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