A2AP_HUMAN
ID A2AP_HUMAN Reviewed; 491 AA.
AC P08697; B4E1B7; Q8N5U7; Q9UCG2; Q9UCG3;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 3.
DT 03-AUG-2022, entry version 218.
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=AAP, PLI;
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] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=2830248; DOI=10.1093/oxfordjournals.jbchem.a122141;
RA Tone M., Kikuno R., Kume-Iwaki A., Hashimoto-Gotoh T.;
RT "Structure of human alpha 2-plasmin inhibitor deduced from the cDNA
RT sequence.";
RL J. Biochem. 102:1033-1041(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM 1).
RX PubMed=3166140; DOI=10.1073/pnas.85.18.6836;
RA Hirosawa S., Nakamura Y., Miura O., Sumi Y., Aoki N.;
RT "Organization of the human alpha 2-plasmin inhibitor gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:6836-6840(1988).
RN [3]
RP ERRATUM OF PUBMED:3166140.
RA Hirosawa S., Nakamura Y., Miura O., Sumi Y., Aoki N.;
RL Proc. Natl. Acad. Sci. U.S.A. 86:1612-1613(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Liver;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT VAL-2.
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-491 (ISOFORM 1).
RX PubMed=2433286; DOI=10.1016/s0021-9258(19)75687-7;
RA Holmes W.E., Nelles L., Lijnen H.R., Collen D.;
RT "Primary structure of human alpha 2-antiplasmin, a serine protease
RT inhibitor (serpin).";
RL J. Biol. Chem. 262:1659-1664(1987).
RN [8]
RP PROTEIN SEQUENCE OF 28-58.
RC TISSUE=Plasma;
RX PubMed=8484741; DOI=10.1042/bj2910623;
RA Bangert K., Johnsen A.H., Christensen U., Thorsen S.;
RT "Different N-terminal forms of alpha 2-plasmin inhibitor in human plasma.";
RL Biochem. J. 291:623-625(1993).
RN [9]
RP PROTEIN SEQUENCE OF 28-52.
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).
RN [10]
RP PROTEIN SEQUENCE OF 40-491.
RX PubMed=2440681; DOI=10.1111/j.1432-1033.1987.tb13551.x;
RA Lijnen H.R., Holmes W.E., van Hoef B., Wiman B., Rodriguez H., Collen D.;
RT "Amino-acid sequence of human alpha 2-antiplasmin.";
RL Eur. J. Biochem. 166:565-574(1987).
RN [11]
RP PROTEIN SEQUENCE OF 40-43.
RX PubMed=21075; DOI=10.1111/j.1432-1033.1977.tb11709.x;
RA Wiman B., Collen D.;
RT "Purification and characterization of human antiplasmin, the fast-acting
RT plasmin inhibitor in plasma.";
RL Eur. J. Biochem. 78:19-26(1977).
RN [12]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 218-491.
RX PubMed=3818581; DOI=10.1093/oxfordjournals.jbchem.a121846;
RA Sumi Y., Nakamura Y., Aoki N., Sakai M., Muramatsu M.;
RT "Structure of the carboxyl-terminal half of human alpha 2-plasmin inhibitor
RT deduced from that of cDNA.";
RL J. Biochem. 100:1399-1402(1986).
RN [13]
RP PROTEIN SEQUENCE OF 481-491, AND SULFATION AT TYR-484.
RX PubMed=2434496; DOI=10.1016/s0021-9258(18)61471-1;
RA Hortin G., Fok K.F., Toren P.C., Strauss A.W.;
RT "Sulfation of a tyrosine residue in the plasmin-binding domain of alpha 2-
RT antiplasmin.";
RL J. Biol. Chem. 262:3082-3085(1987).
RN [14]
RP REACTIVE SITES.
RX PubMed=2456616; DOI=10.1126/science.2456616;
RA Potempa J., Shieh B.-H., Travis J.;
RT "Alpha-2-antiplasmin: a serpin with two separate but overlapping reactive
RT sites.";
RL Science 241:699-700(1988).
RN [15]
RP DISULFIDE BOND.
RX PubMed=9169621; DOI=10.1042/bj3230847;
RA Christensen S., Valnickova Z., Thogersen I.B., Olsen E.H., Enghild J.J.;
RT "Assignment of a single disulphide bridge in human alpha2-antiplasmin:
RT implications for the structural and functional properties.";
RL Biochem. J. 323:847-852(1997).
RN [16]
RP CLEAVAGE BY SOLUBLE FAP FORM, AND CLEAVAGE SITE.
