PLMN_SHEEP
ID PLMN_SHEEP Reviewed; 343 AA.
AC P81286;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Plasminogen;
DE EC=3.4.21.7;
DE Flags: Fragment;
GN Name=PLG;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=1492092;
RA Schaller J., Straub C., Kampfer U., Rickli E.E.;
RT "Complete amino acid sequence of ovine miniplasminogen.";
RL Protein Seq. Data Anal. 5:21-25(1992).
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 -!- 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 PIR; B61545; B61545.
DR AlphaFoldDB; P81286; -.
DR SMR; P81286; -.
DR STRING; 9940.ENSOARP00000005065; -.
DR MEROPS; S01.233; -.
DR eggNOG; ENOG502QVNP; Eukaryota.
DR Proteomes; UP000002356; Unplaced.
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; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 1.
DR Gene3D; 2.40.20.10; -; 1.
DR InterPro; IPR000001; Kringle.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR018056; Kringle_CS.
DR InterPro; IPR038178; Kringle_sf.
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 Pfam; PF00051; Kringle; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00130; KR; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF57440; SSF57440; 1.
DR PROSITE; PS00021; KRINGLE_1; 1.
DR PROSITE; PS50070; KRINGLE_2; 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; Direct protein sequencing; Disulfide bond; Fibrinolysis;
KW Hemostasis; Hydrolase; Kringle; Phosphoprotein; Protease;
KW Reference proteome; Repeat; Secreted; Serine protease; Tissue remodeling;
KW Zymogen.
FT CHAIN <1..>343
FT /note="Plasminogen"
FT /id="PRO_0000088704"
FT DOMAIN <1..17
FT /note="Kringle 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 41..120
FT /note="Kringle 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 114..341
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION <1..140
FT /note="Plasmin heavy chain A"
FT REGION 141..>343
FT /note="Plasmin light chain B"
FT ACT_SITE 155
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 198
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 293
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00747"
FT MOD_RES 221
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00747"
FT DISULFID 15..94
FT /evidence="ECO:0000250"
FT DISULFID 36..77
FT /evidence="ECO:0000250"
FT DISULFID 65..89
FT /evidence="ECO:0000250"
FT DISULFID 140..156
FT /evidence="ECO:0000250"
FT DISULFID 232..299
FT /evidence="ECO:0000250"
FT DISULFID 262..278
FT /evidence="ECO:0000250"
FT DISULFID 289..317
FT /evidence="ECO:0000250"
FT NON_TER 1
FT NON_TER 343
SQ SEQUENCE 343 AA; 37662 MW; 8DF6EBA92D596EE0 CRC64;
APQAPSVENP PEADCMLGIG KGYRGKKATT VAGVPCQEWA AQEPHRHGIF TPETNPRAGL
EKNYCRNPDG DVNGPWCYTT NPRKLFDYCD IPQCESSFDC GKPKVEPKKC PARVVGGCVA
TPHSWPWQVS LRRRSREHFC GGTLISPEWV LTAAHCLDSI LGPSFYTVIL GAHYEMAREA
SVQEIPVSRL FLEPSRADIA LLKLSSPAVI TDEVIPACLP SPNYVVADKT VCYITGWGET
QGTFGVGRLK EARLPVIENK VCNRYEYLNG RVKSTELCAG DLAGGTDSCQ GDSGGPLVCF
EKDKYILQGV TSWGLGCARP NKPGVYVRVS TYVPWIEETM RRY
