PLMN_NOTEU
ID PLMN_NOTEU Reviewed; 806 AA.
AC O18783;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Plasminogen;
DE EC=3.4.21.7;
DE Contains:
DE RecName: Full=Plasmin heavy chain A;
DE Contains:
DE RecName: Full=Activation peptide;
DE Contains:
DE RecName: Full=Plasmin heavy chain A, short form;
DE Contains:
DE RecName: Full=Plasmin light chain B;
DE Flags: Precursor;
GN Name=PLG;
OS Notamacropus eugenii (Tammar wallaby) (Macropus eugenii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Diprotodontia; Macropodidae; Notamacropus.
OX NCBI_TaxID=9315;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=9342350; DOI=10.1073/pnas.94.22.11992;
RA Lawn R.M., Schwartz K., Patthy L.;
RT "Convergent evolution of apolipoprotein(a) in primates and hedgehog.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:11992-11997(1997).
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 (By
CC similarity). {ECO:0000250}.
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;
CC -!- ACTIVITY REGULATION: Converted into plasmin by plasminogen activators,
CC both plasminogen and its activator being bound to fibrin. Activated
CC with catalytic amounts of streptokinase (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CSPG4 and AMOT. Interacts (via the Kringle
CC domains) with HRG; the interaction tethers PLG to the cell surface and
CC enhances its activation. Interacts (via Kringle 4 domain) with ADA; the
CC interaction stimulates PLG activation when in complex with DPP4.
CC Angiostatin: Interacts with ATP5F1A; the interaction inhibits most of
CC the angiogenic effects of angiostatin. {ECO:0000250|UniProtKB:P00747}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Locates to the cell
CC surface where it is proteolytically cleaved to produce the active
CC plasmin. Interaction with HRG tethers it to the cell surface (By
CC similarity). {ECO:0000250}.
CC -!- DOMAIN: Kringle domains mediate interaction with CSPG4. {ECO:0000250}.
CC -!- PTM: In the presence of the inhibitor, the activation involves only
CC cleavage after Arg-576, yielding two chains held together by two
CC disulfide bonds. In the absence of the inhibitor, the activation
CC involves additionally the removal of the activation peptide (By
CC similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: Plasmin is inactivated by alpha-2-antiplasmin
CC immediately after dissociation from the clot. {ECO:0000250}.
CC -!- MISCELLANEOUS: In the presence of the inhibitor, the activation
CC involves only cleavage after Arg-576, resulting in 2 chains held
CC together by 2 disulfide bonds. Without the inhibitor, the activation
CC involves also removal of the activation peptide (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Plasminogen subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; AF012297; AAB65760.1; -; mRNA.
DR AlphaFoldDB; O18783; -.
DR SMR; O18783; -.
DR MEROPS; S01.233; -.
DR PRIDE; O18783; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR GO; GO:0042730; P:fibrinolysis; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0048771; P:tissue remodeling; IEA:UniProtKB-KW.
DR CDD; cd00108; KR; 5.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 1.
DR Gene3D; 2.40.20.10; -; 5.
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 InterPro; IPR023317; Pept_S1A_plasmin.
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 Pfam; PF00051; Kringle; 5.
DR Pfam; PF00024; PAN_1; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF001150; Plasmin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00130; KR; 5.
DR SMART; SM00473; PAN_AP; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF57440; SSF57440; 5.
DR PROSITE; PS00021; KRINGLE_1; 5.
DR PROSITE; PS50070; KRINGLE_2; 5.
