ID S7PRA1_MYOBR Unreviewed; 840 AA.
AC S7PRA1;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Plasminogen {ECO:0000256|ARBA:ARBA00020043};
DE EC=3.4.21.7 {ECO:0000256|ARBA:ARBA00012184};
GN ORFNames=D623_10006400 {ECO:0000313|EMBL:EPQ13353.1};
OS Myotis brandtii (Brandt's bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ13353.1, ECO:0000313|Proteomes:UP000052978};
RN [1] {ECO:0000313|Proteomes:UP000052978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23962925; DOI=10.1038/ncomms3212;
RA Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y.,
RA Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., Hee Yim S.,
RA Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., Chen G., Kulakova O.I.,
RA Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., Sunyaev S.R., Zhang G.,
RA Krogh A., Wang J., Gladyshev V.N.;
RT "Genome analysis reveals insights into physiology and longevity of the
RT Brandt's bat Myotis brandtii.";
RL Nat. Commun. 4:2212-2212(2013).
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.
CC {ECO:0000256|ARBA:ARBA00025229}.
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; Evidence={ECO:0000256|ARBA:ARBA00000717};
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:0000256|ARBA:ARBA00038571}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00121}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KE163695; EPQ13353.1; -; Genomic_DNA.
DR AlphaFoldDB; S7PRA1; -.
DR MEROPS; S01.233; -.
DR eggNOG; ENOG502QVNP; Eukaryota.
DR Proteomes; UP000052978; Unassembled WGS sequence.
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; 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; 5.
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; 2.
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 4: Predicted;
KW Blood coagulation {ECO:0000256|ARBA:ARBA00023084};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00121}; Fibrinolysis {ECO:0000256|ARBA:ARBA00023281};
KW Hemostasis {ECO:0000256|ARBA:ARBA00022696};
KW Hydrolase {ECO:0000256|RuleBase:RU363034};
KW Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW ProRule:PRU00121}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protease {ECO:0000256|RuleBase:RU363034};
KW Reference proteome {ECO:0000313|Proteomes:UP000052978};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW Signal {ECO:0000256|SAM:SignalP};
KW Tissue remodeling {ECO:0000256|ARBA:ARBA00023148};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..840
FT /note="Plasminogen"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004543660"
FT DOMAIN 20..98
FT /note="Apple"
FT /evidence="ECO:0000259|PROSITE:PS50948"
FT DOMAIN 102..181
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 184..262
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 274..352
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 376..454
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 510..590
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 611..838
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 460..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 652
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001150-1"
FT ACT_SITE 695
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001150-1"
FT ACT_SITE 790
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001150-1"
FT BINDING 136
FT /ligand="L-lysine"
FT /ligand_id="ChEBI:CHEBI:32551"
FT /evidence="ECO:0000256|PIRSR:PIRSR001150-2"
FT BINDING 158
FT /ligand="L-lysine"
FT /ligand_id="ChEBI:CHEBI:32551"
FT /evidence="ECO:0000256|PIRSR:PIRSR001150-2"
FT BINDING 172
FT /ligand="L-lysine"
FT /ligand_id="ChEBI:CHEBI:32551"
FT /evidence="ECO:0000256|PIRSR:PIRSR001150-2"
FT BINDING 432
FT /ligand="L-lysine"
FT /ligand_id="ChEBI:CHEBI:32551"
FT /evidence="ECO:0000256|PIRSR:PIRSR001150-2"
FT BINDING 445
FT /ligand="L-lysine"
FT /ligand_id="ChEBI:CHEBI:32551"
FT /evidence="ECO:0000256|PIRSR:PIRSR001150-2"
FT DISULFID 185..262
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 206..245
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 234..257
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 275..352
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 296..335
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 324..347
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 377..454
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 398..437
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 426..449
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
SQ SEQUENCE 840 AA; 93078 MW; FF87C22233612DCE CRC64;
MGRQELLLLL LLFLRPGHGD PLDSYVNTQG ASLITLTRKE LPAGSIAECA AKCEEETTFT
CRSFQYHSKE QHCVVMGDNS KSAPVLRMRD VVLYEKRIYL SECKTGNGRR YRGTVSKTKN
GVACQKWSDH SPHIPRFSPT SHPLEGLEEN YCRNPDNDEK GPWCYTTDPA TRFDYCTIPE
CEEECMHCSG ENYEGTISRT KSGLECQAWD SQTPHAHGYI PAKFPSKNLK MNYCRNPDGE
PSPWCFTTNP NKRWELCDIP RCTTPPPSSG PTHQCLKGRG ESYVGKVAVT LSGHTCQRWS
EQTPHKHNRT PENFPCKNLE ENYCRNPDGE SAPWCFTTNS KVRWEHCKIP SCESSQLSPE
QAEATVPPEQ TPVVQECYHG NGQSYRGTSS TTITGRKCQS WSSMTPHRHS KTPDQIPNAG
LTMNYCRNPD GDKGPWCYTT DPSVRWEFCN LKKCSETQGA VMNTPPEVPP VSPQGSSEAE
AGPDIGEPAA AALVPHPRST EPDLRPLPAD CMLGNGKGYR GKKATTVAGT ACQAWAAQEP
HRHSIFTPET NPRAGLEKNY CRNPDGDVNG PWCYTTDPKK LFDYCDVPQC ASSSFDCGKP
KVEPKKCPGR VVGGCVANPH SWPWQVSLRT RFRMHFCGGT LLSPDWVLTA AHCLERSSRP
SSYKVILGAH HEQNLEADVQ ERDVSKLVLE PTRADIALLK LSSPAIITDK VIPACLPSAD
YVVADRTVCY ITGWGETQGT FGAGLLKEAQ LPVIENKVCN RYEYLNGRVK STELCAGLLA
GGADSCQGDS GGPLVCFEKD KYILQGVTSW GLGCARPNKP GVYVRVSRFV KWIEETMKNN
//
