A2AP_MOUSE
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 03-AUG-2022, entry version 175.
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, Spleen,
RC 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 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; Q61247; -.
DR PeptideAtlas; Q61247; -.
DR PRIDE; Q61247; -.
DR ProteomicsDB; 286005; -.
DR Antibodypedia; 852; 562 antibodies from 39 providers.
DR DNASU; 18816; -.
DR Ensembl; ENSMUST00000043696; ENSMUSP00000048704; ENSMUSG00000038224.
DR Ensembl; ENSMUST00000108437; ENSMUSP00000104076; ENSMUSG00000038224.
DR GeneID; 18816; -.
DR KEGG; mmu:18816; -.
DR UCSC; uc007kdr.2; mouse.
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; EMTWKKS; -.
DR OrthoDB; 1124079at2759; -.
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 71 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 63 other tissues.
DR ExpressionAtlas; Q61247; baseline and differential.
DR Genevisible; Q61247; MM.
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: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:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
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; -; 1.
DR Gene3D; 3.30.497.10; -; 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; PTHR11461; 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; 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
