ID PLMN_BOVIN Reviewed; 812 AA.
AC P06868; Q28162;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 08-NOV-2023, entry version 175.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX AGRICOLA=IND20546772; DOI=10.1016/0958-6946(94)00033-L;
RA Berglund L., Andersen M.D., Petersen T.E.;
RT "Cloning and characterization of the bovine plasminogen cDNA.";
RL Int. Dairy J. 5:593-603(1995).
RN [2]
RP PROTEIN SEQUENCE OF 27-812, AND GLYCOSYLATION AT ASN-315 AND SER-365.
RX PubMed=3846532; DOI=10.1111/j.1432-1033.1985.tb08921.x;
RA Schaller J., Moser P.W., Dannegger-Muller G.A.K., Rosselet S.J.,
RA Kampfer U., Rickli E.E.;
RT "Complete amino acid sequence of bovine plasminogen. Comparison with human
RT plasminogen.";
RL Eur. J. Biochem. 149:267-278(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 706-812.
RX PubMed=6148961; DOI=10.1021/bi00313a035;
RA Malinowski D.P., Sadler J.E., Davie E.W.;
RT "Characterization of a complementary deoxyribonucleic acid coding for human
RT and bovine plasminogen.";
RL Biochemistry 23:4243-4250(1984).
RN [4]
RP GLYCOSYLATION AT ASN-315 AND SER-365, AND STRUCTURE OF CARBOHYDRATES.
RX PubMed=3356193; DOI=10.1111/j.1432-1033.1988.tb13966.x;
RA Marti T., Schaller J., Rickli E.E., Schmid K., Kamerling J.P., Gerwig G.J.,
RA van Halbeek H., Vliegenthart J.F.G.;
RT "The N- and O-linked carbohydrate chains of human, bovine and porcine
RT plasminogen. Species specificity in relation to sialylation and
RT fucosylation patterns.";
RL Eur. J. Biochem. 173:57-63(1988).
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: N-linked glycan contains N-acetyllactosamine and sialic acid. O-
CC linked glycans consist of Gal-GalNAc disaccharide which is modified
CC with up to 2 sialic acid residues (microheterogeneity).
CC {ECO:0000269|PubMed:3356193, ECO:0000269|PubMed:3846532}.
CC -!- PTM: In the presence of the inhibitor, the activation involves only
CC cleavage after Arg-583, 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; X79402; CAA55939.1; -; mRNA.
DR EMBL; K02935; AAA30714.1; -; mRNA.
DR PIR; S45046; PLBO.
DR RefSeq; NP_776376.1; NM_173951.2.
DR AlphaFoldDB; P06868; -.
DR SMR; P06868; -.
DR STRING; 9913.ENSBTAP00000001674; -.
DR BindingDB; P06868; -.
DR ChEMBL; CHEMBL2957; -.
DR MEROPS; S01.233; -.
DR GlyConnect; 500; 12 N-Linked glycans (1 site), 2 O-Linked glycans (1 site).
DR GlyCosmos; P06868; 2 sites, 26 glycans.
DR PaxDb; 9913-ENSBTAP00000001674; -.
DR PeptideAtlas; P06868; -.
DR GeneID; 280897; -.
DR KEGG; bta:280897; -.
DR CTD; 5340; -.
DR eggNOG; ENOG502QVNP; Eukaryota.
DR InParanoid; P06868; -.
DR OrthoDB; 211181at2759; -.
DR SABIO-RK; P06868; -.
DR PRO; PR:P06868; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
DR GO; GO:0019904; F:protein domain specific binding; IPI:AgBase.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005102; F:signaling receptor binding; IPI:AgBase.
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; IBA:GO_Central.
DR GO; GO:0009408; P:response to heat; IDA:AgBase.
DR GO; GO:0048771; P:tissue remodeling; IEA:UniProtKB-KW.
DR CDD; cd00108; KR; 5.
DR CDD; cd01099; PAN_AP_HGF; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 3.50.4.10; Hepatocyte Growth Factor; 1.
DR Gene3D; 2.40.20.10; Plasminogen Kringle 4; 4.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
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 PANTHER; PTHR24261:SF13; PLASMINOGEN; 1.
DR PANTHER; PTHR24261; PLASMINOGEN-RELATED; 1.
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 PRINTS; PR00018; KRINGLE.
DR SMART; SM00130; KR; 5.
DR SMART; SM00473; PAN_AP; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF57414; Hairpin loop containing domain-like; 1.
