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UROK_CHICK
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   03-AUG-2022, entry version 160.
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}.
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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.ENSGALP00000042397; -.
DR   MEROPS; S01.231; -.
DR   PaxDb; P15120; -.
DR   GeneID; 396424; -.
DR   KEGG; gga:396424; -.
DR   CTD; 5328; -.
DR   VEuPathDB; HostDB:geneid_396424; -.
DR   eggNOG; ENOG502QRMI; Eukaryota.
DR   InParanoid; P15120; -.
DR   OrthoDB; 1314811at2759; -.
DR   PhylomeDB; P15120; -.
DR   PRO; PR:P15120; -.
DR   Proteomes; UP000000539; 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:0031639; P:plasminogen activation; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   GO; GO:0033628; P:regulation of cell adhesion mediated by integrin; IBA:GO_Central.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; -; 1.
DR   Gene3D; 2.40.20.10; -; 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   InterPro; IPR034814; Urokinase.
DR   PANTHER; PTHR24264:SF38; PTHR24264:SF38; 1.
DR   Pfam; PF00051; Kringle; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00130; KR; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   SUPFAM; SSF57440; SSF57440; 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
 
 
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