PLG
entrez
5340
canonical
uniprot
P00747
canonical
ensembl
ENSG00000122194
resolver
ensp
ENSP00000308938
resolver
ensp
ENSP00000355891
resolver
enst
ENST00000308192
resolver
enst
ENST00000366924
resolver
genesymbol
PLG
resolver
hgnc
HGNC:9071
resolver
uniprot
Q15146
resolver
uniprot
Q5TEH4
resolver
uniprot
Q5TEH5
resolver
uniprot
Q6PA00
resolver
uniprot_entry
PLMN_HUMAN
resolver
uniprot_entry
Q5TEH5_HUMAN
resolver
uniprot_sec
Q15146
resolver
uniprot_sec
Q5TEH4
resolver
uniprot_sec
Q6PA00
resolver
activity_regulation
ACTIVITY REGULATION: [Plasmin]: Converted into plasmin by tissue-type (PLAT) and urokinase-type (PLAU) plasminogen activator (PubMed:14699093). The activation by PLAT is enhanced by fibrin at the surface of blood clots (PubMed:6094526). The partial proteolysis of fibrin by plasmin mainly exposes C-terminal lysine residues which in turn help recruit and activate plasminogen (PubMed:6094526, PubMed:6919539). The activation by PLAU occurs at the surface of cells and is more specific of extracellular matrix remodeling (PubMed:28849762). Activated by streptokinase (PubMed:12456874). Plasmin activity is also inhibited by SERPINF2; plasmin is inactivated by alpha-2-antiplasmin immediately after dissociation from the clot (PubMed:14699093). {ECO:0000269|PubMed:12456874, ECO:0000269|PubMed:14699093, ECO:0000269|PubMed:28849762, ECO:0000269|PubMed:6094526, ECO:0000269|PubMed:6919539}.
uniprot
proteins
amino_acid_sequence
MEHKEVVLLLLLFLKSGQGEPLDDYVNTQGASLFSVTKKQLGAGSIEECAAKCEEDEEFTCRAFQYHSKEQQCVIMAENRKSSIIIRMRDVVLFEKKVYLSECKTGNGKNYRGTMSKTKNGITCQKWSSTSPHRPRFSPATHPSEGLEENYCRNPDNDPQGPWCYTTDPEKRYDYCDILECEEECMHCSGENYDGKISKTMSGLECQAWDSQSPHAHGYIPSKFPNKNLKKNYCRNPDRELRPWCFTTDPNKRWELCDIPRCTTPPPSSGPTYQCLKGTGENYRGNVAVTVSGHTCQHWSAQTPHTHNRTPENFPCKNLDENYCRNPDGKRAPWCHTTNSQVRWEYCKIPSCDSSPVSTEQLAPTAPPELTPVVQDCYHGDGQSYRGTSSTTTTGKKCQSWSSMTPHRHQKTPENYPNAGLTMNYCRNPDADKGPWCFTTDPSVRWEYCNLKKCSGTEASVVAPPPVVLLPDVETPSEEDCMFGNGKGYRGKRATTVTGTPCQDWAAQEPHRHSIFTPETNPRAGLEKNYCRNPDGDVGGPWCYTTNPRKLYDYCDVPQCAAPSFDCGKPQVEPKKCPGRVVGGCVAHPHSWPWQVSLRTRFGMHFCGGTLISPEWVLTAAHCLEKSPRPSSYKVILGAHQEVNLEPHVQEIEVSRLFLEPTRKDIALLKLSSPAVITDKVIPACLPSPNYVVADRTECFITGWGETQGTFGAGLLKEAQLPVIENKVCNRYEFLNGRVQSTELCAGHLAGGTDSCQGDSGGPLVCFEKDKYILQGVTSWGLGCARPNKPGVYVRVSRFVTWIEGVMRNN
uniprot
proteins
disease_involvement
DISEASE: Plasminogen deficiency (PLGD) [MIM:217090]: A disorder characterized by decreased serum plasminogen activity. Two forms of the disorder are distinguished: type 1 deficiency is additionally characterized by decreased plasminogen antigen levels and clinical symptoms, whereas type 2 deficiency, also known as dysplasminogenemia, is characterized by normal, or slightly reduced antigen levels, and absence of clinical manifestations. Plasminogen deficiency type 1 results in markedly impaired extracellular fibrinolysis and chronic mucosal pseudomembranous lesions due to subepithelial fibrin deposition and inflammation. The most common clinical manifestation of type 1 deficiency is ligneous conjunctivitis in which pseudomembranes formation on the palpebral surfaces of the eye progresses to white, yellow-white, or red thick masses with a wood-like consistency that replace the normal mucosa. {ECO:0000269|PubMed:10233898, ECO:0000269|PubMed:1427790, ECO:0000269|PubMed:1986355, ECO:0000269|PubMed:6216475, ECO:0000269|PubMed:6238949, ECO:0000269|PubMed:8392398, ECO:0000269|PubMed:9242524, ECO:0000269|PubMed:9858247}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Angioedema, hereditary, 4 (HAE4) [MIM:619360]: A