DR SUPFAM; SSF57440; Kringle-like; 5.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
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 1: Evidence at protein level;
KW Blood coagulation; Cleavage on pair of basic residues;
KW Direct protein sequencing; Disulfide bond; Fibrinolysis; Glycoprotein;
KW Hemostasis; Hydrolase; Kringle; Phosphoprotein; Protease;
KW Reference proteome; Repeat; Secreted; Serine protease; Signal;
KW Tissue remodeling; Zymogen.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:3846532"
FT CHAIN 27..812
FT /note="Plasminogen"
FT /id="PRO_0000028039"
FT CHAIN 27..583
FT /note="Plasmin heavy chain A"
FT /id="PRO_0000028040"
FT PEPTIDE 27..104
FT /note="Activation peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000028041"
FT CHAIN 105..583
FT /note="Plasmin heavy chain A, short form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000028042"
FT CHAIN 584..812
FT /note="Plasmin light chain B"
FT /id="PRO_0000028043"
FT DOMAIN 29..105
FT /note="PAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 110..188
FT /note="Kringle 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 192..269
FT /note="Kringle 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 282..359
FT /note="Kringle 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 384..461
FT /note="Kringle 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 485..564
FT /note="Kringle 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 584..810
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 624
FT /note="Charge relay system"
FT ACT_SITE 667
FT /note="Charge relay system"
FT ACT_SITE 762
FT /note="Charge relay system"
FT MOD_RES 600
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00747"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:3356193,
FT ECO:0000269|PubMed:3846532"
FT /id="CAR_000014"
FT CARBOHYD 365
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:3356193,
FT ECO:0000269|PubMed:3846532"
FT /id="CAR_000015"
FT DISULFID 56..80
FT /evidence="ECO:0000250"
FT DISULFID 60..68
FT /evidence="ECO:0000250"
FT DISULFID 110..188
FT /evidence="ECO:0000250"
FT DISULFID 131..171
FT /evidence="ECO:0000250"
FT DISULFID 159..183
FT /evidence="ECO:0000250"
FT DISULFID 192..269
FT /evidence="ECO:0000250"
FT DISULFID 195..323
FT /evidence="ECO:0000250"
FT DISULFID 213..252
FT /evidence="ECO:0000250"
FT DISULFID 241..264
FT /evidence="ECO:0000250"
FT DISULFID 282..359
FT /evidence="ECO:0000250"
FT DISULFID 303..342
FT /evidence="ECO:0000250"
FT DISULFID 331..354
FT /evidence="ECO:0000250"
FT DISULFID 384..461
FT /evidence="ECO:0000250"
FT DISULFID 405..444
FT /evidence="ECO:0000250"
FT DISULFID 433..456
FT /evidence="ECO:0000250"
FT DISULFID 485..564
FT /evidence="ECO:0000250"
FT DISULFID 506..547
FT /evidence="ECO:0000250"
FT DISULFID 535..559
FT /evidence="ECO:0000250"
FT DISULFID 570..687
FT /note="Interchain (between A and B chains)"
FT /evidence="ECO:0000250"
FT DISULFID 580..588
FT /note="Interchain (between A and B chains)"
FT /evidence="ECO:0000250"
FT DISULFID 609..625
FT /evidence="ECO:0000250"
FT DISULFID 701..768
FT /evidence="ECO:0000250"
FT DISULFID 731..747
FT /evidence="ECO:0000250"
FT DISULFID 758..786
FT /evidence="ECO:0000250"
FT CONFLICT 335
FT /note="N -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 516
FT /note="Q -> H (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 555
FT /note="P -> L (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 744
FT /note="T -> R (in Ref. 3; AAA30714)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 812 AA; 91216 MW; 38A6AA691E220946 CRC64;
MLPASPKMEH KAVVFLLLLF LKSGLGDLLD DYVNTQGASL LSLSRKNLAG RSVEDCAAKC
EEETDFVCRA FQYHSKEQQC VVMAENSKNT PVFRMRDVIL YEKRIYLLEC KTGNGQTYRG
TTAETKSGVT CQKWSATSPH VPKFSPEKFP LAGLEENYCR NPDNDENGPW CYTTDPDKRY
DYCDIPECED KCMHCSGENY EGKIAKTMSG RDCQAWDSQS PHAHGYIPSK FPNKNLKMNY
CRNPDGEPRP WCFTTDPQKR WEFCDIPRCT TPPPSSGPKY QCLKGTGKNY GGTVAVTESG
HTCQRWSEQT PHKHNRTPEN FPCKNLEENY CRNPNGEKAP WCYTTNSEVR WEYCTIPSCE
SSPLSTERMD VPVPPEQTPV PQDCYHGNGQ SYRGTSSTTI TGRKCQSWSS MTPHRHLKTP
ENYPNAGLTM NYCRNPDADK SPWCYTTDPR VRWEFCNLKK CSETPEQVPA APQAPGVENP
PEADCMIGTG KSYRGKKATT VAGVPCQEWA AQEPHQHSIF TPETNPQSGL ERNYCRNPDG
DVNGPWCYTM NPRKPFDYCD VPQCESSFDC GKPKVEPKKC SGRIVGGCVS KPHSWPWQVS
LRRSSRHFCG GTLISPKWVL TAAHCLDNIL ALSFYKVILG AHNEKVREQS VQEIPVSRLF
REPSQADIAL LKLSRPAIIT KEVIPACLPP PNYMVAARTE CYITGWGETQ GTFGEGLLKE
AHLPVIENKV CNRNEYLDGR VKPTELCAGH LIGGTDSCQG DSGGPLVCFE KDKYILQGVT
SWGLGCARPN KPGVYVRVSP YVPWIEETMR RN
//
