PLMN_PIG
ID PLMN_PIG Reviewed; 809 AA.
AC P06867; Q19AZ9;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 3.
DT 25-MAY-2022, entry version 162.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Chen Y., Tan W., Cheng J.;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 20-579.
RA Schaller J., Marti T., Roesselet S.J., Kaempfer U., Rickli E.E.;
RT "Amino acid sequence of the heavy chain of porcine plasmin. Comparison of
RT the carbohydrate attachment sites with the human and bovine species.";
RL Fibrinolysis 1:91-102(1987).
RN [3]
RP PROTEIN SEQUENCE OF 469-809.
RX PubMed=3846533; DOI=10.1111/j.1432-1033.1985.tb08923.x;
RA Marti T., Schaller J., Rickli E.E.;
RT "Determination of the complete amino-acid sequence of porcine
RT miniplasminogen.";
RL Eur. J. Biochem. 149:279-285(1985).
RN [4]
RP GLYCOSYLATION AT ASN-308 AND THR-268, 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, sialic acid and is
CC core fucosylated. O-linked glycans consist of Gal-GalNAc disaccharide
CC which is modified with up to 2 sialic acid residues
CC (microheterogeneity). {ECO:0000269|PubMed:3356193}.
CC -!- PTM: In the presence of the inhibitor, the activation involves only
CC cleavage after Arg-579, 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; DQ530369; ABF82358.1; -; mRNA.
DR PIR; S03733; PLPG.
DR RefSeq; NP_001038055.1; NM_001044590.2.
DR AlphaFoldDB; P06867; -.
DR SMR; P06867; -.
DR IntAct; P06867; 1.
DR STRING; 9823.ENSSSCP00000004364; -.
DR MEROPS; S01.233; -.
DR GlyConnect; 501; 12 N-Linked glycans (1 site), 2 O-Linked glycans (1 site).
DR PaxDb; P06867; -.
DR PeptideAtlas; P06867; -.
DR PRIDE; P06867; -.
DR GeneID; 733660; -.
DR KEGG; ssc:733660; -.
DR CTD; 5340; -.
DR eggNOG; ENOG502QVNP; Eukaryota.
DR InParanoid; P06867; -.
DR OrthoDB; 164039at2759; -.
DR SABIO-RK; P06867; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; IBA:GO_Central.
DR GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
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: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; 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; 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..19
FT /evidence="ECO:0000269|Ref.2"
FT CHAIN 20..809
FT /note="Plasminogen"
FT /id="PRO_0000285882"
FT CHAIN 20..579
FT /note="Plasmin heavy chain A"
FT /id="PRO_0000028075"
FT PEPTIDE 20..97
FT /note="Activation peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000028076"
FT CHAIN 98..579
FT /note="Plasmin heavy chain A, short form"
FT /id="PRO_0000028077"
FT CHAIN 580..809
FT /note="Plasmin light chain B"
FT /id="PRO_0000028078"
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 377..454
FT /note="Kringle 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 480..559
FT /note="Kringle 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 580..807
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 621
FT /note="Charge relay system"
FT ACT_SITE 664
FT /note="Charge relay system"
FT ACT_SITE 759
FT /note="Charge relay system"
FT MOD_RES 596
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00747"
FT CARBOHYD 268
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:3356193"
FT /id="CAR_000020"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:3356193"
FT /id="CAR_000019"
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 377..454
FT /evidence="ECO:0000250"
FT DISULFID 398..437
FT /evidence="ECO:0000250"
FT DISULFID 426..449
FT /evidence="ECO:0000250"
FT DISULFID 480..559
FT /evidence="ECO:0000250"
FT DISULFID 501..542
FT /evidence="ECO:0000250"
FT DISULFID 530..554
FT /evidence="ECO:0000250"
FT DISULFID 566..684
FT /note="Interchain (between A and B chains)"
FT /evidence="ECO:0000250"
FT DISULFID 576..584
FT /note="Interchain (between A and B chains)"
FT /evidence="ECO:0000250"
FT DISULFID 606..622
FT /evidence="ECO:0000250"
FT DISULFID 698..765
FT /evidence="ECO:0000250"
FT DISULFID 728..744
FT /evidence="ECO:0000250"
FT DISULFID 755..783
FT /evidence="ECO:0000250"
FT CONFLICT 361
FT /note="Y -> H (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 599
FT /note="H -> Y (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 602
FT /note="G -> R (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 675
FT /note="I -> V (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 809 AA; 90615 MW; 198261D2082A075D CRC64;
MDHKEVVLLL LLFLKSGLGD SLDDYVNTQG AFLFSLSRKQ VAARSVEECA AKCEAETNFI
CRAFQYHSKD QQCVVMAENS KTSPIARMRD VVLFEKRIYL SECKTGNGKN YRGTTSKTKS
GVICQKWSVS SPHIPKYSPE KFPLAGLEEN YCRNPDNDEK GPWCYTTDPE TRFDYCDIPE
CEDECMHCSG EHYEGKISKT MSGIECQSWG SQSPHAHGYL PSKFPNKNLK MNYCRNPDGE
PRPWCFTTDP NKRWEFCDIP RCTTPPPTSG PTYQCLKGRG ENYRGTVSVT ASGHTCQRWS
AQSPHKHNRT PENFPCKNLE ENYCRNPDGE TAPWCYTTDS EVRWDYCKIP SCGSSTTSTE
YLDAPVPPEQ TPVAQDCYRG NGESYRGTSS TTITGRKCQS WVSMTPHRHE KTPGNFPNAG
LTMNYCRNPD ADKSPWCYTT DPRVRWEYCN LKKCSETEQQ VTNFPAIAQV PSVEDLSEDC
MFGNGKRYRG KRATTVAGVP CQEWAAQEPH RHSIFTPETN PRAGLEKNYC RNPDGDDNGP
WCYTTNPQKL FDYCDVPQCV TSSFDCGKPK VEPKKCPARV VGGCVSIPHS WPWQISLRHR
YGGHFCGGTL ISPEWVLTAK HCLEKSSSPS SYKVILGAHE EYHLGEGVQE IDVSKLFKEP
SEADIALLKL SSPAIITDKV IPACLPTPNY VVADRTACYI TGWGETKGTY GAGLLKEARL
PVIENKVCNR YEYLGGKVSP NELCAGHLAG GIDSCQGDSG GPLVCFEKDK YILQGVTSWG
LGCALPNKPG VYVRVSRFVT WIEEIMRRN
