ID A0A8U0QI18_SALNM Unreviewed; 1504 AA.
AC A0A8U0QI18;
DT 12-OCT-2022, integrated into UniProtKB/TrEMBL.
DT 12-OCT-2022, sequence version 1.
DT 28-JAN-2026, entry version 17.
DE SubName: Full=Plasminogen-like {ECO:0000313|RefSeq:XP_038844093.1};
GN Name=LOC120043602 {ECO:0000313|RefSeq:XP_038844093.1};
OS Salvelinus namaycush (Lake trout) (Salmo namaycush).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salvelinus.
OX NCBI_TaxID=8040 {ECO:0000313|Proteomes:UP000808372, ECO:0000313|RefSeq:XP_038844093.1};
RN [1] {ECO:0000313|RefSeq:XP_038844093.1}
RP IDENTIFICATION.
RC TISSUE=White muscle {ECO:0000313|RefSeq:XP_038844093.1};
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
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_038844093.1; XM_038988165.1.
DR GeneID; 120043602; -.
DR KEGG; snh:120043602; -.
DR Proteomes; UP000808372; Unplaced.
DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0005102; F:signaling receptor binding; IEA:TreeGrafter.
DR GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00108; KR; 12.
DR CDD; cd01099; PAN_AP_HGF; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR FunFam; 2.40.20.10:FF:000011; Plasminogen; 10.
DR FunFam; 3.50.4.10:FF:000027; Plasminogen; 1.
DR FunFam; 2.40.10.10:FF:000003; Transmembrane serine protease 3; 1.
DR Gene3D; 3.50.4.10; Hepatocyte Growth Factor; 1.
DR Gene3D; 2.40.20.10; Plasminogen Kringle 4; 12.
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; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR050759; Serine_protease_kringle.
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; 12.
DR Pfam; PF00024; PAN_1; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR PRINTS; PR00018; KRINGLE.
DR SMART; SM00130; KR; 12.
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; 12.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS00021; KRINGLE_1; 11.
DR PROSITE; PS50070; KRINGLE_2; 12.
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}; Hemostasis {ECO:0000256|ARBA:ARBA00022696};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363034};
KW Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW ProRule:PRU00121};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU363034};
KW Reference proteome {ECO:0000313|Proteomes:UP000808372};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU363034}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1504
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5035936704"
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 193..271
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 313..391
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 409..487
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 505..583
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 601..679
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 697..775
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 793..871
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 889..967
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 985..1063
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 1081..1159
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 1166..1246
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 1274..1501
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 1194..1219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1194..1204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 194..271
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 215..254
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 243..266
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 314..391
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 335..374
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 363..386
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 410..487
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 431..470
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 459..482
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 506..583
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 527..566
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 555..578
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 602..679
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 623..662
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 651..674
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 698..775
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 719..758
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 747..770
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 794..871
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 815..854
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 843..866
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 890..967
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 911..950
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 939..962
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 986..1063
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 1007..1046
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 1035..1058
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 1082..1159
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 1103..1142
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 1131..1154
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
SQ SEQUENCE 1504 AA; 165381 MW; 32343579B5D709B1 CRC64;
MDLYKAVLLG VLFSAVSAGV LDEYAKTEGA RIMSILKREY SVGTVLECAI KCNAETAFTC
RSFIYIEKDQ ECLTIPANTK TEHVLRRTST ALYEKKVYLM ECVNGIGMDY RGTKSKTKSG
KTCQRWASKY PHNPNMTPST HPNADLESNF CRNPDGDSKG PWCYTKDPET RWETCNVQDC
SASKPPTVVE ELTCSTGDGV AYRGTVAVTT SGKACQAWAA QTPQKHNRTP DNYPSNGLTL
NYCRNPDNER MPWCYTTDPE TRWEYCKVPS CGDVPGPGHF TLSCDDDDDD VNALDLFCSK
ELLKPPTVVE ELTCSTGDGV AYRGTVAVTT SGKACQAWAA QTPQKHNRTP DNYPSNGLTL
NYCRNPDNER MPWCYTTDPE TRWEYCKVPS CGDVPGPASK PPTVVEELTC STGDGVAYRG
TVAVTTSGKA CQAWAAQTPQ KHNRTPDNYP SNGLTLNYCR NPDNERMPWC YTTDPETRWE
YCKVPSCGDV PGPASKPPTV VEELTCSTGD GVAYRGTVAV TTSGKACQAW AAQTPQKHNR
TPDNYPSNGL DLNYCRNPDN ERMPWCYTTD PETRWEYCKV PSCGDVPGPA SKPPTVVEEL
TCSTGDGVAY RGTVAVTTSG KACQAWAAQT PQKHNRTPDN YPSNGLDLNY CRNPDNERMP
WCYTTDPETR WEYCKVPSCG DVPGPASKPP TVVEELTCST GDGVAYRGTV AVTTSGKACQ
AWAAQTPQKH NRTPDNYPSK GLDLNYCRNP DNERMPWCYT TDPETRWEYC KVPSCGDVPG
PASKPPTVVE ELTCSTGDGV AYRGTVAVTT SGKACQAWAA QTPQKHNRTP DNYPSNGLDL
NYCRNPDNER MPWCYTTDPE TRWEYCKVPS CGDVPGPASK PPTVVEELTC STGDGVAYRG
TVAVTMSGKA CQAWAAQTPQ KHNRTPDNYP SKGLDLNYCR NPDNERMPWC YTTDPETRWE
YCKVPSCGDV PGPASKPPTV VEELTCSTGD GVAYRGTVAV TTSGKACQAW AAQTPQKHNR
TPDNYPSKGL DLNYCRNPDN ERMPWCYTTD PETRWEYCKV PSCGDVPGPA SEPPTVVEEL
TCSTGDGVAY RGTVAVTTSG KACQAWAAQT PQKHNRTPDN YPSNGLDLNY CRNPDNERMP
WCYTTDPETR WEYCKVPSCG DVPGPDCKVG NGGTYRGPAS MTMLGVTCQR WSSQSPHQHA
SFNPESHPDK GLESNNCRNP DNDVNGPWCY TTDRSKKWDY CQIPECAGLK CGQPVTKPKR
CFGRKSNQIK LYRIVGGCVS KPHSWPWQIS LRTNTGVHFC GGTLIAPQWV LTAAHCLERS
KRPSAYKVFM GTHTERGNEA TKQERNLEKL ILGPDRTDIA LLKLETPALI NDKVLPACLP
EKDYVVPPGT ECYVTGWGET QGTGGDGILK ETGFPVIENK VCNRPAYLNN RVKDHEMCAG
NIEGGTDSCQ GDSGGPLVCH AQNSFVLQGV TSWGLGCANA LKPGVYARVS KFTDWINSQM
KIHS
//