DR PROSITE; PS50948; PAN; 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 Blood coagulation; Disulfide bond; Fibrinolysis; Hemostasis; Hydrolase;
KW Kringle; Phosphoprotein; Protease; Repeat; Secreted; Serine protease;
KW Signal; Tissue remodeling; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..806
FT /note="Plasminogen"
FT /id="PRO_0000028064"
FT CHAIN 20..576
FT /note="Plasmin heavy chain A"
FT /evidence="ECO:0000250"
FT /id="PRO_0000028065"
FT PEPTIDE 20..96
FT /note="Activation peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000028066"
FT CHAIN 97..576
FT /note="Plasmin heavy chain A, short form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000028067"
FT CHAIN 577..806
FT /note="Plasmin light chain B"
FT /evidence="ECO:0000250"
FT /id="PRO_0000028068"
FT DOMAIN 20..98
FT /note="PAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 102..181
FT /note="Kringle 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 184..262
FT /note="Kringle 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 274..352
FT /note="Kringle 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 370..448
FT /note="Kringle 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 475..555
FT /note="Kringle 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 577..804
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 618
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 661
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 756
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT MOD_RES 593
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00747"
FT MOD_RES 684
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00747"
FT DISULFID 49..73
FT /evidence="ECO:0000250"
FT DISULFID 53..61
FT /evidence="ECO:0000250"
FT DISULFID 103..181
FT /evidence="ECO:0000250"
FT DISULFID 124..164
FT /evidence="ECO:0000250"
FT DISULFID 152..176
FT /evidence="ECO:0000250"
FT DISULFID 185..262
FT /evidence="ECO:0000250"
FT DISULFID 188..316
FT /evidence="ECO:0000250"
FT DISULFID 206..245
FT /evidence="ECO:0000250"
FT DISULFID 234..257
FT /evidence="ECO:0000250"
FT DISULFID 275..352
FT /evidence="ECO:0000250"
FT DISULFID 296..335
FT /evidence="ECO:0000250"
FT DISULFID 324..347
FT /evidence="ECO:0000250"
FT DISULFID 371..448
FT /evidence="ECO:0000250"
FT DISULFID 392..431
FT /evidence="ECO:0000250"
FT DISULFID 420..443
FT /evidence="ECO:0000250"
FT DISULFID 476..555
FT /evidence="ECO:0000250"
FT DISULFID 497..538
FT /evidence="ECO:0000250"
FT DISULFID 526..550
FT /evidence="ECO:0000250"
FT DISULFID 563..681
FT /note="Interchain (between A and B chains)"
FT /evidence="ECO:0000250"
FT DISULFID 573..581
FT /note="Interchain (between A and B chains)"
FT /evidence="ECO:0000250"
FT DISULFID 603..619
FT /evidence="ECO:0000250"
FT DISULFID 695..762
FT /evidence="ECO:0000250"
FT DISULFID 725..741
FT /evidence="ECO:0000250"
FT DISULFID 752..780
FT /evidence="ECO:0000250"
SQ SEQUENCE 806 AA; 90981 MW; 95FAA86DC20064D5 CRC64;
MEYGKVIFLF LLFLKSGQGE SLENYIKTEG ASLSNSQKKQ FVASSTEECE ALCEKETEFV
CRSFEHYNKE QKCVIMSENS KTSSVERKRD VVLFEKRIYL SDCKSGNGRN YRGTLSKTKS
GITCQKWSDL SPHVPNYAPS KYPDAGLEKN YCRNPDDDVK GPWCYTTNPD IRYEYCDVPE
CEDECMHCSG ENYRGTISKT ESGIECQPWD SQEPHSHEYI PSKFPSKDLK ENYCRNPDGE
PRPWCFTSNP EKRWEFCNIP RCSSPPPPPG PMLQCLKGRG ENYRGKIAVT KSGHTCQRWN
KQTPHKHNRT PENFPCRGLD ENYCRNPDGE LEPWCYTTNP DVRQEYCAIP SCGTSSPHTD
RVEQSPVIQE CYEGKGENYR GTTSTTISGK KCQAWSSMTP HQHKKTPDNF PNADLIRNYC
RNPDGDKSPW CYTMDPTVRW EFCNLEKCSG TGSTVLNAQT TRVPSVDTTS HPESDCMYGS
GKDYRGKRST TVTGTLCQAW TAQEPHRHTI FTPDTYPRAG LEENYCRNPD GDPNGPWCYT
TNPKKLFDYC DIPQCVSPSS FDCGKPRVEP QKCPGRIVGG CYAQPHSWPW QISLRTRFGE
HFCGGTLIAP QWVLTAAHCL ERSQWPGAYK VILGLHREVN PESYSQEIGV SRLFKGPLAA
DIALLKLNRP AAINDKVIPA CLPSQDFMVP DRTLCHVTGW GDTQGTSPRG LLKQASLPVI
DNRVCNRHEY LNGRVKSTEL CAGHLVGRGD SCQGDSGGPL ICFEDDKYVL QGVTSWGLGC
ARPNKPGVYV RVSRYISWIE DVMKNN