form of angioedema, a disorder characterized by episodic local swelling involving subcutaneous or submucous tissue of the upper respiratory and gastrointestinal tracts, face, extremities, and genitalia. HAE4 is an autosomal dominant form with incomplete penetrance, variable expressivity, and female predominance. {ECO:0000269|PubMed:28795768, ECO:0000269|PubMed:29548426, ECO:0000269|PubMed:29952006, ECO:0000269|PubMed:29987869, ECO:0000269|PubMed:33114181, ECO:0000269|PubMed:33799813}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.4.21.7
uniprot
proteins
function
FUNCTION: [Plasmin]: Protease which primary function is to degrade fibrin, the main component of blood clots (PubMed:6094526, PubMed:6919539). Also cleaves other components of blood clots like thrombospondin-1/THBS1 and von Willebrand factor (VWF) (PubMed:24449821, PubMed:7679575). Can also directly and/or through the activation of other proteases degrade the various components of the extracellular matrix including collagen, fibronectin and laminin (PubMed:14699093, PubMed:28849762, PubMed:9171346). Thereby, regulates a variety of biological processes including embryonic development, tissue remodeling, and inflammation (PubMed:9171346). In ovulation, weakens the walls of the Graafian follicle (By similarity). In vitro, it is also able to cleave several complement zymogens, such as C1, C4 and C5 (PubMed:6447255). {ECO:0000250|UniProtKB:Q01177, ECO:0000269|PubMed:14699093, ECO:0000269|PubMed:24449821, ECO:0000269|PubMed:28849762, ECO:0000269|PubMed:6094526, ECO:0000269|PubMed:6447255, ECO:0000269|PubMed:6919539, ECO:0000269|PubMed:7679575, ECO:0000269|PubMed:9171346}.; FUNCTION: [Angiostatin]: Has an antiangiogenic activity and inhibits neovascularization (PubMed:10077593, PubMed:7525077, PubMed:9102221). Could act through the inhibition of the ATP synthase subunit ATP5F1A (PubMed:10077593). {ECO:0000269|PubMed:10077593, ECO:0000269|PubMed:7525077, ECO:0000269|PubMed:9102221}.; FUNCTION: (Microbial infection) Binds to OspC on the surface of B.burgdorferi cells, possibly conferring an extracellular protease activity on the bacteria that allows it to traverse host tissue. {ECO:0000269|PubMed:22433849}.; FUNCTION: (Microbial infection) Interacts with dengue virus type 2 particles (PubMed:31726374). Enhances dengue virus type 2 infection in Aedes aegypti mosquito midgut by increasing midgut internalization, resulting in higher infection rates and viral dissemination in mosquitoes (PubMed:31726374). {ECO:0000269|PubMed:31726374}.
uniprot
proteins
mass_dalton
90569
uniprot
proteins
mutagenesis
MUTAGEN 741; /note="S->A: Loss of serine-type endopeptidase activity. Proteolytically cleaved, but loss of cell detachment."; /evidence="ECO:0000269|PubMed:14699093, ECO:0000269|PubMed:21949403
uniprot
proteins
post_translational_modification
PTM: N-linked glycan contains N-acetyllactosamine and sialic acid. O-linked glycans consist of Gal-GalNAc disaccharide modified with up to 2 sialic acid residues (microheterogeneity). {ECO:0000269|PubMed:18780401, ECO:0000269|PubMed:3356193, ECO:0000269|PubMed:9054441}.; PTM: [Plasmin]: Activation requires cleavage in two chains held together by two disulfide bonds. Removal of the activation peptide is also part of the activation mechanisms. {ECO:0000269|PubMed:4270330}.; PTM: (Microbial infection) The Y.pestis Pla protein cleaves between Arg-580 and Val-581, generating plasmin which facilitates bacterial migration and infection (PubMed:22645135). {ECO:0000269|PubMed:22645135}.
