KLK2_HORSE
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 03-AUG-2022, entry version 116.
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}.
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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 PaxDb; Q6H321; -.
DR GeneID; 100034023; -.
DR KEGG; ecb:100034023; -.
DR CTD; 100034023; -.
DR HOGENOM; CLU_006842_1_1_1; -.
DR InParanoid; Q6H321; -.
DR OMA; KWIKETI; -.
DR OrthoDB; 1314811at2759; -.
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: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; -; 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 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
