ID A0A452DLA1_CAPHI Unreviewed; 560 AA.
AC A0A452DLA1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
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:ENSCHIP00000000198.1};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000000198.1, ECO:0000313|Proteomes:UP000291000};
RN [1] {ECO:0000313|Ensembl:ENSCHIP00000000198.1, ECO:0000313|Proteomes:UP000291000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCHIP00000000198.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; LWLT01000029; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A452DLA1; -.
DR Ensembl; ENSCHIT00000000222.1; ENSCHIP00000000198.1; ENSCHIG00000000147.1.
DR GeneTree; ENSGT00940000158930; -.
DR OMA; WCYIFKA; -.
DR Proteomes; UP000291000; Chromosome 27.
DR Bgee; ENSCHIG00000000147; Expressed in testis and 17 other cell types or tissues.
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:0031639; P:plasminogen activation; IEA:InterPro.
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; 1.
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:UP000291000};
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..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..560
FT /note="Plasminogen activator"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019395674"
FT DOMAIN 34..76
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 77..115
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 121..203
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 37..47
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 97
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 36..66
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 64..73
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 81..92
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 86..103
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3,
FT ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 105..114
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3,
FT ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 122..203
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 143..185
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 174..198
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; 62646 MW; E3B4866A31BF883D CRC64;
MMNAVKTQFL CLLLCGAVFT WPSQVEAGLS VVTVTCRDEK TQMTYLQHES WLRPLLRGNQ
VEHCRCNGGR AQCHSVPVRS CSEPWCFNGG TCQQALYSSE FVCQCPEGFM GKLCEIDATA
TCYKDQGVAY RGTWSTAESG AECASWNSSG LAMKPYSGRR PGAIRLGLGN HNYCRNPDQD
SKPWCYVFKA GKYVSEFCST PACTKAAEED GDCYTGNGLA YRGTRSRTKS GASCLPWNSV
FLTSKIYTAW KSNARALGLG KHNHCRNPDG DAQPWCHVWK DRQPTWEYCD VPQCVTCGLR
QYKRPQFRIK GGLFADITSH PWQAAIFVKN RRSPGQRFLC GGILISSCWV LSAAHCFQER
YPPHHLKVVL GRTYRLVPGE EEQMFEVEKY IVHKEFDDDT YDNDIALLHL KSDSLTCAQE
SGSVRTICLP DASLQLPDWT ECELSGYGKH EASSPFFSER LKEAHVRLYP SSRCTSRHLF
NRTVTNNMLC AGDTRSGGDH TNLHDACQGD SGGPLVCMKD NHMTLVGIIS WGLGCGQKDI
PGVYTKVTNY LDWIRDNMQP
//
