ID   PAI2_RAT                Reviewed;         416 AA.
AC   P29524;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   02-SEP-2026, entry version 162.
DE   RecName: Full=Plasminogen activator inhibitor 2 type A;
DE            Short=PAI-2;
DE            Short=PAI2A;
DE   AltName: Full=Serpin B2;
GN   Name=Serpinb2; Synonyms=Pai2, Planh2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Grundmann U., Rein T.;
RL   Submitted (FEB-1992) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Inhibits urokinase-type plasminogen activator.
CC   -!- SUBUNIT: Interacts with PSMB1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Secreted, extracellular
CC       space {ECO:0000250}.
CC   -!- PTM: The signal sequence is not cleaved. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the serpin family. Ov-serpin subfamily.
CC       {ECO:0000305}.
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DR   EMBL; X64563; CAA45864.1; -; mRNA.
DR   PIR; S19896; S19896.
DR   RefSeq; NP_067728.1; NM_021696.2.
DR   RefSeq; XP_006249701.1; XM_006249639.5.
DR   RefSeq; XP_008767717.1; XM_008769495.4.
DR   AlphaFoldDB; P29524; -.
DR   SMR; P29524; -.
DR   FunCoup; P29524; 80.
DR   STRING; 10116.ENSRNOP00000003409; -.
DR   MEROPS; I04.007; -.
DR   GlyCosmos; P29524; 4 sites, No reported glycans.
DR   GlyGen; P29524; 4 sites.
DR   PhosphoSitePlus; P29524; -.
DR   PaxDb; 10116-ENSRNOP00000003409; -.
DR   Ensembl; ENSRNOT00000003409.7; ENSRNOP00000003409.4; ENSRNOG00000002460.7.
DR   Ensembl; ENSRNOT00055020006; ENSRNOP00055016117; ENSRNOG00055011772.
DR   Ensembl; ENSRNOT00060015866; ENSRNOP00060012390; ENSRNOG00060009407.
DR   Ensembl; ENSRNOT00065023431; ENSRNOP00065018229; ENSRNOG00065014204.
DR   GeneID; 60325; -.
DR   KEGG; rno:60325; -.
DR   UCSC; RGD:621823; rat.
DR   AGR; RGD:621823; -.
DR   CTD; 5055; -.
DR   RGD; 621823; Serpinb2.
DR   eggNOG; KOG2392; Eukaryota.
DR   GeneTree; ENSGT00940000161637; -.
DR   HOGENOM; CLU_023330_0_2_1; -.
DR   InParanoid; P29524; -.
DR   OMA; MEDLYVA; -.
DR   OrthoDB; 671595at2759; -.
DR   PhylomeDB; P29524; -.
DR   Reactome; R-RNO-75205; Dissolution of Fibrin Clot.
DR   PRO; PR:P29524; -.
DR   Proteomes; UP000002494; Chromosome 13.
DR   Bgee; ENSRNOG00000002460; Expressed in esophagus and 3 other cell types or tissues.
DR   ExpressionAtlas; P29524; baseline and differential.
DR   GO; GO:0001533; C:cornified envelope; ISO:RGD.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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   CDD; cd19562; serpinB2_PAI-2; 1.
DR   FunFam; 2.30.39.10:FF:000001; Serpin family B member 2; 1.
DR   Gene3D; 2.30.39.10; Alpha-1-antitrypsin, domain 1; 1.
DR   Gene3D; 3.30.497.10; Antithrombin, subunit I, domain 2; 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:SF61; PLASMINOGEN ACTIVATOR INHIBITOR 2; 1.
DR   PANTHER; PTHR11461; SERINE PROTEASE INHIBITOR, SERPIN; 1.
DR   Pfam; PF00079; Serpin; 1.
DR   SMART; SM00093; SERPIN; 1.
DR   SUPFAM; SSF56574; Serpins; 1.
DR   PROSITE; PS00284; SERPIN; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Glycoprotein; Plasminogen activation; Protease inhibitor;
KW   Reference proteome; Secreted; Serine protease inhibitor; Signal.
FT   CHAIN           1..416
FT                   /note="Plasminogen activator inhibitor 2 type A"
FT                   /id="PRO_0000223298"
FT   SIGNAL          1..?
FT                   /note="Not cleaved"
FT                   /evidence="ECO:0000250"
FT   SITE            381..382
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        23
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        228
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        262
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        402
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   416 AA;  47248 MW;  2877EDFB6AF8B81F CRC64;
     MEELSMANTM FALNLLKQIE QSNSTQNIFI SPWSISSTLA IVFLGAQANT EEQMAKVLNF
     DKIGSYDLTP GNPENFHGCD FAQHIQRDNY PVAILQAQAR DKIHSAFSSL SSTINTPRLG
     DYLLESANKL FGEKSARFKE EYIQRCKKYY STEPEAVDFL ECANEARKKI NSWVKTQTKG
     EIPNLLPEGS VDEDTKMVLV NTIYFKGRWK TPFQKRLNGL YPFRVNLNES KPVQMMYLRE
     KLNIGYIKDL KTQILELPYI GNISMFLLLP DEIEDSSTGL EMLEREINFD NFNKWISKET
     LDEDDVLVYI PKFKLAQNYE LKPILQRMGM EDAFNKGKAD FSGMSESNDL FLSEVFHQAT
     VDVNEEGTVA AGGTGAVMTG RTGHGGPQFV ADHPFLFFIM NNITRTILFV GRFSSP
//