GHLEGGKDTC VGDSGGPLMC DGVLQGVTSW GYVPCGTPNK
     PSVAVRVLSY VKWIEDTIAE NS
//