RX PubMed=14751930; DOI=10.1182/blood-2003-12-4240;
RA Lee K.N., Jackson K.W., Christiansen V.J., Chung K.H., McKee P.A.;
RT "A novel plasma proteinase potentiates alpha2-antiplasmin inhibition of
RT fibrin digestion.";
RL Blood 103:3783-3788(2004).
RN [17]
RP FUNCTION IN MEMBRANE-ANCHORED SERINE PROTEASE TMPRSS7 INHIBITION, AND
RP HETERODIMER WITH TMPRSS7.
RX PubMed=15853774; DOI=10.1042/bj20050299;
RA Szabo R., Netzel-Arnett S., Hobson J.P., Antalis T.M., Bugge T.H.;
RT "Matriptase-3 is a novel phylogenetically preserved membrane-anchored
RT serine protease with broad serpin reactivity.";
RL Biochem. J. 390:231-242(2005).
RN [18]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-126; ASN-295 AND ASN-309.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [19]
RP CLEAVAGE BY PLASMA MEMBRANE AND SOLUBLE FAP FORMS, AND CLEAVAGE SITE.
RX PubMed=16223769; DOI=10.1182/blood-2005-08-3452;
RA Lee K.N., Jackson K.W., Christiansen V.J., Lee C.S., Chun J.G., McKee P.A.;
RT "Antiplasmin-cleaving enzyme is a soluble form of fibroblast activation
RT protein.";
RL Blood 107:1397-1404(2006).
RN [20]
RP VARIANT APLID GLU-176 DEL.
RX PubMed=2572590; DOI=10.1016/s0021-9258(19)84699-9;
RA Miura O., Sugahara Y., Aoki N.;
RT "Hereditary alpha 2-plasmin inhibitor deficiency caused by a transport-
RT deficient mutation (alpha 2-PI-Okinawa). Deletion of Glu137 by a
RT trinucleotide deletion blocks intracellular transport.";
RL J. Biol. Chem. 264:18213-18219(1989).
RN [21]
RP VARIANT APLID MET-411, AND VARIANTS VAL-27; TRP-33 AND LYS-434.
RX PubMed=10583218; DOI=10.1046/j.1365-2141.1999.01708.x;
RA Lind B., Thorsen S.;
RT "A novel missense mutation in the human plasmin inhibitor (alpha2-
RT antiplasmin) gene associated with a bleeding tendency.";
RL Br. J. Haematol. 107:317-322(1999).
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. {ECO:0000269|PubMed:15853774}.
CC -!- SUBUNIT: Forms protease inhibiting heterodimer with TMPRSS7.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P08697-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P08697-2; Sequence=VSP_043833, VSP_043834;
CC -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
CC -!- PTM: Proteolytically cleaved at Pro-39 by both the prolyl endopeptidase
CC FAP form and antiplasmin-cleaving enzyme FAP soluble form to generate
CC mature alpha-2-antiplasmin. {ECO:0000269|PubMed:14751930,
CC ECO:0000269|PubMed:16223769}.
CC -!- DISEASE: Alpha-2-plasmin inhibitor deficiency (APLID) [MIM:262850]: An
CC autosomal recessive disorder resulting in severe hemorrhagic diathesis.
CC {ECO:0000269|PubMed:10583218, ECO:0000269|PubMed:2572590}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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DR EMBL; D00174; BAA00124.1; -; mRNA.
DR EMBL; M20786; AAA51554.1; -; Genomic_DNA.
DR EMBL; M20782; AAA51554.1; JOINED; Genomic_DNA.
DR EMBL; M20783; AAA51554.1; JOINED; Genomic_DNA.
DR EMBL; M20784; AAA51554.1; JOINED; Genomic_DNA.
DR EMBL; M20785; AAA51554.1; JOINED; Genomic_DNA.
DR EMBL; AK303763; BAG64729.1; -; mRNA.
DR EMBL; AC130343; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC031592; AAH31592.1; -; mRNA.
DR EMBL; J02654; AAA35543.1; -; mRNA.
DR EMBL; D00116; BAA00070.1; -; mRNA.
DR CCDS; CCDS11011.1; -. [P08697-1]
DR CCDS; CCDS54064.1; -. [P08697-2]
DR PIR; A31402; ITHUA2.
DR RefSeq; NP_000925.2; NM_000934.3. [P08697-1]
DR RefSeq; NP_001159392.1; NM_001165920.1. [P08697-1]
DR RefSeq; NP_001159393.1; NM_001165921.1. [P08697-2]
DR AlphaFoldDB; P08697; -.
DR SMR; P08697; -.
DR BioGRID; 111360; 33.
DR IntAct; P08697; 2.
DR STRING; 9606.ENSP00000321853; -.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB08888; Ocriplasmin.
DR MEROPS; I04.023; -.
