ID   A2AP_MOUSE              Reviewed;         491 AA.
AC   Q61247;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   24-JAN-2024, entry version 183.
DE   RecName: Full=Alpha-2-antiplasmin;
DE            Short=Alpha-2-AP;
DE   AltName: Full=Alpha-2-plasmin inhibitor;
DE            Short=Alpha-2-PI;
DE   AltName: Full=Serpin F2;
DE   Flags: Precursor;
GN   Name=Serpinf2; Synonyms=Pli;
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].
RC   STRAIN=C57BL/6 X CBA; TISSUE=Liver;
RX   PubMed=8647939; DOI=10.1172/jci118694;
RA   Menoud P.-A., Sappino N., Boudal-Khoshbeen M., Vassalli J.-D.,
RA   Sappino A.P.;
RT   "The kidney is a major site of alpha(2)-antiplasmin production.";
RL   J. Clin. Invest. 97:2478-2484(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver;
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   [3]
RP   PROTEIN SEQUENCE OF 28-33.
RX   PubMed=7523120; DOI=10.1111/j.1432-1033.1994.00863.x;
RA   Lijnen H.R., van Hoef B., Beelen V., Collen D.;
RT   "Characterization of the murine plasma fibrinolytic system.";
RL   Eur. J. Biochem. 224:863-871(1994).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC   Spleen, and Testis;
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: Serine protease inhibitor. The major targets of this
CC       inhibitor are plasmin and trypsin, but it also inactivates matriptase-
CC       3/TMPRSS7 and chymotrypsin (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Forms protease inhibiting heterodimer with TMPRSS7.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
CC   -!- PTM: Proteolytically cleaved at Pro-35 by both the prolyl endopeptidase
CC       FAP form and antiplasmin-cleaving enzyme FAP soluble form to generate
CC       mature alpha-2-antiplasmin. {ECO:0000250|UniProtKB:P08697}.
CC   -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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DR   EMBL; Z36774; CAA85350.1; -; mRNA.
DR   EMBL; BC026756; AAH26756.1; -; mRNA.
DR   CCDS; CCDS25046.1; -.
DR   PIR; S47217; S47217.
DR   RefSeq; NP_032904.1; NM_008878.2.
DR   PDB; 2R9Y; X-ray; 2.65 A; A=71-491.
DR   PDBsum; 2R9Y; -.
DR   AlphaFoldDB; Q61247; -.
DR   SMR; Q61247; -.
DR   BioGRID; 202249; 3.
DR   STRING; 10090.ENSMUSP00000048704; -.
DR   MEROPS; I04.023; -.
DR   GlyCosmos; Q61247; 4 sites, No reported glycans.
DR   GlyGen; Q61247; 4 sites.
DR   iPTMnet; Q61247; -.
DR   PhosphoSitePlus; Q61247; -.
DR   CPTAC; non-CPTAC-3405; -.
DR   CPTAC; non-CPTAC-5573; -.
DR   MaxQB; Q61247; -.
DR   PaxDb; 10090-ENSMUSP00000048704; -.
DR   PeptideAtlas; Q61247; -.
DR   ProteomicsDB; 286005; -.
DR   Antibodypedia; 852; 612 antibodies from 39 providers.
DR   DNASU; 18816; -.
DR   Ensembl; ENSMUST00000043696.9; ENSMUSP00000048704.3; ENSMUSG00000038224.13.
DR   Ensembl; ENSMUST00000108437.8; ENSMUSP00000104076.2; ENSMUSG00000038224.13.
DR   GeneID; 18816; -.
DR   KEGG; mmu:18816; -.
DR   UCSC; uc007kdr.2; mouse.
DR   AGR; MGI:107173; -.
DR   CTD; 5345; -.
DR   MGI; MGI:107173; Serpinf2.
DR   VEuPathDB; HostDB:ENSMUSG00000038224; -.