uniprot
proteins
protein_family
Peptidase S1 family
uniprot
proteins
protein_family
Plasminogen subfamily
uniprot
proteins
pubmed
10077593
uniprot
proteins
pubmed
10233898
uniprot
proteins
pubmed
10656799
uniprot
proteins
pubmed
10889192
uniprot
proteins
pubmed
11350170
uniprot
proteins
pubmed
12054798
uniprot
proteins
pubmed
122932
uniprot
proteins
pubmed
12456874
uniprot
proteins
pubmed
126863
uniprot
proteins
pubmed
142009
uniprot
proteins
pubmed
1427790
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
14699093
uniprot
proteins
pubmed
15016824
uniprot
proteins
pubmed
15211511
uniprot
proteins
pubmed
15299951
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15613921
uniprot
proteins
pubmed
16043488
uniprot
proteins
pubmed
1657148
uniprot
proteins
pubmed
1657149
uniprot
proteins
pubmed
18780401
uniprot
proteins
pubmed
19712047
uniprot
proteins
pubmed
1986355
uniprot
proteins
pubmed
2143188
uniprot
proteins
pubmed
2157850
uniprot
proteins
pubmed
21949403
uniprot
proteins
pubmed
22433849
uniprot
proteins
pubmed
22540246
uniprot
proteins
pubmed
22645135
uniprot
proteins
pubmed
2318848
uniprot
proteins
pubmed
23204165
uniprot
proteins
pubmed
23335990
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24449821
uniprot
proteins
pubmed
27387503
uniprot
proteins
pubmed
28795768
uniprot
proteins
pubmed
28849762
uniprot
proteins
pubmed
29548426
uniprot
proteins
pubmed
29952006
uniprot
proteins
pubmed
29987869
uniprot
proteins
pubmed
3030813
uniprot
proteins
pubmed
31726374
uniprot
proteins
pubmed
33114181
uniprot
proteins
pubmed
3356193
uniprot
proteins
pubmed
33799813
uniprot
proteins
pubmed
34502392
uniprot
proteins
pubmed
34800067
uniprot
proteins
pubmed
36756125
uniprot
proteins
pubmed
4240117
uniprot
proteins
pubmed
4270330
uniprot
proteins
pubmed
4694729
uniprot
proteins
pubmed
6094526
uniprot
proteins
pubmed
6148961
uniprot
proteins
pubmed
6216475
uniprot
proteins
pubmed
6238949
uniprot
proteins
pubmed
6447255
uniprot
proteins
pubmed
6919539
uniprot
proteins
pubmed
7525077
uniprot
proteins
pubmed
7679575
uniprot
proteins
pubmed
7706303
uniprot
proteins
pubmed
8054447
uniprot
proteins
pubmed
8181475
uniprot
proteins
pubmed
8181476
uniprot
proteins
pubmed
8392398
uniprot
proteins
pubmed
8611560
uniprot
proteins
pubmed
8652577
uniprot
proteins
pubmed
9054441
uniprot
proteins
pubmed
9102221
uniprot
proteins
pubmed
9102401
uniprot
proteins
pubmed
9171346
uniprot
proteins
pubmed
9201958
uniprot
proteins
pubmed
9242524
uniprot
proteins
pubmed
9305949
uniprot
proteins
pubmed
9521645
uniprot
proteins
pubmed
9548733
uniprot
proteins
pubmed
9783753
uniprot
proteins
pubmed
9858247
uniprot
proteins
sequence_length
810
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Plasmin]: Secreted {ECO:0000269|PubMed:10077593, ECO:0000269|PubMed:14699093}. Note=Locates to the cell surface where it is proteolytically cleaved to produce the active plasmin (PubMed:14699093). Interaction with HRG tethers it to the cell surface (PubMed:15613921, PubMed:19712047, PubMed:9102401). {ECO:0000269|PubMed:14699093, ECO:0000269|PubMed:15613921, ECO:0000269|PubMed:19712047, ECO:0000269|PubMed:9102401}.; SUBCELLULAR LOCATION: [Angiostatin]: Secreted {ECO:0000305|PubMed:7525077, ECO:0000305|PubMed:9548733}.
uniprot
proteins