PLMN_ERIEU
ID PLMN_ERIEU Reviewed; 810 AA.
AC Q29485;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 120.
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 Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=7592597; DOI=10.1074/jbc.270.41.24004;
RA Lawn R.M., Boonmark N.W., Schwartz K., Lindahl G.E., Wade D.P., Byrne C.D.,
RA Fong K.J., Meer K., Patthy L.;
RT "The recurring evolution of lipoprotein(a). Insights from cloning of
RT hedgehog apolipoprotein(a).";
RL J. Biol. Chem. 270:24004-24009(1995).
RN [2]
RP SEQUENCE REVISION.
RA Lawn R.M.;
RL Submitted (FEB-1997) 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 (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. Cannot be
CC activated with streptokinase.
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-582, 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.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Plasminogen subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; U33171; AAC48717.1; -; mRNA.
DR PIR; I46260; I46260.
DR AlphaFoldDB; Q29485; -.
DR SMR; Q29485; -.
DR STRING; 9365.XP_007521666.1; -.
DR MEROPS; S01.233; -.
DR PRIDE; Q29485; -.
DR eggNOG; ENOG502QVNP; Eukaryota.
DR Proteomes; UP000079721; Unplaced.
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; -; 4.
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; Cleavage on pair of basic residues; Disulfide bond;
KW Fibrinolysis; Glycoprotein; Hemostasis; Hydrolase; Kringle; Phosphoprotein;
KW Protease; Reference proteome; Repeat; Secreted; Serine protease; Signal;
KW Tissue remodeling; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT CHAIN 20..810
FT /note="Plasminogen"
FT /id="PRO_0000028046"
FT CHAIN 20..582
FT /note="Plasmin heavy chain A"
FT /evidence="ECO:0000250"
FT /id="PRO_0000028047"
FT PEPTIDE 20..97
FT /note="Activation peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000028048"
FT CHAIN 98..582
FT /note="Plasmin heavy chain A, short form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000028049"
FT CHAIN 583..810
FT /note="Plasmin light chain B"
FT /evidence="ECO:0000250"
FT /id="PRO_0000028050"
FT DOMAIN 20..98
FT /note="PAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 103..181
FT /note="Kringle 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 185..262
FT /note="Kringle 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 275..352
FT /note="Kringle 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 379..456
FT /note="Kringle 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 482..561
FT /note="Kringle 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 582..808
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 398..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 622
FT /note="Charge relay system"
FT ACT_SITE 665
FT /note="Charge relay system"
FT ACT_SITE 760
FT /note="Charge relay system"
FT MOD_RES 598
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00747"
FT CARBOHYD 339
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 379..456
FT /evidence="ECO:0000250"
FT DISULFID 400..439
FT /evidence="ECO:0000250"
FT DISULFID 428..451
FT /evidence="ECO:0000250"
FT DISULFID 482..561
FT /evidence="ECO:0000250"
FT DISULFID 503..544
FT /evidence="ECO:0000250"
FT DISULFID 532..556
FT /evidence="ECO:0000250"
FT DISULFID 569..685
FT /note="Interchain (between A and B chains)"
FT /evidence="ECO:0000250"
FT DISULFID 579..586
FT /note="Interchain (between A and B chains)"
FT /evidence="ECO:0000250"
FT DISULFID 607..623
FT /evidence="ECO:0000250"
FT DISULFID 699..766
FT /evidence="ECO:0000250"
FT DISULFID 729..745
FT /evidence="ECO:0000250"
FT DISULFID 756..784
FT /evidence="ECO:0000250"
SQ SEQUENCE 810 AA; 90902 MW; 8E75780946017A16 CRC64;
MQRKELVLLF LLFLQPGHGI PLDDYVTTQG ASLCSSTKKQ LSVGSTEECA VKCEKETSFI
CRSFQYHSKE QQCVIMAENS KSTPVLRMRD VILFEKKMYL SECKVGNGKY YRGTVSKTKT
GLTCQKWSAE TPHKPRFSPD ENPSEGLDQN YCRNPDNDPK GPWCYTMDPE VRYEYCEIIQ
CEDECMHCSG QNYVGKISRT MSGLECQPWD SQIPHPHGFI PSKFPSKNLK MNYCRNPDGE
PRPWCFTMDR NKRWEYCDIP RCTTPPPPSG PTYQCLMGNG EHYQGNVAVT VSGLTCQRWG
EQSPHRHDRT PENYPCKNLD ENYCRNPDGE PAPWCFTTNS SVRWEFCKIP DCVSSASETE
HSDAPVIVPP EQTPVVQECY QGNGQTYRGT SSTTITGKKC QPWTSMRPHR HSKTPENYPD
ADLTMNYCRN PDGDKGPWCY TTDPSVRWEF CNLKKCSGTE MSATNSSPVQ VSSASESSEQ
DCIIDNGKGY RGTKATTGAG TPCQAWAAQE PHRHSIFTPE TNPRADLQEN YCRNPDGDAN
GPWCYTTNPR KLFDYCDIPH CVSPSSADCG KPKVEPKKCP GRVGGCVAHP HSWPWQVSLR
RFGQHFCGGT LISPEWVVTA AHCLEKFSNP AIYKVVLGAH QETRLERDVQ IKGVTKMFLE
PYRADIALLK LSSPAIITDK DHPACLPNSN YMVADRSLCY ITGWGETKGT YGAGLLKEAQ
LPVIENKVCN RQSFLNGRVR STELCAGHLA GGVDSCQGDS GGPLVCFEKD RYILQGVTSW
GLGCARLTRP GVYVRVSRYV SWLQDVMRNN
