ID I3ME10_ICTTR Unreviewed; 560 AA.
AC I3ME10;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=Plasminogen activator {ECO:0000256|PIRNR:PIRNR001145};
DE EC=3.4.21.68 {ECO:0000256|PIRNR:PIRNR001145};
GN Name=PLAT {ECO:0000313|Ensembl:ENSSTOP00000008687.3};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000008687.3, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000008687.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Specific cleavage of Arg-|-Val bond in plasminogen to form
CC plasmin.; EC=3.4.21.68; Evidence={ECO:0000256|ARBA:ARBA00001538,
CC ECO:0000256|PIRNR:PIRNR001145};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|PIRNR:PIRNR001145}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC {ECO:0000256|PIRNR:PIRNR001145}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; AGTP01107042; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; I3ME10; -.
DR STRING; 43179.ENSSTOP00000008687; -.
DR Ensembl; ENSSTOT00000009683.3; ENSSTOP00000008687.3; ENSSTOG00000009680.3.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000158930; -.
DR HOGENOM; CLU_006842_18_4_1; -.
DR InParanoid; I3ME10; -.
DR TreeFam; TF329901; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR GO; GO:0030141; C:secretory granule; IEA:Ensembl.
DR GO; GO:0097180; C:serine protease inhibitor complex; IEA:Ensembl.
DR GO; GO:0051219; F:phosphoprotein binding; IEA:Ensembl.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
DR GO; GO:0045861; P:negative regulation of proteolysis; IEA:Ensembl.
DR GO; GO:0031639; P:plasminogen activation; IEA:Ensembl.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0014909; P:smooth muscle cell migration; IEA:Ensembl.
DR GO; GO:0099183; P:trans-synaptic signaling by BDNF, modulating synaptic transmission; IEA:Ensembl.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00061; FN1; 1.
DR CDD; cd00108; KR; 2.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 1.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR Gene3D; 2.40.20.10; Plasminogen Kringle 4; 2.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000083; Fibronectin_type1.
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 InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR026280; Tissue_plasm_act.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24264:SF42; TISSUE-TYPE PLASMINOGEN ACTIVATOR; 1.
DR PANTHER; PTHR24264; TRYPSIN-RELATED; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF00039; fn1; 1.
DR Pfam; PF00051; Kringle; 2.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF001145; Tissue_plasm_act; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR PRINTS; PR00018; KRINGLE.
DR SMART; SM00181; EGF; 1.
DR SMART; SM00058; FN1; 1.
DR SMART; SM00130; KR; 2.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF57603; FnI-like domain; 1.
DR SUPFAM; SSF57440; Kringle-like; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01253; FN1_1; 1.
DR PROSITE; PS51091; FN1_2; 1.
DR PROSITE; PS00021; KRINGLE_1; 2.
DR PROSITE; PS50070; KRINGLE_2; 2.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR001145-3};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR001145};
KW Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW ProRule:PRU00121};
KW Plasminogen activation {ECO:0000256|ARBA:ARBA00023202,
KW ECO:0000256|PIRNR:PIRNR001145};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PIRNR:PIRNR001145};
KW Reference proteome {ECO:0000313|Proteomes:UP000005215};
KW Secreted {ECO:0000256|PIRNR:PIRNR001145};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|PIRNR:PIRNR001145}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..560
FT /note="Plasminogen activator"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012587648"
FT DOMAIN 36..78
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 79..117
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 123..205
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 212..294
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 309..559
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 39..49
FT /note="Important for binding to annexin A2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-2"
FT ACT_SITE 355
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-1"
FT ACT_SITE 404
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-1"
FT ACT_SITE 511
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-1"
FT SITE 99
FT /note="Important for binding to LRP1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-2"
FT SITE 462
FT /note="Important for single-chain activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-2"
FT SITE 510
FT /note="Important for single-chain activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-2"
FT DISULFID 38..68
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 66..75
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 83..94
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 88..105
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3,
FT ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 107..116
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3,
FT ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 124..205
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 145..187
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 176..200
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 213..294
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 234..276
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 265..289
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 297..428
FT /note="Interchain (between A and B chains)"
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 340..356
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 348..417
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 442..517
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 474..490
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 507..535
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
SQ SEQUENCE 560 AA; 63447 MW; 4CE77E1663A433CC CRC64;
MKKGLLCVLL LCEVVFTLPR QEIYTRFRRG ARSYRVMCRD EKTQMIYQQH ESWLRPMLRS
NRVEYCWCNS GRPQCHSVPI KSCSESRCFN GGTCWQAIYF SDFVCQCPEG FAGKRCEIDT
SATCYKDQGI TYRGTWSTVE SGAECVNWNS SVLALKSYNG RRPDAIKLGL GNHNYCRNPD
RDSKPWCYVF KAGKYTSEFC STPACSKGKN EDCYFGKGLA YRGTQSLTTS GASCLPWNSM
ILIGKSYTAW KTNSQALGLG KHNYCRNPDG DAKPWCHVLK DRKLTWEYCD MPQCSTCGLR
QYKQPQFRIK GGLFTDITSH PWQAAIFAKN RRSPGERFLC GGVLISSCWV LSAAHCFLER
FPPHHLKVVL GRTYRVVPGE EEQKFEVEKY IVHNEFDDDT YDNDIALLQL KSDSLQCAQD
SNSVRTVCLP DANLQLADWT ECELSGYGKH EASSPFYSER LKEAHVRLYP SSRCTSQHMF
NKTVTNNMLC AGDTRSGGNQ ANLHDACQGD SGGPLVCVKD KRMTLVGIIS WGLGCGKKDV
PGIYTKVTNY LDWIQKNMQP
//
