Overview
| Uniprot ID | P00747 |
| Protein Name | Plasminogen |
| Gene Name | PLG |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 39 |
SLFSVTKKQLGAGSI |
Function
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)
Protein Sequence
10
MEHKEVVLLL
20
LLFLKSGQGE
30
PLDDYVNTQG
40
ASLFSVTKKQ
50
LGAGSIEECA
60
AKCEEDEEFT
70
CRAFQYHSKE
80
QQCVIMAENR
90
KSSIIIRMRD
100
VVLFEKKVYL
110
SECKTGNGKN
120
YRGTMSKTKN
130
GITCQKWSST
140
SPHRPRFSPA
150
THPSEGLEEN
160
YCRNPDNDPQ
170
GPWCYTTDPE
180
KRYDYCDILE
190
CEEECMHCSG
200
ENYDGKISKT
210
MSGLECQAWD
220
SQSPHAHGYI
230
PSKFPNKNLK
240
KNYCRNPDRE
250
LRPWCFTTDP
260
NKRWELCDIP
270
RCTTPPPSSG
280
PTYQCLKGTG
290
ENYRGNVAVT
300
VSGHTCQHWS
310
AQTPHTHNRT
320
PENFPCKNLD
330
ENYCRNPDGK
340
RAPWCHTTNS
350
QVRWEYCKIP
360
SCDSSPVSTE
370
QLAPTAPPEL
380
TPVVQDCYHG
390
DGQSYRGTSS
400
TTTTGKKCQS
410
WSSMTPHRHQ
420
KTPENYPNAG
430
LTMNYCRNPD
440
ADKGPWCFTT
450
DPSVRWEYCN
460
LKKCSGTEAS
470
VVAPPPVVLL
480
PDVETPSEED
490
CMFGNGKGYR
500
GKRATTVTGT
510
PCQDWAAQEP
520
HRHSIFTPET
530
NPRAGLEKNY
540
CRNPDGDVGG
550
PWCYTTNPRK
560
LYDYCDVPQC
570
AAPSFDCGKP
580
QVEPKKCPGR
590
VVGGCVAHPH
600
SWPWQVSLRT
610
RFGMHFCGGT
620
LISPEWVLTA
630
AHCLEKSPRP
640
SSYKVILGAH
650
QEVNLEPHVQ
660
EIEVSRLFLE
670
PTRKDIALLK
680
LSSPAVITDK
690
VIPACLPSPN
700
YVVADRTECF
710
ITGWGETQGT
720
FGAGLLKEAQ
730
LPVIENKVCN
740
RYEFLNGRVQ
750
STELCAGHLA
760
GGTDSCQGDS
770
GGPLVCFEKD
780
KYILQGVTSW
790
GLGCARPNKP
800
GVYVRVSRFV
810
TWIEGVMRNN
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0072562 |
blood microparticle |
| Cellular Component |
GO:0009986 |
cell surface |
| Cellular Component |
GO:0009897 |
external side of plasma membrane |
| Cellular Component |
GO:0070062 |
extracellular exosome |
| Cellular Component |
GO:0031012 |
extracellular matrix |
| Cellular Component |
GO:0005576 |
extracellular region |
| Cellular Component |
GO:0005615 |
extracellular space |
| Cellular Component |
GO:0098978 |
glutamatergic synapse |
| Cellular Component |
GO:0005886 |
plasma membrane |
| Cellular Component |
GO:0031093 |
platelet alpha granule lumen |
| Cellular Component |
GO:0098685 |
Schaffer collateral - CA1 synapse |
| Molecular Function |
GO:0034185 |
apolipoprotein binding |
| Molecular Function |
GO:0004175 |
endopeptidase activity |
| Molecular Function |
GO:0019899 |
enzyme binding |
| Molecular Function |
GO:0019900 |
kinase binding |
| Molecular Function |
GO:0002020 |
protease binding |
| Molecular Function |
GO:1990405 |
protein antigen binding |
| Molecular Function |
GO:0019904 |
protein domain specific binding |
| Molecular Function |
GO:0051087 |
protein-folding chaperone binding |
| Molecular Function |
GO:0004252 |
serine-type endopeptidase activity |
| Molecular Function |
GO:0008236 |
serine-type peptidase activity |
| Molecular Function |
GO:0005102 |
signaling receptor binding |
| Biological Process |
GO:0051702 |
biological process involved in interaction with symbiont |
| Biological Process |
GO:0007596 |
blood coagulation |
| Biological Process |
GO:0030574 |
collagen catabolic process |
| Biological Process |
GO:0022617 |
extracellular matrix disassembly |
| Biological Process |
GO:0042730 |
fibrinolysis |
| Biological Process |
GO:2000048 |
negative regulation of cell-cell adhesion mediated by cadherin |
| Biological Process |
GO:0010812 |
negative regulation of cell-substrate adhesion |
| Biological Process |
GO:0051918 |
negative regulation of fibrinolysis |
| Biological Process |
GO:0043536 |
positive regulation of blood vessel endothelial cell migration |
| Biological Process |
GO:0051919 |
positive regulation of fibrinolysis |
| Biological Process |
GO:0006508 |
proteolysis |
| Biological Process |
GO:0048771 |
tissue remodeling |
| Biological Process |
GO:0099183 |
trans-synaptic signaling by BDNF, modulating synaptic transmission |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.