ID A0A091QSR7_MERNU Unreviewed; 785 AA.
AC A0A091QSR7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Plasminogen {ECO:0000256|ARBA:ARBA00020043};
DE EC=3.4.21.7 {ECO:0000256|ARBA:ARBA00012184};
DE Flags: Fragment;
GN ORFNames=N331_12645 {ECO:0000313|EMBL:KFQ30228.1};
OS Merops nubicus (Northern carmine bee-eater).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Coraciiformes; Meropidae; Merops.
OX NCBI_TaxID=57421 {ECO:0000313|EMBL:KFQ30228.1, ECO:0000313|Proteomes:UP000052967};
RN [1] {ECO:0000313|EMBL:KFQ30228.1, ECO:0000313|Proteomes:UP000052967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N331 {ECO:0000313|EMBL:KFQ30228.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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 -!- 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}.
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DR EMBL; KK705817; KFQ30228.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091QSR7; -.
DR Proteomes; UP000052967; 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; cd00190; Tryp_SPc; 1.
DR Gene3D; 3.50.4.10; Hepatocyte Growth Factor; 1.
DR Gene3D; 2.40.20.10; Plasminogen Kringle 4; 4.
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; 1.
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:UP000052967};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW Tissue remodeling {ECO:0000256|ARBA:ARBA00023148};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 1..81
FT /note="Apple"
FT /evidence="ECO:0000259|PROSITE:PS50948"
FT DOMAIN 85..164
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 167..245
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 257..335
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 356..434
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 455..535
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 556..783
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT ACT_SITE 597
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001150-1"
FT ACT_SITE 640
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001150-1"
FT ACT_SITE 735
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001150-1"
FT BINDING 141
FT /ligand="L-lysine"
FT /ligand_id="ChEBI:CHEBI:32551"
FT /evidence="ECO:0000256|PIRSR:PIRSR001150-2"
FT BINDING 155
FT /ligand="L-lysine"
FT /ligand_id="ChEBI:CHEBI:32551"
FT /evidence="ECO:0000256|PIRSR:PIRSR001150-2"
FT BINDING 412
FT /ligand="L-lysine"
FT /ligand_id="ChEBI:CHEBI:32551"
FT /evidence="ECO:0000256|PIRSR:PIRSR001150-2"
FT BINDING 425
FT /ligand="L-lysine"
FT /ligand_id="ChEBI:CHEBI:32551"
FT /evidence="ECO:0000256|PIRSR:PIRSR001150-2"
FT DISULFID 168..245
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 189..228
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 217..240
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 258..335
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 279..318
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 307..330
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 357..434
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 378..417
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 406..429
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ30228.1"
FT NON_TER 785
FT /evidence="ECO:0000313|EMBL:KFQ30228.1"
SQ SEQUENCE 785 AA; 88829 MW; AEDA2A1A5A3D2B79 CRC64;
QGNVLDSYVK TEGAWLLNPK KQIYKAKSKE ECAEQCEAET KFTCRAFLFT SKDQQCLTLA
ENTKTAVIFR RTNAVLYEKR IYLLECKKGN GVDYRGTEAK TQRGVPCQKW GDSDPHKPNY
TPEKYPSAGL EENYCRNPDN DEKGPWCYTT DPATRFDYCN IPECEEECMH CSGENYHGVV
STTESGLECQ PWDSQEPHSH GYLPENFPEK DLRKNYCRNP DGEPRPWCFT TSPTKRWEYC
NIPRCTTPPP APAPGRQCLS GRGEDYRGTI SVTESGNTCQ HWSSQTPHRH ARTPENYPCK
SLEENYCRNP DGEKMPWCYT TNRTARWEYC TIPSCDGTKP EAPAVDEPEQ AEVTEECYEG
NGVTYRGTAS FTVTGKKCQA WSSMSPHRHN KTAEHFPNAD LKQNYCRNPD ADSRPWCYTT
DPSVRWEYCD LKRCDVHVQV TLPKPPQTTV DSNLDCINGN GKDYRGTVAK TGRGRTCQEW
SSQRPHAHDY FTPMTHPRAG LDKNYCRNPD GDVNGPWCYT TDPRKAWEYC DIPKCPPAQY
ECGKSKFRPK LCAQRIVAGC VSHPHSWPWQ ISLRTSYGLH FCGGTLIDPQ WVLTAAHCLE
RSSRPSSYKV YLGLHRERAS EPSVQKQDVE KLFKEPNKAD IALLKLSSPA IINNHVIPVC
LPKEHSVLGG REECYVTGWG DTRGTGGDGY LKETGFPVIE NKICNRPEFL NGRVKKNELC
AGNIHGGTDS CQGDSGGPLV CLDQDKFVQH GVTSWGLGCA QPMKPGVYVR VSNYIPWIRS
IMENN
//
