PRS45_BOVIN
ID PRS45_BOVIN Reviewed; 316 AA.
AC A2VE36;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=Serine protease 45;
DE EC=3.4.21.-;
DE AltName: Full=Testis serine protease 5;
DE Flags: Precursor;
GN Name=PRSS45; Synonyms=TESSP5;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; BC133553; AAI33554.1; -; mRNA.
DR RefSeq; NP_001075924.1; NM_001082455.2.
DR AlphaFoldDB; A2VE36; -.
DR SMR; A2VE36; -.
DR STRING; 9913.ENSBTAP00000005550; -.
DR MEROPS; S01.326; -.
DR PaxDb; A2VE36; -.
DR GeneID; 540798; -.
DR KEGG; bta:540798; -.
DR CTD; 260408; -.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; A2VE36; -.
DR OrthoDB; 1314811at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; 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 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.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW Secreted; Serine protease; Signal.
FT SIGNAL 1..38
FT /evidence="ECO:0000255"
FT CHAIN 39..316
FT /note="Serine protease 45"
FT /id="PRO_0000349306"
FT DOMAIN 49..290
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 89
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 137
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 242
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 74..90
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 171..248
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 206..229
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 238..266
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 316 AA; 35251 MW; 80393E157BFBA49F CRC64;
MAASLSRLSA GLAASRPLGL SRSFLLLVLL LLNSGYKGDS TKPACGQPWW PKNLDLSRHW
PWEVSLRVGN EHVCGGALID LKWVVTAAHC IQGTKEYSVI LGTSKLKPPN STRTLLIPVR
DIIMHPKYWG RTFIMGDVAL LQLYNPVIIS KYVQPICLPE PNYSLKVGTK CWVTGWGQVK
QRFSANSTLA SELQEAEVFI MDNKKCDQIY RKKSHIPRVV PLVLGDMICA TNYREDLCSG
DSGGPLACEV EGRWILAGVL SWEKACAKVR NPGVYTRITK YSRWIKKQIS NGILSVPCTS
AWLLLLFWLL QPQMGP
