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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
 
 
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