PAI2_MOUSE
ID PAI2_MOUSE Reviewed; 415 AA.
AC P12388; O35687; Q9QWP6; Q9QWP7; Q9QWP8; Q9QWP9; Q9QWQ0; Q9QWZ5; Q9QWZ6;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Plasminogen activator inhibitor 2, macrophage;
DE Short=PAI-2;
DE AltName: Full=Serpin B2;
GN Name=Serpinb2; Synonyms=Pai2, Planh2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-27.
RC STRAIN=AKR/J; TISSUE=Myeloid;
RX PubMed=2583099; DOI=10.1002/j.1460-2075.1989.tb08489.x;
RA Belin D., Wohlwend A., Schleuning W.-D., Kruithof E.K.O., Vassalli J.-D.;
RT "Facultative polypeptide translocation allows a single mRNA to encode the
RT secreted and cytosolic forms of plasminogen activators inhibitor 2.";
RL EMBO J. 8:3287-3294(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=AKR/J; TISSUE=Myeloid;
RA Belin D.;
RL Submitted (SEP-1989) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLU-239; TYR-258; ILE-259
RP AND ARG-284.
RC STRAIN=129; TISSUE=Liver;
RA Belin D., Tapparel C., Sappino N., Silva F.;
RT "Sequence and tissue-specific expression of the murine PAI-2 gene.";
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34; 54-74; 89-115; 124-156; 163-237
RP AND 265-302.
RC STRAIN=129/Sv;
RX PubMed=9892694; DOI=10.1073/pnas.96.2.686;
RA Dougherty K.M., Pearson J.M., Yang A.Y., Westrick R.J., Baker M.S.,
RA Ginsburg D.;
RT "The plasminogen activator inhibitor-2 gene is not required for normal
RT murine development or survival.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:686-691(1999).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Inhibits urokinase-type plasminogen activator. The monocyte
CC derived PAI-2 is distinct from the endothelial cell-derived PAI-1. Not
CC required for normal murine development or survival.
CC -!- SUBUNIT: Interacts with PSMB1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Secreted, extracellular space.
CC -!- PTM: The signal sequence is not cleaved.
CC -!- SIMILARITY: Belongs to the serpin family. Ov-serpin subfamily.
CC {ECO:0000305}.
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DR EMBL; X16490; CAA34507.1; -; mRNA.
DR EMBL; AJ000386; CAA04047.1; -; Genomic_DNA.
DR EMBL; AJ000384; CAA04047.1; JOINED; Genomic_DNA.
DR EMBL; AJ000385; CAA04047.1; JOINED; Genomic_DNA.
DR EMBL; AF069683; AAD08915.1; -; Genomic_DNA.
DR EMBL; AF069685; AAD08916.1; -; Genomic_DNA.
DR EMBL; AF069684; AAD08916.1; JOINED; Genomic_DNA.
DR EMBL; AF069687; AAD08917.1; -; Genomic_DNA.
DR EMBL; AF069686; AAD08917.1; JOINED; Genomic_DNA.
DR EMBL; AF069689; AAD08918.1; -; Genomic_DNA.
DR EMBL; AF069688; AAD08918.1; JOINED; Genomic_DNA.
DR EMBL; AF069690; AAD08919.1; -; Genomic_DNA.
DR EMBL; AF069692; AAD08920.1; -; Genomic_DNA.
DR EMBL; AF069691; AAD08920.1; JOINED; Genomic_DNA.
DR EMBL; AF069694; AAD08921.1; -; Genomic_DNA.
DR EMBL; AF069693; AAD08921.1; JOINED; Genomic_DNA.
DR CCDS; CCDS15219.1; -.
DR PIR; S20047; S20047.
DR RefSeq; NP_001167641.1; NM_001174170.1.
DR RefSeq; NP_035241.1; NM_011111.4.
DR AlphaFoldDB; P12388; -.
DR SMR; P12388; -.
DR STRING; 10090.ENSMUSP00000065277; -.
DR MEROPS; I04.007; -.
DR GlyGen; P12388; 4 sites.
DR PhosphoSitePlus; P12388; -.
DR PaxDb; P12388; -.
DR PeptideAtlas; P12388; -.
DR PRIDE; P12388; -.
DR ProteomicsDB; 294374; -.
DR Antibodypedia; 1909; 488 antibodies from 34 providers.
DR DNASU; 18788; -.
