ID   PAI2_HUMAN              Reviewed;         415 AA.
AC   P05120; Q96E96;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   24-JAN-2024, entry version 225.
DE   RecName: Full=Plasminogen activator inhibitor 2;
DE            Short=PAI-2;
DE   AltName: Full=Monocyte Arg-serpin;
DE   AltName: Full=Placental plasminogen activator inhibitor;
DE   AltName: Full=Serpin B2;
DE   AltName: Full=Urokinase inhibitor;
DE   Flags: Precursor;
GN   Name=SERPINB2; Synonyms=PAI2, PLANH2;
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 [MRNA].
RC   TISSUE=Placenta;
RX   PubMed=3029122; DOI=10.1016/s0021-9258(18)61414-0;
RA   Ye R.D., Wun T.-Z., Sadler J.E.;
RT   "cDNA cloning and expression in Escherichia coli of a plasminogen activator
RT   inhibitor from human placenta.";
RL   J. Biol. Chem. 262:3718-3725(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3325828; DOI=10.1128/mcb.7.12.4564-4567.1987;
RA   Schleuning W.-D., Medcalf R.L., Hession C., Rothenbuhler R., Shaw A.,
RA   Kruithof E.K.O.;
RT   "Plasminogen activator inhibitor 2: regulation of gene transcription during
RT   phorbol ester-mediated differentiation of U-937 human histiocytic lymphoma
RT   cells.";
RL   Mol. Cell. Biol. 7:4564-4567(1987).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Monocyte;
RX   PubMed=3496414; DOI=10.1084/jem.166.1.77;
RA   Webb A.C., Collins K.L., Snyder S.F., Alexander S.J., Rosenwasser L.J.,
RA   Eddy R.L., Shows T.B., Auron P.E.;
RT   "Human monocyte Arg-Serpin cDNA. Sequence, chromosomal assignment, and
RT   homology to plasminogen activator-inhibitor.";
RL   J. Exp. Med. 166:77-94(1987).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Monocyte;
RX   PubMed=3257578; DOI=10.1073/pnas.85.4.985;
RA   Antalis T.M., Clark M.A., Barnes T., Lehrbach P.R., Devine P.L.,
RA   Schevzov G., Goss N.H., Stephens R.W., Tolstoshev P.;
RT   "Cloning and expression of a cDNA coding for a human monocyte-derived
RT   plasminogen activator inhibitor.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:985-989(1988).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2494165; DOI=10.1016/s0021-9258(18)83572-4;
RA   Ye R.D., Ahern S.M., le Beau M.M., Lebo R.V., Sadler J.E.;
RT   "Structure of the gene for human plasminogen activator inhibitor-2. The
RT   nearest mammalian homologue of chicken ovalbumin.";
RL   J. Biol. Chem. 264:5495-5502(1989).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2303256; DOI=10.1016/0888-7543(90)90461-3;
RA   Samia J.A., Alexander S.J., Horton K.W., Auron P.E., Byers M.G.,
RA   Shows T.B. Jr., Webb A.C.;
RT   "Chromosomal organization and localization of the human urokinase inhibitor
RT   gene: perfect structural conservation with ovalbumin.";
RL   Genomics 6:159-167(1990).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   PROTEIN SEQUENCE OF 12-17; 103-108 AND 314-321.
RX   PubMed=1286667; DOI=10.1002/elps.11501301199;
RA   Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
RA   Vandekerckhove J.;
RT   "Microsequences of 145 proteins recorded in the two-dimensional gel protein
RT   database of normal human epidermal keratinocytes.";
RL   Electrophoresis 13:960-969(1992).
RN   [9]
RP   INTERACTION WITH PSMB1.
RX   PubMed=14732874; DOI=10.1093/abbs/36.1.42;
RA   Fan J., Zhang Y.Q., Li P., Hou M., Tan L., Wang X., Zhu Y.S.;
RT   "Interaction of plasminogen activator inhibitor-2 and proteasome subunit,
RT   beta type 1.";
RL   Acta Biochim. Biophys. Sin. 36:42-46(2004).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX   PubMed=10368272; DOI=10.1016/s0969-2126(99)80008-2;
RA   Harrop S.J., Jankova L., Coles M., Jardine D., Whittaker J.S., Gould A.R.,
RA   Meister A., King G.C., Mabbutt B.C., Curmi P.M.G.;
RT   "The crystal structure of plasminogen activator inhibitor 2 at 2.0-A
RT   resolution: implications for serpin function.";
RL   Structure 7:43-54(1999).