DR GlyConnect; 1002; 2 N-Linked glycans (1 site).
DR GlyGen; P08697; 8 sites, 4 N-linked glycans (1 site), 3 O-linked glycans (4 sites).
DR iPTMnet; P08697; -.
DR PhosphoSitePlus; P08697; -.
DR BioMuta; SERPINF2; -.
DR DMDM; 112907; -.
DR SWISS-2DPAGE; P08697; -.
DR CPTAC; non-CPTAC-1065; -.
DR jPOST; P08697; -.
DR MassIVE; P08697; -.
DR MaxQB; P08697; -.
DR PaxDb; P08697; -.
DR PeptideAtlas; P08697; -.
DR PRIDE; P08697; -.
DR ProteomicsDB; 52156; -. [P08697-1]
DR ProteomicsDB; 52157; -. [P08697-2]
DR Antibodypedia; 852; 562 antibodies from 39 providers.
DR DNASU; 5345; -.
DR Ensembl; ENST00000324015.7; ENSP00000321853.3; ENSG00000167711.14. [P08697-1]
DR Ensembl; ENST00000382061.5; ENSP00000371493.4; ENSG00000167711.14. [P08697-1]
DR Ensembl; ENST00000450523.6; ENSP00000403877.2; ENSG00000167711.14. [P08697-2]
DR Ensembl; ENST00000453066.6; ENSP00000402286.2; ENSG00000167711.14. [P08697-1]
DR Ensembl; ENST00000618883.3; ENSP00000479005.1; ENSG00000276838.4.
DR Ensembl; ENST00000622842.2; ENSP00000481874.1; ENSG00000276838.4.
DR GeneID; 5345; -.
DR KEGG; hsa:5345; -.
DR MANE-Select; ENST00000453066.6; ENSP00000402286.2; NM_000934.4; NP_000925.2.
DR UCSC; uc002ftk.1; human. [P08697-1]
DR CTD; 5345; -.
DR DisGeNET; 5345; -.
DR GeneCards; SERPINF2; -.
DR HGNC; HGNC:9075; SERPINF2.
DR HPA; ENSG00000167711; Tissue enriched (liver).
DR MalaCards; SERPINF2; -.
DR MIM; 262850; phenotype.
DR MIM; 613168; gene.
DR neXtProt; NX_P08697; -.
DR OpenTargets; ENSG00000167711; -.
DR Orphanet; 79; Congenital alpha2-antiplasmin deficiency.
DR PharmGKB; PA35522; -.
DR VEuPathDB; HostDB:ENSG00000167711; -.
DR eggNOG; KOG2392; Eukaryota.
DR GeneTree; ENSGT00940000158386; -.
DR HOGENOM; CLU_023330_3_2_1; -.
DR InParanoid; P08697; -.
DR OMA; EMTWKKS; -.
DR OrthoDB; 1124079at2759; -.
DR PhylomeDB; P08697; -.
DR TreeFam; TF317350; -.
DR PathwayCommons; P08697; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR Reactome; R-HSA-75205; Dissolution of Fibrin Clot.
DR SignaLink; P08697; -.
DR BioGRID-ORCS; 5345; 8 hits in 1068 CRISPR screens.
DR ChiTaRS; SERPINF2; human.
DR GeneWiki; Alpha_2-antiplasmin; -.
DR GenomeRNAi; 5345; -.
DR Pharos; P08697; Tbio.
DR PRO; PR:P08697; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P08697; protein.
DR Bgee; ENSG00000167711; Expressed in right lobe of liver and 94 other tissues.
DR ExpressionAtlas; P08697; baseline and differential.
DR Genevisible; P08697; HS.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR GO; GO:0005577; C:fibrinogen complex; IDA:BHF-UCL.
DR GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; TAS:ProtInc.
DR GO; GO:0002020; F:protease binding; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:BHF-UCL.
DR GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
DR GO; GO:0048514; P:blood vessel morphogenesis; ISS:BHF-UCL.
DR GO; GO:0030199; P:collagen fibril organization; ISS:BHF-UCL.
DR GO; GO:0042730; P:fibrinolysis; TAS:Reactome.
DR GO; GO:0002034; P:maintenance of blood vessel diameter homeostasis by renin-angiotensin; ISS:BHF-UCL.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
DR GO; GO:0051918; P:negative regulation of fibrinolysis; IDA:BHF-UCL.
DR GO; GO:0010757; P:negative regulation of plasminogen activation; IDA:BHF-UCL.
DR GO; GO:0045597; P:positive regulation of cell differentiation; IDA:BHF-UCL.
DR GO; GO:2000049; P:positive regulation of cell-cell adhesion mediated by cadherin; TAS:BHF-UCL.
