ID A0A087QH19_APTFO Unreviewed; 789 AA.
AC A0A087QH19;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Plasminogen {ECO:0000256|ARBA:ARBA00020043};
DE EC=3.4.21.7 {ECO:0000256|ARBA:ARBA00012184};
DE Flags: Fragment;
GN ORFNames=AS27_01205 {ECO:0000313|EMBL:KFM00523.1};
OS Aptenodytes forsteri (Emperor penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC Aptenodytes.
OX NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM00523.1, ECO:0000313|Proteomes:UP000053286};
RN [1] {ECO:0000313|EMBL:KFM00523.1, ECO:0000313|Proteomes:UP000053286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM00523.1};
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; KL225581; KFM00523.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087QH19; -.
DR STRING; 9233.A0A087QH19; -.
DR Proteomes; UP000053286; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0042730; P:fibrinolysis; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
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 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.
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 Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW ProRule:PRU00121}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000053286};
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 175..253
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 265..342
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 361..439
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 468..548
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 553..789
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 444..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 417
FT /ligand="L-lysine"
FT /ligand_id="ChEBI:CHEBI:32551"
FT /evidence="ECO:0000256|PIRSR:PIRSR001150-2"
FT DISULFID 176..253
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 197..236
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 225..248
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 287..326
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 362..439
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 383..422
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 411..434
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFM00523.1"
FT NON_TER 789
FT /evidence="ECO:0000313|EMBL:KFM00523.1"
SQ SEQUENCE 789 AA; 89735 MW; FFD6FAD8C2191CBA CRC64;
KGDILDDYLR TDGVWILTRN KQFYKTNNEK ECAEKCEAER NFNCRAFLFT RKKLQCLTLA
ENAKMTVMFN SMDAVLYEKK IYLLQCKKGI GKDYRGTEAK TRRGIPCQKW AEKTPHNPNY
TPEKHPSAGL DENYCRNPDG DESGPWCYTT DPATRFDYCN IPECESQVTH TGEVECVQCN
GEDYHGEVSR TESGLECQRW DAQEPHMHGF TLKHFPEKDL KMNYCRNPDG ELRPWCFTTS
PAKRWEYCNI PHCTTHPPVS GLGSQCLSGK GEDYRGRIAI TESGNACQHW NTQFPHRHGW
IPDRYPCKGL EENYCRNPDG EKRPWCYTTS SVRWEYCAIP HCDGTEQGIV DAPVQVSLSE
ECYRGKGQSY RGTTSITVSG KKCQAWNSMF PHRHEKTPDR FPNADLRDNY CRNPDGDNSP
WCFTTDPSTI WEYCNLKRCD DHTQEPAPND PPATTAQNVG LTTPTTSDCI NGNGKDYRGT
VAKTGRGRTC QEWSSQKPHS HKYFTPVTHP RAGLDKNYCR NPDGDVNGVW CFTTDPEKKW
EHCEIPRCSS SEYNCGKVPM RSERACEQYS MCDAPPGSWP WHVSLRMSTN VHHCAGTLIH
PQWVLTAAQC LQESTKPSSY RVFLGIQNLN AAEPSLQIQS VQKVLKEPSG ADIALLKLNS
PVTITDHVKP VCLPETSLMV ERNTVCFLTA WEKTRDNRLK DMEFPVLENR VCNHPEFLNG
SVKNHEFCGG FTFGSIGNCQ AEVGGPLVCQ DKDRFVQYGV TSWGLDCTQP SKPVFVRIPN
FVSWIKNAM
//
