ID   UROK_PAPCY              Reviewed;         433 AA.
AC   P16227;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   22-FEB-2023, entry version 138.
DE   RecName: Full=Urokinase-type plasminogen activator;
DE            Short=U-plasminogen activator;
DE            Short=uPA;
DE            EC=3.4.21.73;
DE   Contains:
DE     RecName: Full=Urokinase-type plasminogen activator long chain A;
DE   Contains:
DE     RecName: Full=Urokinase-type plasminogen activator short chain A;
DE   Contains:
DE     RecName: Full=Urokinase-type plasminogen activator chain B;
DE   Flags: Precursor;
GN   Name=PLAU;
OS   Papio cynocephalus (Yellow baboon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Papio.
OX   NCBI_TaxID=9556;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Thoracic aorta;
RX   PubMed=2113276; DOI=10.1093/nar/18.11.3411;
RA   Au Y.P.T., Wang T.W., Clowes A.W.;
RT   "Nucleotide and deduced amino acid sequences of baboon urokinase-type
RT   plasminogen activator.";
RL   Nucleic Acids Res. 18:3411-3411(1990).
CC   -!- FUNCTION: Specifically cleaves the zymogen plasminogen to form the
CC       active enzyme plasmin. {ECO:0000250|UniProtKB:P00749}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Specific cleavage of Arg-|-Val bond in plasminogen to form
CC         plasmin.; EC=3.4.21.73;
CC   -!- ACTIVITY REGULATION: Inhibited by SERPINA5.
CC       {ECO:0000250|UniProtKB:P00749}.
CC   -!- SUBUNIT: Found in high and low molecular mass forms. Each consists of
CC       two chains, A and B. The high molecular mass form contains a long chain
CC       A which is cleaved to yield a short chain A. Forms heterodimer with
CC       SERPINA5. Binds LRP1B; binding is followed by internalization and
CC       degradation. Interacts with MRC2. Interacts with PLAUR. In complex with
CC       SERPINE1, interacts with PLAUR/uPAR. Interacts with SORL1 and LRP1,
CC       either alone or in complex with SERPINE1; these interactions are
CC       abolished in the presence of LRPAP1/RAP. The ternary complex composed
CC       of PLAUR-PLAU-PAI1 also interacts with SORLA.
CC       {ECO:0000250|UniProtKB:P00749}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P00749}.
CC   -!- PTM: Phosphorylation of Ser-157 and Ser-325 abolishes proadhesive
CC       ability but does not interfere with receptor binding. {ECO:0000250}.
CC   -!- PTM: Produced as an inactive single-chain protein (pro-uPA or sc-uPA),
CC       is processed into the active disulfide-linked two-chain form of
CC       PLAU/uPA by a proteolytic event mediated, at least, by TMPRSS4.
CC       {ECO:0000250|UniProtKB:P00749}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X51935; CAA36200.1; -; mRNA.
DR   PIR; S14687; UKBAY.
DR   AlphaFoldDB; P16227; -.
DR   SMR; P16227; -.
DR   MEROPS; S01.231; -.
DR   GlyCosmos; P16227; 1 site, No reported glycans.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
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; 2.
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; 1.
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; PS50026; EGF_3; 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   2: Evidence at transcript level;
KW   Disulfide bond; EGF-like domain; Glycoprotein; Hydrolase; Kringle;
KW   Phosphoprotein; Plasminogen activation; Protease; Secreted;
KW   Serine protease; Signal; Zymogen.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..433
FT                   /note="Urokinase-type plasminogen activator"
FT                   /id="PRO_0000028326"
FT   CHAIN           21..176
FT                   /note="Urokinase-type plasminogen activator long chain A"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000028327"
FT   CHAIN           155..176
FT                   /note="Urokinase-type plasminogen activator short chain A"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000028328"
FT   CHAIN           178..433
FT                   /note="Urokinase-type plasminogen activator chain B"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000028329"
FT   DOMAIN          26..62
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          69..150
FT                   /note="Kringle"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT   DOMAIN          178..426
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   REGION          33..56
FT                   /note="Binds urokinase plasminogen activator surface
FT                   receptor"
FT                   /evidence="ECO:0000250"
FT   REGION          151..177
FT                   /note="Connecting peptide"
FT   ACT_SITE        223
FT                   /note="Charge relay system"
FT   ACT_SITE        274
FT                   /note="Charge relay system"
FT   ACT_SITE        378
FT                   /note="Charge relay system"
FT   MOD_RES         157
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P00749"
FT   MOD_RES         325
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P00749"
FT   CARBOHYD        324
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        30..38
FT                   /evidence="ECO:0000250"
FT   DISULFID        32..50
FT                   /evidence="ECO:0000250"
FT   DISULFID        52..61
FT                   /evidence="ECO:0000250"
FT   DISULFID        69..150
FT                   /evidence="ECO:0000250"
FT   DISULFID        90..132
FT                   /evidence="ECO:0000250"
FT   DISULFID        121..145
FT                   /evidence="ECO:0000250"
FT   DISULFID        167..298
FT                   /note="Interchain (between A and B chains)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076,
FT                   ECO:0000255|PROSITE-ProRule:PRU00121, ECO:0000255|PROSITE-
FT                   ProRule:PRU00274"
FT   DISULFID        208..224
FT                   /evidence="ECO:0000250"
FT   DISULFID        216..287
FT                   /evidence="ECO:0000250"
FT   DISULFID        315..384
FT                   /evidence="ECO:0000250"
FT   DISULFID        347..363
FT                   /evidence="ECO:0000250"
FT   DISULFID        374..402
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   433 AA;  48595 MW;  816D22DFEDDC8792 CRC64;
     MRALLAHLLL CVLVVSASKG SRELQVPSDC GCLNGGTCMS NKYFSSIHWC NCPKKFGGQH
     CEIDKSKTCY EGNGHFYRGK ASTDTMGRSC LAWNSATVLQ QTYHAHRSDA LQLGLGKHNY
     CRNPDNRRRP WCYVQVGLKQ RVQECMVHNC ADGKKPSSPP EELQFQCGQR TLRPRFKIVG
     GEFTTIENQP WFAAIYRRHR GGSVTYVCGG SLISPCWVVS ATHCFINYPK KEDYIVYLGR
     SRLNSNTQGE MKFEVENLIL HEDYSADTLA HHNDIALLKI RSKEGRCAQP SRTIQTICLP
     SMYNDPNDPP FGTSCEITGF GKENSTDYLY PEQLKMTVVK LVSHQKCQQP HYYGSEVTTK
     MLCAADPQWE TDSCQGDSGG PLVCSIQGHM TLTGIVSWGR GCALKDKPGV YTRVSRFLPW
     IHSHTREQNG LAL
//