DR Ensembl; ENSMUST00000009356; ENSMUSP00000009356; ENSMUSG00000062345.
DR Ensembl; ENSMUST00000064916; ENSMUSP00000065277; ENSMUSG00000062345.
DR GeneID; 18788; -.
DR KEGG; mmu:18788; -.
DR UCSC; uc007chn.2; mouse.
DR CTD; 5055; -.
DR MGI; MGI:97609; Serpinb2.
DR VEuPathDB; HostDB:ENSMUSG00000062345; -.
DR eggNOG; KOG2392; Eukaryota.
DR GeneTree; ENSGT00940000161637; -.
DR HOGENOM; CLU_023330_0_2_1; -.
DR InParanoid; P12388; -.
DR OMA; YVANAIF; -.
DR OrthoDB; 1124079at2759; -.
DR PhylomeDB; P12388; -.
DR TreeFam; TF352619; -.
DR Reactome; R-MMU-75205; Dissolution of Fibrin Clot.
DR BioGRID-ORCS; 18788; 1 hit in 76 CRISPR screens.
DR ChiTaRS; Serpinb2; mouse.
DR PRO; PR:P12388; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P12388; protein.
DR Bgee; ENSMUSG00000062345; Expressed in skin of external ear and 63 other tissues.
DR ExpressionAtlas; P12388; baseline and differential.
DR Genevisible; P12388; MM.
DR GO; GO:0001533; C:cornified envelope; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:InterPro.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
DR GO; GO:0042060; P:wound healing; ISO:MGI.
DR Gene3D; 2.30.39.10; -; 1.
DR Gene3D; 3.30.497.10; -; 1.
DR InterPro; IPR015556; PAI-2.
DR InterPro; IPR023795; Serpin_CS.
DR InterPro; IPR023796; Serpin_dom.
DR InterPro; IPR000215; Serpin_fam.
DR InterPro; IPR036186; Serpin_sf.
DR InterPro; IPR042178; Serpin_sf_1.
DR InterPro; IPR042185; Serpin_sf_2.
DR PANTHER; PTHR11461; PTHR11461; 1.
DR PANTHER; PTHR11461:SF61; PTHR11461:SF61; 1.
DR Pfam; PF00079; Serpin; 1.
DR SMART; SM00093; SERPIN; 1.
DR SUPFAM; SSF56574; SSF56574; 1.
DR PROSITE; PS00284; SERPIN; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Glycoprotein; Plasminogen activation; Protease inhibitor;
KW Reference proteome; Secreted; Serine protease inhibitor; Signal.
FT CHAIN 1..415
FT /note="Plasminogen activator inhibitor 2, macrophage"
FT /id="PRO_0000223297"
FT SIGNAL 1..?
FT /note="Not cleaved"
FT SITE 380..381
FT /note="Reactive bond"
FT CARBOHYD 23
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 339
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 239
FT /note="A -> E"
FT /evidence="ECO:0000269|Ref.3"
FT VARIANT 258
FT /note="H -> Y"
FT /evidence="ECO:0000269|Ref.3"
FT VARIANT 259
FT /note="T -> I"
FT /evidence="ECO:0000269|Ref.3"
FT VARIANT 284
FT /note="S -> R"
FT /evidence="ECO:0000269|Ref.3"
FT CONFLICT 55
FT /note="A -> T (in Ref. 3 and 4)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 415 AA; 46292 MW; C4FC78C5C3CA7D8B CRC64;
MEELSMANTM FALNLLKQIE KSNSTQNIFI SPWSISSTLA IVLLGAGGNT EQQMAKVLQF
NEIGSYGITT RNPENFSGCD FAQQIQKENY PSAILQAQAG DKIHSAFSSL SSTINTPQGD
YLLESANKLF GEKSARFKEE YIQLSKKYYS TEPEAVDFLE CAEEAREKIN SWVKTQTKGE
IPNLLPEGSV DEDTKMVLVN AVYFKGKWKT PFEKKLNGLY PFRVNSHESI PVQMMFLHAK
LNIGYIKDLK TQILELPHTG NISMLLLLPD EIEDASTGLE LLESEINFAN FNKWISKDTL
DEDDVVVYIP KFKLAQSYEL KSILQSMGME DAFNKGKANF SGMSERNDLF LSEVFHQASV
DVTEEGTVAA GGTGAVMTGR TGHGGPQFVA DHPFLFFIMD KITHTILFVG RFSSP
