ID A0A2K6P8X5_RHIRO Unreviewed; 464 AA.
AC A0A2K6P8X5;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Urokinase-type plasminogen activator {ECO:0000256|ARBA:ARBA00019414};
DE EC=3.4.21.73 {ECO:0000256|ARBA:ARBA00013183};
GN Name=PLAU {ECO:0000313|Ensembl:ENSRROP00000012998.1};
OS Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000012998.1, ECO:0000313|Proteomes:UP000233200};
RN [1] {ECO:0000313|Ensembl:ENSRROP00000012998.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Specifically cleaves the zymogen plasminogen to form the
CC active enzyme plasmin. {ECO:0000256|ARBA:ARBA00004018}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Specific cleavage of Arg-|-Val bond in plasminogen to form
CC plasmin.; EC=3.4.21.73; Evidence={ECO:0000256|ARBA:ARBA00000942};
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00121}.
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DR AlphaFoldDB; A0A2K6P8X5; -.
DR Ensembl; ENSRROT00000037121.1; ENSRROP00000012998.1; ENSRROG00000030786.1.
DR GeneTree; ENSGT01050000244971; -.
DR Proteomes; UP000233200; Unplaced.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00108; KR; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR Gene3D; 2.40.20.10; Plasminogen Kringle 4; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 3.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000001; Kringle.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR018056; Kringle_CS.
DR InterPro; IPR038178; Kringle_sf.
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; PTHR24264; TRYPSIN-RELATED; 1.
DR PANTHER; PTHR24264:SF38; UROKINASE-TYPE PLASMINOGEN ACTIVATOR; 1.
DR Pfam; PF00051; Kringle; 1.
DR Pfam; PF00089; Trypsin; 2.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR PRINTS; PR00018; KRINGLE.
DR SMART; SM00130; KR; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF57440; Kringle-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS00021; KRINGLE_1; 1.
DR PROSITE; PS50070; KRINGLE_2; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW Hydrolase {ECO:0000256|RuleBase:RU363034};
KW Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW ProRule:PRU00121}; Protease {ECO:0000256|RuleBase:RU363034};
KW Reference proteome {ECO:0000313|Proteomes:UP000233200};
KW Serine protease {ECO:0000256|RuleBase:RU363034}.
FT DOMAIN 30..112
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 140..457
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 464 AA; 51931 MW; 3595D1C7312A0AC9 CRC64;
MSNKYFSSIH WCNCPKKFGG QHCEIDKSKT CYEGNGHFYR GKASTDTMGR SCLAWNSATV
LQQIYHAHRS DALQLGLGKH NYCRNPDNRR QPWCYVQVGL KQLVQECMVH NCADGKKPSS
PPEELQFQCG QKTLKPRFKI IGGEFTTIEN QPWFAAIYRR HRGGSVTYVC GGSLISPCWV
VSATHCFMYG PGFLLFGSSA PPQTHPFLLP SKGFCLISPS SAPLLAAHGL GDKSCFEASR
EGRGSGRISW DCLMDFFSHS NYPKKEDYIV YLGRSRLNSN TQGEMKFEVE NLILHEDYSA
DTLAHHNDIA LLKIRSKEGR CAQPSRTIQT ICLPSMYNDP PFGTSCEITG FGKENSTDYL
YPEQLKMTVV KLISHQKCQQ PHYYGSEVTT KMLCAADPQW ETDSCQGDSG GPLVCSIQGH
MTLTGIVSWG RGCALKDKPG VYTRVSRFLP WIHSHTREEN GLAL
//