PRS58_BOVIN
ID PRS58_BOVIN Reviewed; 242 AA.
AC Q32LI2;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Probable inactive serine protease 58;
DE AltName: Full=Trypsin-X3;
DE Flags: Precursor;
GN Name=PRSS58; Synonyms=TRYX3;
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 (NOV-2005) 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}.
CC -!- CAUTION: Asn-56 is present instead of the conserved His which is
CC expected to be an active site residue. Asn-102 is present instead of
CC the conserved Asp which is expected to be an active site residue. Thr-
CC 196 is present instead of the conserved Ser which is expected to be an
CC active site residue. It is therefore expected that this protein has
CC lost its catalytic activity. {ECO:0000305}.
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DR EMBL; BC109563; AAI09564.1; -; mRNA.
DR RefSeq; NP_001035599.1; NM_001040509.2.
DR AlphaFoldDB; Q32LI2; -.
DR SMR; Q32LI2; -.
DR STRING; 9913.ENSBTAP00000004732; -.
DR MEROPS; S01.085; -.
DR PaxDb; Q32LI2; -.
DR Ensembl; ENSBTAT00000004732; ENSBTAP00000004732; ENSBTAG00000003628.
DR GeneID; 506919; -.
DR KEGG; bta:506919; -.
DR CTD; 136541; -.
DR VEuPathDB; HostDB:ENSBTAG00000003628; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT01020000230389; -.
DR HOGENOM; CLU_006842_1_6_1; -.
DR InParanoid; Q32LI2; -.
DR OMA; RWCGGSI; -.
DR OrthoDB; 1314811at2759; -.
DR TreeFam; TF331065; -.
DR Proteomes; UP000009136; Chromosome 4.
DR Bgee; ENSBTAG00000003628; Expressed in semen and 8 other tissues.
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:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
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; IPR001254; Trypsin_dom.
DR Pfam; PF00089; Trypsin; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Reference proteome; Secreted;
KW Serine protease homolog; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..242
FT /note="Probable inactive serine protease 58"
FT /id="PRO_0000317762"
FT DOMAIN 18..240
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 41..57
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 134..202
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 166..181
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 192..216
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 242 AA; 27412 MW; 2781366AE1894BA0 CRC64;
MNLILLWALL NLPVALTFDP NYKDDITPPY LIYLKSDYLP CVGVLIHPLW VITAANCNLP
RLQLILGVTK PSNIDEEKYV QVVGYEKMIH HPQFSITSIE HNLMLIKLQT HIELNNYVKI
VSLPKEPAAE DDTCIVSTWA YNLCDHYKDP DSLQNVNISV ISKVECLKAY KYMHIRDSMM
CVGIVPGRRQ PCKEVTAAPA VCNGILQGIL TFADGCVLRA DVGIYTRIIN YIPWIENTIQ
NN