RN   [12]
RP   VARIANTS ASP-120; HIS-229; LYS-404 AND CYS-413.
RX   PubMed=10391209; DOI=10.1038/10290;
RA   Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA   Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA   Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA   Lander E.S.;
RT   "Characterization of single-nucleotide polymorphisms in coding regions of
RT   human genes.";
RL   Nat. Genet. 22:231-238(1999).
RN   [13]
RP   ERRATUM OF PUBMED:10391209.
RA   Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA   Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA   Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA   Lander E.S.;
RL   Nat. Genet. 23:373-373(1999).
CC   -!- FUNCTION: Inhibits urokinase-type plasminogen activator. The monocyte
CC       derived PAI-2 is distinct from the endothelial cell-derived PAI-1.
CC   -!- SUBUNIT: Interacts with PSMB1. {ECO:0000269|PubMed:14732874}.
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; J02685; AAA36413.1; -; mRNA.
DR   EMBL; M18082; AAA60006.1; -; mRNA.
DR   EMBL; Y00630; CAA68666.1; -; mRNA.
DR   EMBL; J03603; AAA60004.1; -; mRNA.
DR   EMBL; M24657; AAA60348.1; -; Genomic_DNA.
DR   EMBL; M24651; AAA60348.1; JOINED; Genomic_DNA.
DR   EMBL; M24652; AAA60348.1; JOINED; Genomic_DNA.
DR   EMBL; M24653; AAA60348.1; JOINED; Genomic_DNA.
DR   EMBL; M24654; AAA60348.1; JOINED; Genomic_DNA.
DR   EMBL; M24655; AAA60348.1; JOINED; Genomic_DNA.
DR   EMBL; M24656; AAA60348.1; JOINED; Genomic_DNA.
DR   EMBL; M31551; AAA36797.1; -; Genomic_DNA.
DR   EMBL; M31547; AAA36797.1; JOINED; Genomic_DNA.
DR   EMBL; M31548; AAA36797.1; JOINED; Genomic_DNA.
DR   EMBL; M31549; AAA36797.1; JOINED; Genomic_DNA.
DR   EMBL; M31550; AAA36797.1; JOINED; Genomic_DNA.
DR   EMBL; BC012609; AAH12609.1; -; mRNA.
DR   CCDS; CCDS11989.1; -.
DR   PIR; A32853; A32853.
DR   RefSeq; NP_001137290.1; NM_001143818.1.
DR   RefSeq; NP_002566.1; NM_002575.2.
DR   PDB; 1BY7; X-ray; 2.00 A; A=1-415.
DR   PDB; 1JRR; X-ray; 1.60 A; A=1-415, P=367-380.
DR   PDB; 2ARQ; X-ray; 1.85 A; A=1-415, P=367-380.
DR   PDB; 2ARR; X-ray; 1.55 A; A=1-415, P=367-380.
DR   PDBsum; 1BY7; -.
DR   PDBsum; 1JRR; -.
DR   PDBsum; 2ARQ; -.
DR   PDBsum; 2ARR; -.
DR   AlphaFoldDB; P05120; -.
DR   SMR; P05120; -.
DR   BioGRID; 111092; 132.
DR   IntAct; P05120; 47.
DR   STRING; 9606.ENSP00000401645; -.
DR   DrugBank; DB06245; Lanoteplase.
DR   DrugBank; DB00031; Tenecteplase.
DR   DrugBank; DB00013; Urokinase.
DR   MEROPS; I04.007; -.
DR   GlyCosmos; P05120; 3 sites, No reported glycans.
DR   GlyGen; P05120; 3 sites.
DR   iPTMnet; P05120; -.
DR   PhosphoSitePlus; P05120; -.
DR   SwissPalm; P05120; -.
DR   BioMuta; SERPINB2; -.
DR   DMDM; 1352712; -.
DR   EPD; P05120; -.
DR   jPOST; P05120; -.
DR   MassIVE; P05120; -.
DR   MaxQB; P05120; -.
DR   PaxDb; 9606-ENSP00000401645; -.
DR   PeptideAtlas; P05120; -.
DR   ProteomicsDB; 51801; -.
DR   Pumba; P05120; -.
DR   Antibodypedia; 1909; 540 antibodies from 34 providers.
DR   DNASU; 5055; -.
DR   Ensembl; ENST00000299502.9; ENSP00000299502.4; ENSG00000197632.9.