DR   eggNOG; KOG2392; Eukaryota.
DR   GeneTree; ENSGT00940000158386; -.
DR   HOGENOM; CLU_023330_3_2_1; -.
DR   InParanoid; Q61247; -.
DR   OMA; HAYPLRW; -.
DR   OrthoDB; 3218836at2759; -.
DR   PhylomeDB; Q61247; -.
DR   TreeFam; TF317350; -.
DR   Reactome; R-MMU-114608; Platelet degranulation.
DR   Reactome; R-MMU-75205; Dissolution of Fibrin Clot.
DR   BioGRID-ORCS; 18816; 2 hits in 76 CRISPR screens.
DR   ChiTaRS; Serpinf2; mouse.
DR   EvolutionaryTrace; Q61247; -.
DR   PRO; PR:Q61247; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q61247; Protein.
DR   Bgee; ENSMUSG00000038224; Expressed in yolk sac and 66 other cell types or tissues.
DR   ExpressionAtlas; Q61247; baseline and differential.
DR   GO; GO:0009986; C:cell surface; ISO:MGI.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0005615; C:extracellular space; ISO:MGI.
DR   GO; GO:0005577; C:fibrinogen complex; ISO:MGI.
DR   GO; GO:0004866; F:endopeptidase inhibitor activity; ISO:MGI.
DR   GO; GO:0002020; F:protease binding; ISO:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; ISO:MGI.
DR   GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
DR   GO; GO:0048514; P:blood vessel morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0030199; P:collagen fibril organization; IMP:BHF-UCL.
DR   GO; GO:0002034; P:maintenance of blood vessel diameter homeostasis by renin-angiotensin; IMP:BHF-UCL.
DR   GO; GO:0051918; P:negative regulation of fibrinolysis; ISO:MGI.
DR   GO; GO:0010757; P:negative regulation of plasminogen activation; ISO:MGI.
DR   GO; GO:0045597; P:positive regulation of cell differentiation; IMP:BHF-UCL.
DR   GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IMP:BHF-UCL.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR   GO; GO:0046330; P:positive regulation of JNK cascade; ISO:MGI.
DR   GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IMP:BHF-UCL.
DR   GO; GO:0051496; P:positive regulation of stress fiber assembly; ISO:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR   GO; GO:0071636; P:positive regulation of transforming growth factor beta production; IMP:BHF-UCL.
DR   CDD; cd02053; serpinF2_A2AP; 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; IPR033833; Alpha2AP_serpin_dom.
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:SF20; ALPHA-2-ANTIPLASMIN; 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; Q61247; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Acute phase; Direct protein sequencing; Disulfide bond;
KW   Glycoprotein; Protease inhibitor; Reference proteome; Secreted;
KW   Serine protease inhibitor; Signal; Sulfation.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000269|PubMed:7523120"
FT   PROPEP          28..39
FT                   /evidence="ECO:0000269|PubMed:7523120"
FT                   /id="PRO_0000430668"
FT   CHAIN           40..491
FT                   /note="Alpha-2-antiplasmin"
FT                   /id="PRO_0000032513"
FT   REGION          439..491
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            39..40
FT                   /note="Cleavage; by prolyl endopeptidase FAP, antiplasmin-
FT                   cleaving enzyme FAP soluble form"
FT                   /evidence="ECO:0000250|UniProtKB:P08697"
FT   SITE            403..404
FT                   /note="Reactive bond for plasmin"
FT   SITE            404..405
FT                   /note="Reactive bond for chymotrypsin"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         484
