ID Q6TCI0_MOUSE Unreviewed; 466 AA.
AC Q6TCI0;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE RecName: Full=Plasminogen {ECO:0000256|ARBA:ARBA00020043};
DE EC=3.4.21.7 {ECO:0000256|ARBA:ARBA00012184};
GN Name=Plg {ECO:0000313|MGI:MGI:97620};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000313|EMBL:AAR07361.1};
RN [1] {ECO:0000313|EMBL:AAR07361.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Kunming {ECO:0000313|EMBL:AAR07361.1};
RA Qiao H., Tang B., Sun X.;
RT "Cloning of mouse angiostatin (kringle 1-4) from Kunming mouse strain.";
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plasmin dissolves the fibrin of blood clots and acts as a
CC proteolytic factor in a variety of other processes including embryonic
CC development, tissue remodeling, tumor invasion, and inflammation. In
CC ovulation, weakens the walls of the Graafian follicle. It activates the
CC urokinase-type plasminogen activator, collagenases and several
CC complement zymogens, such as C1 and C5. Cleavage of fibronectin and
CC laminin leads to cell detachment and apoptosis. Also cleaves fibrin,
CC thrombospondin and von Willebrand factor. Its role in tissue remodeling
CC and tumor invasion may be modulated by CSPG4. Binds to cells.
CC {ECO:0000256|ARBA:ARBA00025229}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: Lys-|-Xaa > Arg-|-Xaa, higher
CC selectivity than trypsin. Converts fibrin into soluble products.;
CC EC=3.4.21.7; Evidence={ECO:0000256|ARBA:ARBA00000717};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00121}.
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DR EMBL; AY424276; AAR07361.1; -; mRNA.
DR AlphaFoldDB; Q6TCI0; -.
DR PeptideAtlas; Q6TCI0; -.
DR AGR; MGI:97620; -.
DR MGI; MGI:97620; Plg.
DR ChiTaRS; Plg; mouse.
DR CDD; cd00108; KR; 4.
DR CDD; cd01099; PAN_AP_HGF; 1.
DR Gene3D; 3.50.4.10; Hepatocyte Growth Factor; 1.
DR Gene3D; 2.40.20.10; Plasminogen Kringle 4; 3.
DR InterPro; IPR000001; Kringle.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR018056; Kringle_CS.
DR InterPro; IPR038178; Kringle_sf.
DR InterPro; IPR003609; Pan_app.
DR PANTHER; PTHR24261:SF13; PLASMINOGEN; 1.
DR PANTHER; PTHR24261; PLASMINOGEN-RELATED; 1.
DR Pfam; PF00051; Kringle; 4.
DR Pfam; PF00024; PAN_1; 1.
DR PRINTS; PR00018; KRINGLE.
DR SMART; SM00130; KR; 4.
DR SMART; SM00473; PAN_AP; 1.
DR SUPFAM; SSF57414; Hairpin loop containing domain-like; 1.
DR SUPFAM; SSF57440; Kringle-like; 4.
DR PROSITE; PS00021; KRINGLE_1; 4.
DR PROSITE; PS50070; KRINGLE_2; 4.
DR PROSITE; PS50948; PAN; 1.
PE 2: Evidence at transcript level;
KW Blood coagulation {ECO:0000256|ARBA:ARBA00023084};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00121}; Fibrinolysis {ECO:0000256|ARBA:ARBA00023281};
KW Hemostasis {ECO:0000256|ARBA:ARBA00022696};
KW Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW ProRule:PRU00121}; Signal {ECO:0000256|SAM:SignalP};
KW Tissue remodeling {ECO:0000256|ARBA:ARBA00023148};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..466
FT /note="Plasminogen"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004280062"
FT DOMAIN 20..98
FT /note="Apple"
FT /evidence="ECO:0000259|PROSITE:PS50948"
FT DOMAIN 102..181
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 184..262
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 274..352
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 376..454
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DISULFID 185..262
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 206..245
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 234..257
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 275..352
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 296..335
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 324..347
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 377..454
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 398..437
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 426..449
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
SQ SEQUENCE 466 AA; 52718 MW; 3ED3298C34C39116 CRC64;
MDHKEVILLF LLLLKPGQGD SLDGYISTQG ASLFSLTKKQ LAAGGVSDCL AKCEGETDFV
CRSFQYHSKE QQCVIMAENS KTSSIIRMRD VILFEKRVYL SECKTGIGNG YRGTMSRTKS
GVACQKWGAT FPHVPNYSPS THPNEGLEEN YCRNPDNDEQ GPWCYTTDPD KRYDYCNIPE
CEEECMYCSG EKYEGKISKT MSGLDCQAWD SQSPHAHGYI PAKFPSKNLK MNYCRNPDGE
PRPWCFTTDP TKRWEYCDIP RCTTPPPPPS PTYQCLKGRG ENYRGTVSVT VSGKTCQRWS
EQTPHRHNRT PENFPCKNLE ENYCRNPDGE TAPWCYTTDS QLRWEYCEIP SCESSASPDQ
SDSSVPPEEQ TPVVQECYQS DGQSYRGTSS TTITGKKCQS WAAMFPHRHS KTPENFPDAG
LEMNYCRNPD GDKGPWCYTT DPSVRWEYCN LKRCSETGGS VVELPT
//