DR   Ensembl; ENST00000457692.5; ENSP00000401645.1; ENSG00000197632.9.
DR   GeneID; 5055; -.
DR   KEGG; hsa:5055; -.
DR   MANE-Select; ENST00000299502.9; ENSP00000299502.4; NM_002575.3; NP_002566.1.
DR   UCSC; uc002ljo.4; human.
DR   AGR; HGNC:8584; -.
DR   CTD; 5055; -.
DR   DisGeNET; 5055; -.
DR   GeneCards; SERPINB2; -.
DR   HGNC; HGNC:8584; SERPINB2.
DR   HPA; ENSG00000197632; Tissue enhanced (esophagus, lymphoid tissue, skin).
DR   MIM; 173390; gene.
DR   neXtProt; NX_P05120; -.
DR   OpenTargets; ENSG00000197632; -.
DR   PharmGKB; PA35500; -.
DR   VEuPathDB; HostDB:ENSG00000197632; -.
DR   eggNOG; KOG2392; Eukaryota.
DR   GeneTree; ENSGT00940000161637; -.
DR   HOGENOM; CLU_023330_0_2_1; -.
DR   InParanoid; P05120; -.
DR   OMA; FFKQQCQ; -.
DR   OrthoDB; 3218836at2759; -.
DR   PhylomeDB; P05120; -.
DR   TreeFam; TF352619; -.
DR   PathwayCommons; P05120; -.
DR   Reactome; R-HSA-75205; Dissolution of Fibrin Clot.
DR   Reactome; R-HSA-8950505; Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation.
DR   SignaLink; P05120; -.
DR   SIGNOR; P05120; -.
DR   BioGRID-ORCS; 5055; 12 hits in 1157 CRISPR screens.
DR   ChiTaRS; SERPINB2; human.
DR   EvolutionaryTrace; P05120; -.
DR   GeneWiki; Plasminogen_activator_inhibitor-2; -.
DR   GenomeRNAi; 5055; -.
DR   Pharos; P05120; Tbio.
DR   PRO; PR:P05120; -.
DR   Proteomes; UP000005640; Chromosome 18.
DR   RNAct; P05120; Protein.
DR   Bgee; ENSG00000197632; Expressed in amniotic fluid and 116 other cell types or tissues.
DR   ExpressionAtlas; P05120; baseline and differential.
DR   GO; GO:0001533; C:cornified envelope; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR   GO; GO:0042730; P:fibrinolysis; TAS:Reactome.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; TAS:ProtInc.
DR   CDD; cd19562; serpinB2_PAI-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.
DR   Genevisible; P05120; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Direct protein sequencing; Disulfide bond;
KW   Glycoprotein; Plasminogen activation; Protease inhibitor;
KW   Reference proteome; Secreted; Serine protease inhibitor; Signal.
FT   CHAIN           1..415
FT                   /note="Plasminogen activator inhibitor 2"
FT                   /id="PRO_0000223296"
FT   SIGNAL          1..?
FT                   /note="Not cleaved"
FT   SITE            380..381
FT                   /note="Reactive bond"
FT   CARBOHYD        75
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        115
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        339
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        5..405
FT   VARIANT         120
FT                   /note="N -> D (in dbSNP:rs6098)"
FT                   /evidence="ECO:0000269|PubMed:10391209"
FT                   /id="VAR_011743"
FT   VARIANT         229
FT                   /note="R -> H (in dbSNP:rs6100)"
FT                   /evidence="ECO:0000269|PubMed:10391209"
FT                   /id="VAR_014173"
FT   VARIANT         374
FT                   /note="G -> A (in dbSNP:rs34066931)"
FT                   /id="VAR_051946"
FT   VARIANT         404
FT                   /note="N -> K (in dbSNP:rs6103)"
FT                   /evidence="ECO:0000269|PubMed:10391209"
FT                   /id="VAR_011744"
FT   VARIANT         413
FT                   /note="S -> C (in dbSNP:rs6104)"
FT                   /evidence="ECO:0000269|PubMed:10391209"
FT                   /id="VAR_011745"
FT   CONFLICT        170
FT                   /note="N -> Y (in Ref. 7; AAH12609)"
FT                   /evidence="ECO:0000305"
