PAI2_HUMAN
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 03-AUG-2022, entry version 217.
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; 123.
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 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; P05120; -.
DR PeptideAtlas; P05120; -.
DR PRIDE; P05120; -.
DR ProteomicsDB; 51801; -.
DR Antibodypedia; 1909; 488 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 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; LECAEDT; -.
DR OrthoDB; 1124079at2759; -.
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 1071 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 tissues.
DR ExpressionAtlas; P05120; baseline and differential.
DR Genevisible; P05120; HS.
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 GO; GO:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
DR GO; GO:0042060; P:wound healing; IEA:Ensembl.
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 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
