ID   PLMN_PETMA              Reviewed;         325 AA.
AC   P33574;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Plasminogen;
DE            EC=3.4.21.7;
DE   Flags: Fragments;
OS   Petromyzon marinus (Sea lamprey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata;
OC   Hyperoartia; Petromyzontiformes; Petromyzontidae; Petromyzon.
OX   NCBI_TaxID=7757;
RN   [1]
RP   PROTEIN SEQUENCE.
RA   Affolter M., Schaller J., Rickli E.E.;
RT   "Isolation, characterization and partial amino acid sequence of lamprey
RT   plasminogen.";
RL   Protein Seq. Data Anal. 5:207-211(1993).
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.
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   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Plasminogen subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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   PIR; S33879; S33879.
DR   MEROPS; S01.233; -.
DR   Proteomes; UP000245300; 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   Gene3D; 2.40.20.10; -; 2.
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   Pfam; PF00051; Kringle; 2.
DR   SMART; SM00130; KR; 2.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   SUPFAM; SSF57440; SSF57440; 3.
DR   PROSITE; PS00021; KRINGLE_1; 2.
DR   PROSITE; PS50070; KRINGLE_2; 2.
PE   1: Evidence at protein level;
KW   Blood coagulation; Direct protein sequencing; Disulfide bond; Fibrinolysis;
KW   Hemostasis; Hydrolase; Kringle; Protease; Reference proteome; Secreted;
KW   Serine protease; Tissue remodeling; Zymogen.
FT   CHAIN           1..>325
FT                   /note="Plasminogen"
FT                   /id="PRO_0000088706"
FT   DOMAIN          80..146
FT                   /note="Kringle 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT   DOMAIN          159..217
FT                   /note="Kringle 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT   DISULFID        81..146
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT   DISULFID        102..135
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT   DISULFID        124..141
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT   DISULFID        188..212
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT   NON_CONS        15..16
FT                   /evidence="ECO:0000305"
FT   NON_CONS        34..35
FT                   /evidence="ECO:0000305"
FT   NON_CONS        44..45
FT                   /evidence="ECO:0000305"
FT   NON_CONS        76..77
FT                   /evidence="ECO:0000305"
FT   NON_CONS        111..112
FT                   /evidence="ECO:0000305"
FT   NON_CONS        138..139
FT                   /evidence="ECO:0000305"
FT   NON_CONS        158..159
FT                   /evidence="ECO:0000305"
FT   NON_CONS        178..179
FT                   /evidence="ECO:0000305"
FT   NON_CONS        216..217
FT                   /evidence="ECO:0000305"
FT   NON_CONS        236..237
FT                   /evidence="ECO:0000305"
FT   NON_CONS        267..268
FT                   /evidence="ECO:0000305"
FT   NON_CONS        282..283
FT                   /evidence="ECO:0000305"
FT   NON_CONS        295..296
FT                   /evidence="ECO:0000305"
FT   NON_CONS        307..308
FT                   /evidence="ECO:0000305"
FT   NON_CONS        315..316
FT                   /evidence="ECO:0000305"
FT   NON_TER         325
SQ   SEQUENCE   325 AA;  35206 MW;  1B5F0B539AC6ED3C CRC64;
     APIKGYSVTV XLYIFDCQKW SSNYPHKPNF SDATDPKGPW CYTTDYXGAA SVTRSGLRGD
     EQTPHRHTFS PQSFAGLTTA CVKGTGEGYR GTAALTVSGK ACQAWASQTP GDVYSCQGLV
     SNYCRNPDGE KLPWCYTTEY CNVPSCTGGP TGSEYHEILT PAQDXYTGIV EDYRGKMSPD
     AGLEENFCRN PDQDPQGPWC YTXNPEAXPR YCDVLSVVGG XEAQRNSXPR QISLQYGWQT
     VHVQSIHAEP RGVDIALVKI APPAQLTACV ITXWGETQGT GEDVQFCAGY PEGGTDPVSL
     VCLEPCVLAP VLVGVVILPX NDRXQ