FT   HELIX           6..22
FT                   /evidence="ECO:0007829|PDB:2ARR"
FT   STRAND          24..26
FT                   /evidence="ECO:0007829|PDB:2ARR"
FT   STRAND          28..30
FT                   /evidence="ECO:0007829|PDB:2ARR"
FT   HELIX           32..45
FT                   /evidence="ECO:0007829|PDB:2ARR"
FT   HELIX           48..57
FT                   /evidence="ECO:0007829|PDB:2ARR"
FT   TURN            58..62
FT                   /evidence="ECO:0007829|PDB:2ARR"
FT   HELIX           100..102
FT                   /evidence="ECO:0007829|PDB:1BY7"
FT   HELIX           103..115
FT                   /evidence="ECO:0007829|PDB:2ARR"
FT   STRAND          122..132
FT                   /evidence="ECO:0007829|PDB:2ARR"
FT   HELIX           139..149
FT                   /evidence="ECO:0007829|PDB:2ARR"
FT   STRAND          154..156
FT                   /evidence="ECO:0007829|PDB:2ARR"
FT   HELIX           158..176
FT                   /evidence="ECO:0007829|PDB:2ARR"
FT   TURN            177..179
FT                   /evidence="ECO:0007829|PDB:2ARR"
FT   STRAND          194..205
FT                   /evidence="ECO:0007829|PDB:2ARR"
FT   STRAND          208..210
FT                   /evidence="ECO:0007829|PDB:2ARR"
FT   STRAND          220..225
FT                   /evidence="ECO:0007829|PDB:2ARR"
FT   STRAND          228..232
FT                   /evidence="ECO:0007829|PDB:2ARR"
FT   STRAND          234..246
FT                   /evidence="ECO:0007829|PDB:2ARR"
FT   HELIX           247..249
FT                   /evidence="ECO:0007829|PDB:2ARR"
FT   STRAND          251..269
FT                   /evidence="ECO:0007829|PDB:2ARR"
FT   STRAND          275..278
FT                   /evidence="ECO:0007829|PDB:2ARR"
FT   HELIX           280..285
FT                   /evidence="ECO:0007829|PDB:2ARR"
FT   HELIX           288..295
FT                   /evidence="ECO:0007829|PDB:2ARR"
FT   TURN            297..299
FT                   /evidence="ECO:0007829|PDB:1BY7"
FT   STRAND          301..310
FT                   /evidence="ECO:0007829|PDB:2ARR"
FT   STRAND          312..319
FT                   /evidence="ECO:0007829|PDB:2ARR"
FT   HELIX           321..327
FT                   /evidence="ECO:0007829|PDB:2ARR"
FT   HELIX           331..333
FT                   /evidence="ECO:0007829|PDB:2ARR"
FT   TURN            335..337
FT                   /evidence="ECO:0007829|PDB:2ARR"
FT   TURN            341..343
FT                   /evidence="ECO:0007829|PDB:2ARR"
FT   STRAND          349..362
FT                   /evidence="ECO:0007829|PDB:2ARR"
FT   STRAND          368..379
FT                   /evidence="ECO:0007829|PDB:2ARR"
FT   STRAND          387..389
FT                   /evidence="ECO:0007829|PDB:2ARR"
FT   STRAND          394..400
FT                   /evidence="ECO:0007829|PDB:2ARR"
FT   TURN            401..404
FT                   /evidence="ECO:0007829|PDB:2ARR"
FT   STRAND          405..412
FT                   /evidence="ECO:0007829|PDB:2ARR"
SQ   SEQUENCE   415 AA;  46596 MW;  10DFAB5A4B1246FF CRC64;
     MEDLCVANTL FALNLFKHLA KASPTQNLFL SPWSISSTMA MVYMGSRGST EDQMAKVLQF
     NEVGANAVTP MTPENFTSCG FMQQIQKGSY PDAILQAQAA DKIHSSFRSL SSAINASTGN
     YLLESVNKLF GEKSASFREE YIRLCQKYYS SEPQAVDFLE CAEEARKKIN SWVKTQTKGK
     IPNLLPEGSV DGDTRMVLVN AVYFKGKWKT PFEKKLNGLY PFRVNSAQRT PVQMMYLREK
     LNIGYIEDLK AQILELPYAG DVSMFLLLPD EIADVSTGLE LLESEITYDK LNKWTSKDKM
     AEDEVEVYIP QFKLEEHYEL RSILRSMGME DAFNKGRANF SGMSERNDLF LSEVFHQAMV
     DVNEEGTEAA AGTGGVMTGR TGHGGPQFVA DHPFLFLIMH KITNCILFFG RFSSP
//