A2AP_BOVIN
ID A2AP_BOVIN Reviewed; 492 AA.
AC P28800;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 154.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], DISULFIDE BOND, AND GLYCOSYLATION AT ASN-127;
RP ASN-249; ASN-296; ASN-310 AND ASN-317.
RX PubMed=7513654; DOI=10.1016/0014-5793(94)80560-1;
RA Christensen S., Berglund L., Sottrup-Jensen L.;
RT "Primary structure of bovine alpha 2-antiplasmin.";
RL FEBS Lett. 343:223-228(1994).
RN [2]
RP PROTEIN SEQUENCE OF 23-45 AND 374-410.
RC TISSUE=Plasma;
RX PubMed=1385210; DOI=10.1016/0014-5793(92)81419-m;
RA Christensen S., Sottrup-Jensen L.;
RT "Bovine alpha 2-antiplasmin. N-terminal and reactive site sequence.";
RL FEBS Lett. 312:100-104(1992).
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-31 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; X78436; CAA55200.1; -; mRNA.
DR PIR; S43977; S43977.
DR RefSeq; NP_777095.1; NM_174670.2.
DR AlphaFoldDB; P28800; -.
DR SMR; P28800; -.
DR STRING; 9913.ENSBTAP00000027793; -.
DR MEROPS; I04.023; -.
DR iPTMnet; P28800; -.
DR PaxDb; P28800; -.
DR PeptideAtlas; P28800; -.
DR PRIDE; P28800; -.
DR Ensembl; ENSBTAT00000027793; ENSBTAP00000027793; ENSBTAG00000020859.
DR GeneID; 282522; -.
DR KEGG; bta:282522; -.
DR CTD; 5345; -.
DR VEuPathDB; HostDB:ENSBTAG00000020859; -.
DR VGNC; VGNC:34479; SERPINF2.
DR eggNOG; KOG2392; Eukaryota.
DR GeneTree; ENSGT00940000158386; -.
DR HOGENOM; CLU_023330_3_2_1; -.
DR InParanoid; P28800; -.
DR OMA; EMTWKKS; -.
DR OrthoDB; 1124079at2759; -.
DR TreeFam; TF317350; -.
DR Reactome; R-BTA-114608; Platelet degranulation.
DR Reactome; R-BTA-75205; Dissolution of Fibrin Clot.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000020859; Expressed in liver and 64 other tissues.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005577; C:fibrinogen complex; IEA:Ensembl.
DR GO; GO:0002020; F:protease binding; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
DR GO; GO:0048514; P:blood vessel morphogenesis; IEA:Ensembl.
DR GO; GO:0030199; P:collagen fibril organization; IEA:Ensembl.
DR GO; GO:0002034; P:maintenance of blood vessel diameter homeostasis by renin-angiotensin; IEA:Ensembl.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
DR GO; GO:0051918; P:negative regulation of fibrinolysis; IEA:Ensembl.
DR GO; GO:0010757; P:negative regulation of plasminogen activation; IEA:Ensembl.
DR GO; GO:0045597; P:positive regulation of cell differentiation; IEA:Ensembl.
DR GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IEA:Ensembl.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IEA:Ensembl.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0071636; P:positive regulation of transforming growth factor beta production; IEA:Ensembl.
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 Acute phase; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Protease inhibitor; Reference proteome; Secreted;
KW Serine protease inhibitor; Signal; Sulfation.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:1385210"
FT PROPEP 23..40
FT /evidence="ECO:0000269|PubMed:1385210"
FT /id="PRO_0000430667"
FT CHAIN 41..492
FT /note="Alpha-2-antiplasmin"
FT /id="PRO_0000032510"
FT REGION 56..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..479
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 40..41
FT /note="Cleavage; by prolyl endopeptidase FAP, antiplasmin-
FT cleaving enzyme FAP soluble form"
FT /evidence="ECO:0000250|UniProtKB:P08697"
FT SITE 404..405
FT /note="Reactive bond for plasmin"
FT SITE 405..406
FT /note="Reactive bond for chymotrypsin"
FT MOD_RES 485
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:7513654"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:7513654"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:7513654"
FT CARBOHYD 310
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:7513654"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:7513654"
FT DISULFID 71..144
FT /evidence="ECO:0000269|PubMed:7513654"
FT CONFLICT 28
FT /note="T -> Q (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="Q -> P (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 43
FT /note="Q -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 492 AA; 54711 MW; 0755D6FC89B2DF5D CRC64;
MALLWGLLAL ILSCLSSLCS AQFSPVSTME PLDLQLMDGQ AQQKLPPLSL LKLDNQEPGG
QIAPKKAPED CKLSPTPEQT RRLARAMMTF TTDLFSLVAQ SSTRPNLILS PLSVALALSH
LALGAQNQTL QRLKEVLHAD SGPCLPHLLS RLCQDLGPGA FRLAARMYLQ KGFPIKEDFL
EQSEQLFGAK PMSLTGMKGE DLANINRWVK EATEGKIEDF LSDLPDDTVL LLLNAIHFQG
FWRSKFDPNL TQRGAFHLDE QFTVPVDMMQ ALTYPLHWFL LEQPEIQVAH FPFKNNMSFV
VLMPTRFEWN ASQVLANLTW DILHQPSLSE RPTKVQLPKL HLKYQLDLVA TLSQLGLQEL
FQAPDLRGIS DERLVVSSVQ HQSALELSEA GVQAAAATST AMSRMSLSSF IVNRPFLFFI
LEDSTSLPLF VGSVRNPNPG AQPERKEQQD SPDGKDSFQD HKGLPRGDKP FDPDLKLGPP
SEEDYAQPSS PK
