ID A0A1S3S8H0_SALSA Unreviewed; 805 AA.
AC A0A1S3S8H0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Plasminogen {ECO:0000256|ARBA:ARBA00020043, ECO:0000256|PIRNR:PIRNR001150};
DE EC=3.4.21.7 {ECO:0000256|ARBA:ARBA00012184, ECO:0000256|PIRNR:PIRNR001150};
GN Name=LOC106607797 {ECO:0000313|RefSeq:XP_014060635.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014060635.1};
RN [1] {ECO:0000313|RefSeq:XP_014060635.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014060635.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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, ECO:0000256|PIRNR:PIRNR001150}.
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 ECO:0000256|PIRNR:PIRNR001150};
CC -!- ACTIVITY REGULATION: Converted into plasmin by plasminogen activators,
CC both plasminogen and its activator being bound to fibrin.
CC {ECO:0000256|PIRNR:PIRNR001150}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613,
CC ECO:0000256|PIRNR:PIRNR001150}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Plasminogen subfamily.
CC {ECO:0000256|PIRNR:PIRNR001150}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00121}.
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DR RefSeq; XP_014060635.1; XM_014205160.1.
DR AlphaFoldDB; A0A1S3S8H0; -.
DR STRING; 8030.ENSSSAP00000081045; -.
DR PaxDb; 8030-ENSSSAP00000081045; -.
DR GeneID; 106607797; -.
DR KEGG; sasa:106607797; -.
DR CTD; 5340; -.
DR OrthoDB; 211181at2759; -.
DR Proteomes; UP000087266; Chromosome ssa06.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-UniRule.
DR GO; GO:0042730; P:fibrinolysis; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0048771; P:tissue remodeling; IEA:UniProtKB-UniRule.
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; 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; 3.
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 3: Inferred from homology;
KW Blood coagulation {ECO:0000256|ARBA:ARBA00023084,
KW ECO:0000256|PIRNR:PIRNR001150};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00121};
KW Fibrinolysis {ECO:0000256|ARBA:ARBA00023281,
KW ECO:0000256|PIRNR:PIRNR001150};
KW Hemostasis {ECO:0000256|ARBA:ARBA00022696, ECO:0000256|PIRNR:PIRNR001150};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR001150, 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|PIRNR:PIRNR001150, ECO:0000256|RuleBase:RU363034};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Secreted {ECO:0000256|PIRNR:PIRNR001150};
KW Serine protease {ECO:0000256|PIRNR:PIRNR001150,
KW ECO:0000256|RuleBase:RU363034}; Signal {ECO:0000256|SAM:SignalP};
KW Tissue remodeling {ECO:0000256|ARBA:ARBA00023148,
KW ECO:0000256|PIRNR:PIRNR001150}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..805
FT /note="Plasminogen"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010178985"
FT DOMAIN 16..97
FT /note="Apple"
FT /evidence="ECO:0000259|PROSITE:PS50948"
FT DOMAIN 101..180
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 183..261
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 273..351
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 368..446
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 476..556
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 575..802
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 448..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 616
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001150-1"
FT ACT_SITE 659
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001150-1"
FT ACT_SITE 754
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001150-1"
FT BINDING 157
FT /ligand="L-lysine"
FT /ligand_id="ChEBI:CHEBI:32551"
FT /evidence="ECO:0000256|PIRSR:PIRSR001150-2"
FT BINDING 171
FT /ligand="L-lysine"
FT /ligand_id="ChEBI:CHEBI:32551"
FT /evidence="ECO:0000256|PIRSR:PIRSR001150-2"
FT BINDING 424
FT /ligand="L-lysine"
FT /ligand_id="ChEBI:CHEBI:32551"
FT /evidence="ECO:0000256|PIRSR:PIRSR001150-2"
FT BINDING 437
FT /ligand="L-lysine"
FT /ligand_id="ChEBI:CHEBI:32551"
FT /evidence="ECO:0000256|PIRSR:PIRSR001150-2"
FT DISULFID 184..261
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 205..244
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 233..256
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 274..351
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 295..334
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 323..346
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 369..446
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 390..429
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 418..441
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
SQ SEQUENCE 805 AA; 89448 MW; 9E9F5EB137AF8625 CRC64;
MDLYKAMLLG VLFSAVSAGV LDEYAKTEGA RIISVLKREY SVGTVLECAI KCNAETAFTC
RSFIYIEKDQ ECMTIPANTK TEQVLRRTST ALYEKKVYLM ECVNGIGMDY RGTKSKTKSG
KTCQRWASKY PHNPNMTPST HPNADLESNF CRNPDGDSEG PWCYTRDPET RWETCNVQDC
SEECMHCSGE DYRGKISTTE NGYTCQRWNA QKPHNHGYSP SALPEKYLEE DYCRNPDGDP
RPWCFTTSPS KRWDFCSIPR CTSEPPTVVE ELTCSTGDGG AYRGTVAVTT SGKACQVWAA
QTPQKHNRTP DNYPCKGLDL NYCRNPDNER MPWCYTTDPE TRWEYCKVPS CGDVPGPDDA
APTPAEEDCY VGSGSEYRGM VTETISGKKC QSWSSMTPHS HKKTPQDFPK ADLRRNLCRN
PDGDRAPWCY TTDPSVRWEY CAVEKCPTAP KPTSKPDKPD KPDQLRPAPS QTPSPDCKVG
NGGTYRGPTS MTMLGVTCQR WSSQSPHQHA SFNPESHPDK GLESNNCRNP DNDVNGPWCY
TTDRSKKWDY CQIPDCAGLK CGQPVTKPKR CFGRIVGGCV SKPHSWPWQI SLRTNTGVHF
CGGTLIAPQW VLTAAHCLER SKRTSAYKVF LGTHTERANE ATKQERNLEK LILGPDRTDI
ALLKLQTPAL INDKVLPACL PEKDYVVPPG TECYVTGWGE TQGTGGDGLL KETGFPVIEN
KVCNRPAYLN NRVKDHEMCA GNIEGGTDSC QGDSGGPLVC HAQNSFVLQG VTSWGLGCAN
ALKPGVYARV SKFTDWINSQ MKINS
//