DR GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:BHF-UCL.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IDA:BHF-UCL.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISS:BHF-UCL.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IDA:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0071636; P:positive regulation of transforming growth factor beta production; IDA: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 Acute phase; Alternative splicing; Direct protein sequencing;
KW Disease variant; Disulfide bond; Glycoprotein; Isopeptide bond;
KW Protease inhibitor; Reference proteome; Secreted;
KW Serine protease inhibitor; Signal; Sulfation.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|PubMed:1385210,
FT ECO:0000269|PubMed:8484741"
FT PROPEP 28..39
FT /evidence="ECO:0000269|PubMed:14751930,
FT ECO:0000269|PubMed:16223769, ECO:0000269|PubMed:21075,
FT ECO:0000269|PubMed:2440681"
FT /id="PRO_0000032511"
FT CHAIN 40..491
FT /note="Alpha-2-antiplasmin"
FT /id="PRO_0000032512"
FT REGION 55..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..455
FT /note="Polar residues"
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:0000269|PubMed:14751930,
FT ECO:0000269|PubMed:16223769"
FT SITE 403..404
FT /note="Reactive bond for plasmin"
FT SITE 404..405
FT /note="Reactive bond for chymotrypsin"
FT MOD_RES 484
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000269|PubMed:2434496"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 70..143
FT /evidence="ECO:0000269|PubMed:9169621"
FT CROSSLNK 41
FT /note="Isoglutamyl lysine isopeptide (Gln-Lys) (interchain
FT with K-322 in alpha-fibrinogen)"
FT VAR_SEQ 56..119
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043833"
FT VAR_SEQ 120..122
FT /note="LAL -> VQP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043834"
FT VARIANT 2
FT /note="A -> V (in dbSNP:rs2070862)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_047951"
FT VARIANT 27
FT /note="A -> V"
FT /evidence="ECO:0000269|PubMed:10583218"
FT /id="VAR_013252"
FT VARIANT 33
FT /note="R -> W (in dbSNP:rs2070863)"
FT /evidence="ECO:0000269|PubMed:10583218"
FT /id="VAR_013253"
FT VARIANT 98
FT /note="A -> G (in dbSNP:rs36021516)"
FT /id="VAR_051956"
FT VARIANT 176
FT /note="Missing (in APLID; variant Okinawa; probably blocks
FT intracellular transport of alpha-2-plasmin inhibitor)"
FT /evidence="ECO:0000269|PubMed:2572590"
FT /id="VAR_013254"
FT VARIANT 411
FT /note="V -> M (in APLID; dbSNP:rs121965062)"
FT /evidence="ECO:0000269|PubMed:10583218"
FT /id="VAR_013255"
FT VARIANT 434
FT /note="R -> K (in dbSNP:rs1057335)"
FT /evidence="ECO:0000269|PubMed:10583218"
FT /id="VAR_013256"
FT VARIANT 451
FT /note="P -> S (in dbSNP:rs57360598)"
FT /id="VAR_061792"
FT CONFLICT 49
FT /note="L -> G (in Ref. 10; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="N -> D (in Ref. 10; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="H -> D (in Ref. 7; AAA35543)"
FT /evidence="ECO:0000305"
FT CONFLICT 408
FT /note="S -> G (in Ref. 10; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 455
FT /note="D -> N (in Ref. 10; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 491 AA; 54566 MW; 385A1C90E91A63CB CRC64;
MALLWGLLVL SWSCLQGPCS VFSPVSAMEP LGRQLTSGPN QEQVSPLTLL KLGNQEPGGQ
TALKSPPGVC SRDPTPEQTH RLARAMMAFT ADLFSLVAQT STCPNLILSP LSVALALSHL
ALGAQNHTLQ RLQQVLHAGS GPCLPHLLSR LCQDLGPGAF RLAARMYLQK GFPIKEDFLE
QSEQLFGAKP VSLTGKQEDD LANINQWVKE ATEGKIQEFL SGLPEDTVLL LLNAIHFQGF
WRNKFDPSLT QRDSFHLDEQ FTVPVEMMQA RTYPLRWFLL EQPEIQVAHF PFKNNMSFVV
LVPTHFEWNV SQVLANLSWD TLHPPLVWER PTKVRLPKLY LKHQMDLVAT LSQLGLQELF
QAPDLRGISE QSLVVSGVQH QSTLELSEVG VEAAAATSIA MSRMSLSSFS VNRPFLFFIF
EDTTGLPLFV GSVRNPNPSA PRELKEQQDS PGNKDFLQSL KGFPRGDKLF GPDLKLVPPM
EEDYPQFGSP K
