PLGA_HUMAN
ID PLGA_HUMAN Reviewed; 96 AA.
AC Q15195;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Plasminogen-like protein A;
DE AltName: Full=Plasminogen-like protein A1;
DE AltName: Full=Plasminogen-related protein A;
DE Flags: Precursor;
GN Name=PLGLA; Synonyms=PLGLA1, PLGP2, PRGA;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1554698; DOI=10.1021/bi00127a011;
RA Ichinose A.;
RT "Multiple members of the plasminogen-apolipoprotein(a) gene family
RT associated with thrombosis.";
RL Biochemistry 31:3113-3118(1992).
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=10092845; DOI=10.1046/j.1432-1327.1999.00055.x;
RA Lewis V.O., Gehrmann M., Weissbach L., Hyman J.E., Rielly A., Jones D.G.,
RA Llinas M., Schaller J.;
RT "Homologous plasminogen N-terminal and plasminogen-related gene A and B
RT peptides. Characterization of cDNAs and recombinant fusion proteins.";
RL Eur. J. Biochem. 259:618-625(1999).
CC -!- FUNCTION: May bind non-covalently to lysine binding sites present in
CC the kringle structures of plasminogen. This may interfere with the
CC binding of fibrin or alpha-2-antiplasmin to plasminogen and may result
CC in the localization of activity at sites necessary for extracellular
CC matrix destruction (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in liver. {ECO:0000269|PubMed:10092845}.
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DR EMBL; M86873; AAA60168.1; -; Genomic_DNA.
DR EMBL; M86871; AAA60168.1; JOINED; Genomic_DNA.
DR EMBL; M86872; AAA60168.1; JOINED; Genomic_DNA.
DR AlphaFoldDB; Q15195; -.
DR SMR; Q15195; -.
DR iPTMnet; Q15195; -.
DR PhosphoSitePlus; Q15195; -.
DR BioMuta; HGNC:9074; -.
DR DMDM; 74706526; -.
DR jPOST; Q15195; -.
DR MassIVE; Q15195; -.
DR PeptideAtlas; Q15195; -.
DR PRIDE; Q15195; -.
DR ProteomicsDB; 60487; -.
DR GeneCards; PLGLA; -.
DR HGNC; HGNC:9074; PLGLA.
DR MIM; 612212; gene.
DR neXtProt; NX_Q15195; -.
DR InParanoid; Q15195; -.
DR PhylomeDB; Q15195; -.
DR Pharos; Q15195; Tdark.
DR PRO; PR:Q15195; -.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; Q15195; protein.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0036313; F:phosphatidylinositol 3-kinase catalytic subunit binding; IBA:GO_Central.
DR GO; GO:0043553; P:negative regulation of phosphatidylinositol 3-kinase activity; IBA:GO_Central.
DR GO; GO:0014067; P:negative regulation of phosphatidylinositol 3-kinase signaling; IBA:GO_Central.
DR InterPro; IPR003609; Pan_app.
DR InterPro; IPR016351; Plasminogen-rel.
DR Pfam; PF00024; PAN_1; 1.
DR PIRSF; PIRSF002483; Plasminogen-related; 1.
DR SMART; SM00473; PAN_AP; 1.
DR PROSITE; PS50948; PAN; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..96
FT /note="Plasminogen-like protein A"
FT /id="PRO_0000305905"
FT DOMAIN 20..96
FT /note="PAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DISULFID 49..73
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DISULFID 53..61
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
SQ SEQUENCE 96 AA; 10915 MW; CE2C29452F2BA171 CRC64;
MEHKEVVLLL LLFLKSGQGE PLDDYVNAQG ASLFSVTKKQ LGAGSREECA AKCEEDKEFT
CRAFQYHSKE QQCVIMAENK KSSIIIRMRD VVLFEK