ID UROK_CHICK Reviewed; 434 AA. AC P15120; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 27-MAR-2024, entry version 166. 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 chain A; DE Contains: DE RecName: Full=Urokinase-type plasminogen activator chain B; DE Flags: Precursor; GN Name=PLAU; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; OC Phasianinae; Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RX PubMed=2295632; DOI=10.1016/s0021-9258(19)40019-7; RA Leslie N.D., Kessler C.A., Bell S.M., Degen J.L.; RT "The chicken urokinase-type plasminogen activator gene."; RL J. Biol. Chem. 265:1339-1344(1990). CC -!- FUNCTION: Specifically cleaves the zymogen plasminogen to form the CC active enzyme plasmin. CC -!- CATALYTIC ACTIVITY: CC Reaction=Specific cleavage of Arg-|-Val bond in plasminogen to form CC plasmin.; EC=3.4.21.73; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. 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; J05187; AAA49131.1; -; mRNA. DR EMBL; J05188; AAA49130.1; -; Genomic_DNA. DR PIR; A35005; A35005. DR RefSeq; NP_990774.2; NM_205443.2. DR AlphaFoldDB; P15120; -. DR SMR; P15120; -. DR STRING; 9031.ENSGALP00000008143; -. DR MEROPS; S01.231; -. DR GlyCosmos; P15120; 1 site, No reported glycans. DR PaxDb; 9031-ENSGALP00000042397; -. DR Ensembl; ENSGALT00010051182.1; ENSGALP00010030373.1; ENSGALG00010021137.1. DR GeneID; 396424; -. DR KEGG; gga:396424; -. DR CTD; 5328; -. DR VEuPathDB; HostDB:geneid_396424; -. DR eggNOG; ENOG502QRMI; Eukaryota. DR GeneTree; ENSGT00940000164426; -. DR InParanoid; P15120; -. DR OMA; WPWCYVQ; -. DR OrthoDB; 4629979at2759; -. DR PhylomeDB; P15120; -. DR PRO; PR:P15120; -. DR Proteomes; UP000000539; Chromosome 6. 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:0031639; P:plasminogen activation; IBA:GO_Central. DR GO; GO:0033628; P:regulation of cell adhesion mediated by integrin; IBA:GO_Central. DR CDD; cd00054; EGF_CA; 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; 1. 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; PS01186; EGF_2; 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 Plasminogen activation; Protease; Reference proteome; Secreted; KW Serine protease; Signal; Zymogen. FT SIGNAL 1..20 FT /evidence="ECO:0000255" FT CHAIN 21..434 FT /note="Urokinase-type plasminogen activator" FT /id="PRO_0000028337" FT CHAIN 21..171 FT /note="Urokinase-type plasminogen activator chain A" FT /evidence="ECO:0000250" FT /id="PRO_0000028338" FT CHAIN 173..434 FT /note="Urokinase-type plasminogen activator chain B" FT /evidence="ECO:0000250" FT /id="PRO_0000028339" FT DOMAIN 36..72 FT /note="EGF-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 79..158 FT /note="Kringle" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121" FT DOMAIN 173..421 FT /note="Peptidase S1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT REGION 159..172 FT /note="Connecting peptide" FT ACT_SITE 217 FT /note="Charge relay system" FT /evidence="ECO:0000250" FT ACT_SITE 272 FT /note="Charge relay system" FT /evidence="ECO:0000250" FT ACT_SITE 373 FT /note="Charge relay system" FT /evidence="ECO:0000250" FT CARBOHYD 228 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 40..48 FT /evidence="ECO:0000250" FT DISULFID 42..60 FT /evidence="ECO:0000250" FT DISULFID 62..71 FT /evidence="ECO:0000250" FT DISULFID 79..158 FT /evidence="ECO:0000250" FT DISULFID 96..139 FT /evidence="ECO:0000250" FT DISULFID 128..152 FT /evidence="ECO:0000250" FT DISULFID 162..296 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 202..218 FT /evidence="ECO:0000250" FT DISULFID 210..285 FT /evidence="ECO:0000250" FT DISULFID 310..379 FT /evidence="ECO:0000250" FT DISULFID 342..358 FT /evidence="ECO:0000250" FT DISULFID 369..397 FT /evidence="ECO:0000250" SQ SEQUENCE 434 AA; 49400 MW; BD881048DD666A55 CRC64; MKLIIFLTVT LCTLVTGLDS VYIRQYYKLS HKHRPQHREC QCLNGGTCIT YRFFSQIKRC LCPEGYGGLH CEIDTNSICY SGNGEDYRGM AEDPGCLYWD HPSVIRWGDY HADLKNALQL GLGKHNYCRN PNGRSRPWCY TKRRYSIQET PCSTIEKCER TCGQRSFSKY FKIVGGSQAE VETQPWIAGI FQNIMGTDQF LCGGSLIDPC WVLTAAHCFY NPTKKQPNKS VYKVFLGKSI LNTNDEHEQV FMVDEIISHP DFTDHTGGND NDIALIRIRT ASGQCAVESN YVRTVCLPEK NLNLYDNTWC EIAGYGKQNS YDIYYAQRLM SATVNLISQD DCKNKYYDST RVTDNMVCAG DPLWETDACK GDSGGPMVCE HNGRMTLYGI VSWGDGCAKK NKPGVYTRVT RYLNWIDSNM NAVFTKSRSF REPK //