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        126
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        295
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        309
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        316
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        70..143
FT                   /evidence="ECO:0000250"
FT   HELIX           76..100
FT                   /evidence="ECO:0007829|PDB:2R9Y"
FT   STRAND          103..108
FT                   /evidence="ECO:0007829|PDB:2R9Y"
FT   HELIX           110..123
FT                   /evidence="ECO:0007829|PDB:2R9Y"
FT   HELIX           126..135
FT                   /evidence="ECO:0007829|PDB:2R9Y"
FT   HELIX           144..153
FT                   /evidence="ECO:0007829|PDB:2R9Y"
FT   STRAND          157..168
FT                   /evidence="ECO:0007829|PDB:2R9Y"
FT   HELIX           176..186
FT                   /evidence="ECO:0007829|PDB:2R9Y"
FT   HELIX           197..211
FT                   /evidence="ECO:0007829|PDB:2R9Y"
FT   TURN            212..214
FT                   /evidence="ECO:0007829|PDB:2R9Y"
FT   STRAND          228..238
FT                   /evidence="ECO:0007829|PDB:2R9Y"
FT   STRAND          241..243
FT                   /evidence="ECO:0007829|PDB:2R9Y"
FT   HELIX           247..249
FT                   /evidence="ECO:0007829|PDB:2R9Y"
FT   STRAND          251..280
FT                   /evidence="ECO:0007829|PDB:2R9Y"
FT   TURN            281..284
FT                   /evidence="ECO:0007829|PDB:2R9Y"
FT   STRAND          285..306
FT                   /evidence="ECO:0007829|PDB:2R9Y"
FT   HELIX           310..314
FT                   /evidence="ECO:0007829|PDB:2R9Y"
FT   HELIX           319..322
FT                   /evidence="ECO:0007829|PDB:2R9Y"
FT   STRAND          330..337
FT                   /evidence="ECO:0007829|PDB:2R9Y"
FT   STRAND          339..346
FT                   /evidence="ECO:0007829|PDB:2R9Y"
FT   HELIX           348..354
FT                   /evidence="ECO:0007829|PDB:2R9Y"
FT   HELIX           357..360
FT                   /evidence="ECO:0007829|PDB:2R9Y"
FT   TURN            366..368
FT                   /evidence="ECO:0007829|PDB:2R9Y"
FT   STRAND          375..386
FT                   /evidence="ECO:0007829|PDB:2R9Y"
FT   STRAND          390..392
FT                   /evidence="ECO:0007829|PDB:2R9Y"
FT   STRAND          407..410
FT                   /evidence="ECO:0007829|PDB:2R9Y"
FT   STRAND          415..421
FT                   /evidence="ECO:0007829|PDB:2R9Y"
FT   TURN            422..424
FT                   /evidence="ECO:0007829|PDB:2R9Y"
FT   STRAND          427..434
FT                   /evidence="ECO:0007829|PDB:2R9Y"
SQ   SEQUENCE   491 AA;  54972 MW;  B828DECADF0BB5B4 CRC64;
     MALLRGLLVL SLSCLQGPCF TFSPVSAVDL PGQQPVSEQA QQKLPLPALF KLDNQDFGDH
     ATLKRSPGHC KSVPTAEETR RLAQAMMAFT TDLFSLVAQT STSSNLVLSP LSVALALSHL
     ALGAQNQTLH SLHRVLHMNT GSCLPHLLSH FYQNLGPGTI RLAARIYLQK GFPIKDDFLE
     QSERLFGAKP VKLTGKQEED LANINQWVKE ATEGKIEDFL SELPDSTVLL LLNAIHFHGF
     WRTKFDPSLT QKDFFHLDER FTVSVDMMHA VSYPLRWFLL EQPEIQVAHF PFKNNMSFVV
     VMPTYFEWNV SEVLANLTWD TLYHPSLQER PTKVWLPKLH LQQQLDLVAT LSQLGLQELF
     QGPDLRGISE QNLVVSSVQH QSTMELSEAG VEAAAATSVA MNRMSLSSFT VNRPFLFFIM
     EDTIGVPLFV GSVRNPNPSA LPQLQEQRDS PDNRLIGQND KADFHGGKTF GPDLKLAPRM
     EEDYPQFSSP K
//