ID KLK15_SAGOE Reviewed; 255 AA.
AC Q7JIG6;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 22-FEB-2023, entry version 58.
DE RecName: Full=Kallikrein-15;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN Name=KLK15;
OS Saguinus oedipus (Cotton-top tamarin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Saguinus.
OX NCBI_TaxID=9490;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15588589; DOI=10.1016/j.gene.2004.09.020;
RA Olsson A.Y., Valtonen-Andre C., Lilja H., Lundwall A.;
RT "The evolution of the glandular kallikrein locus: identification of
RT orthologs and pseudogenes in the cotton-top tamarin.";
RL Gene 343:347-355(2004).
CC -!- FUNCTION: Protease whose physiological substrate is not yet known.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Kallikrein subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; AF173845; AAS45302.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7JIG6; -.
DR SMR; Q7JIG6; -.
DR MEROPS; S01.081; -.
DR GlyCosmos; Q7JIG6; 2 sites, No reported glycans.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
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 PANTHER; PTHR24271:SF60; KALLIKREIN-15; 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.
PE 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Hydrolase; Protease; Secreted;
KW Serine protease; Signal; Zymogen.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT PROPEP 16..20
FT /note="Activation peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000027962"
FT CHAIN 21..255
FT /note="Kallikrein-15"
FT /id="PRO_0000027963"
FT REGION 21..253
FT /note="Serine protease"
FT ACT_SITE 61
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 105
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 208
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 46..62
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 137..214
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 179..193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 204..229
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 255 AA; 28078 MW; A040914ABC8FEC8D CRC64;
MWLLLPLSFL LTSTAQDGGK LLEGEECAPH SQPWQVALYE RGRFNCGASL ISPHWVLSAA
HCQSRFMRVR LGEHNLRKRD GPEQLRTASR VIPHPRYEAR SHRHDIMLLR LVQPARLTPQ
VRPVVLPTRC PHPGEACVVS GWGLVSHNEP GTTGRPQSQV SLPDTLHCAN ISIISDASCD
KNYPGRLTNT MVCAGAEGRG AESCEGDSGG PLVCGGILQG IVSWGDVPCD NTTKPGVYTK
VCRYVKWIRE TMKRN
//
