ID KLK2_HORSE Reviewed; 261 AA. AC Q6H321; Q8WMN9; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 122. DE RecName: Full=Kallikrein-1E2; DE EC=3.4.21.35; DE AltName: Full=Glandular kallikrein; DE AltName: Full=HPK; DE Flags: Precursor; GN Name=KLK1E2; OS Equus caballus (Horse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus. OX NCBI_TaxID=9796; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Prostate; RX PubMed=15203212; DOI=10.1016/j.ygeno.2004.01.009; RA Olsson A.Y., Lilja H., Lundwall A.; RT "Taxon-specific evolution of glandular kallikrein genes and identification RT of a progenitor of prostate-specific antigen."; RL Genomics 84:147-156(2004). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 62-252, SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, AND X-RAY CRYSTALLOGRAPHY (1.42 ANGSTROMS) OF 25-261. RC TISSUE=Prostate; RX PubMed=12217694; DOI=10.1016/s0022-2836(02)00705-2; RA Carvalho A.L., Sanz L., Barettino D., Romero A., Calvete J.J., Romao M.J.; RT "Crystal structure of a prostate kallikrein isolated from stallion seminal RT plasma: a homologue of human PSA."; RL J. Mol. Biol. 322:325-337(2002). CC -!- FUNCTION: Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in CC kininogen to release Lys-bradykinin. 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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12217694}. CC -!- TISSUE SPECIFICITY: Detected in prostate and semen. CC {ECO:0000269|PubMed:12217694}. 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; AY290704; AAQ23714.1; -; mRNA. DR EMBL; AJ428063; CAD20985.1; -; mRNA. DR RefSeq; NP_001075362.1; NM_001081893.1. DR PDB; 1GVZ; X-ray; 1.42 A; A=25-261. DR PDBsum; 1GVZ; -. DR AlphaFoldDB; Q6H321; -. DR SMR; Q6H321; -. DR STRING; 9796.ENSECAP00000009529; -. DR MEROPS; S01.171; -. DR GlyCosmos; Q6H321; 1 site, No reported glycans. DR PaxDb; 9796-ENSECAP00000009529; -. DR GeneID; 100034023; -. DR KEGG; ecb:100034023; -. DR CTD; 100034023; -. DR HOGENOM; CLU_006842_1_1_1; -. DR InParanoid; Q6H321; -. DR OrthoDB; 4629979at2759; -. DR TreeFam; TF331065; -. DR EvolutionaryTrace; Q6H321; -. DR Proteomes; UP000002281; Unplaced. 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; IEA:UniProtKB-EC. 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 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. PE 1: Evidence at protein level; KW 3D-structure; Disulfide bond; Glycoprotein; Hydrolase; Protease; KW Reference proteome; Secreted; Serine protease; Signal; Zymogen. FT SIGNAL 1..17 FT /evidence="ECO:0000305" FT PROPEP 18..24 FT /note="Activation peptide" FT /evidence="ECO:0000305" FT /id="PRO_0000027921" FT CHAIN 25..261 FT /note="Kallikrein-1E2" FT /id="PRO_0000027922" FT DOMAIN 25..258 FT /note="Peptidase S1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT ACT_SITE 65 FT /note="Charge relay system" FT /evidence="ECO:0000250" FT ACT_SITE 120 FT /note="Charge relay system" FT /evidence="ECO:0000250" FT ACT_SITE 213 FT /note="Charge relay system" FT /evidence="ECO:0000250" FT CARBOHYD 79 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 31..173 FT DISULFID 50..66 FT DISULFID 152..219 FT DISULFID 184..198 FT DISULFID 209..234 FT CONFLICT 82 FT /note="E -> K (in Ref. 2; CAD20985)" FT /evidence="ECO:0000305" FT CONFLICT 250 FT /note="L -> K (in Ref. 2)" FT /evidence="ECO:0000305" FT STRAND 39..44 FT /evidence="ECO:0007829|PDB:1GVZ" FT STRAND 47..56 FT /evidence="ECO:0007829|PDB:1GVZ" FT STRAND 59..62 FT /evidence="ECO:0007829|PDB:1GVZ" FT HELIX 64..66 FT /evidence="ECO:0007829|PDB:1GVZ" FT STRAND 72..76 FT /evidence="ECO:0007829|PDB:1GVZ" FT STRAND 88..90 FT /evidence="ECO:0007829|PDB:1GVZ" FT STRAND 92..97 FT /evidence="ECO:0007829|PDB:1GVZ" FT HELIX 103..107 FT /evidence="ECO:0007829|PDB:1GVZ" FT STRAND 122..128 FT /evidence="ECO:0007829|PDB:1GVZ" FT STRAND 151..158 FT /evidence="ECO:0007829|PDB:1GVZ" FT TURN 162..164 FT /evidence="ECO:0007829|PDB:1GVZ" FT STRAND 166..179 FT /evidence="ECO:0007829|PDB:1GVZ" FT HELIX 181..184 FT /evidence="ECO:0007829|PDB:1GVZ" FT HELIX 189..191 FT /evidence="ECO:0007829|PDB:1GVZ" FT STRAND 196..200 FT /evidence="ECO:0007829|PDB:1GVZ" FT HELIX 210..212 FT /evidence="ECO:0007829|PDB:1GVZ" FT STRAND 216..219 FT /evidence="ECO:0007829|PDB:1GVZ" FT STRAND 222..227 FT /evidence="ECO:0007829|PDB:1GVZ" FT STRAND 231..233 FT /evidence="ECO:0007829|PDB:1GVZ" FT TURN 237..239 FT /evidence="ECO:0007829|PDB:1GVZ" FT STRAND 243..246 FT /evidence="ECO:0007829|PDB:1GVZ" FT HELIX 247..249 FT /evidence="ECO:0007829|PDB:1GVZ" FT HELIX 250..260 FT /evidence="ECO:0007829|PDB:1GVZ" SQ SEQUENCE 261 AA; 29392 MW; DD612F74EAE0CE49 CRC64; MWFLVLCLDL SLGETGALPP IQSRIIGGWE CEKHSKPWQV AVYHQGHFQC GGVLVHPQWV LTAAHCMSDD YQIWLGRHNL SEDEDTAQFH QVSDSFLDPQ FDLSLLKKKY LRPYDDISHD LMLLRLAQPA RITDAVKILD LPTQEPKLGS TCYTSGWGLI STFTNRGSGT LQCVELRLQS NEKCARAYPE KMTEFVLCAT HRDDSGSICL GDSGGALICD GVFQGITSWG YSECADFNDN FVFTKVMPHL KWIKETIEKN S //