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Alpha-2-antiplasmin (Alpha-2-AP) (Alpha-2-plasmin inhibitor) (Alpha-2-PI) (Serpin F2)

 A2AP_HUMAN              Reviewed;         491 AA.
P08697; B4E1B7; Q8N5U7; Q9UCG2; Q9UCG3;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
01-NOV-1990, sequence version 3.
10-OCT-2018, entry version 196.
RecName: Full=Alpha-2-antiplasmin;
Short=Alpha-2-AP;
AltName: Full=Alpha-2-plasmin inhibitor;
Short=Alpha-2-PI;
AltName: Full=Serpin F2;
Flags: Precursor;
Name=SERPINF2; Synonyms=AAP, PLI;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
PubMed=2830248;
Tone M., Kikuno R., Kume-Iwaki A., Hashimoto-Gotoh T.;
"Structure of human alpha 2-plasmin inhibitor deduced from the cDNA
sequence.";
J. Biochem. 102:1033-1041(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM
1).
PubMed=3166140; DOI=10.1073/pnas.85.18.6836;
Hirosawa S., Nakamura Y., Miura O., Sumi Y., Aoki N.;
"Organization of the human alpha 2-plasmin inhibitor gene.";
Proc. Natl. Acad. Sci. U.S.A. 85:6836-6840(1988).
[3]
ERRATUM.
Hirosawa S., Nakamura Y., Miura O., Sumi Y., Aoki N.;
Proc. Natl. Acad. Sci. U.S.A. 86:1612-1613(1989).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Liver;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT VAL-2.
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 4-491 (ISOFORM 1).
PubMed=2433286;
Holmes W.E., Nelles L., Lijnen H.R., Collen D.;
"Primary structure of human alpha 2-antiplasmin, a serine protease
inhibitor (serpin).";
J. Biol. Chem. 262:1659-1664(1987).
[8]
PROTEIN SEQUENCE OF 28-58.
TISSUE=Plasma;
PubMed=8484741; DOI=10.1042/bj2910623;
Bangert K., Johnsen A.H., Christensen U., Thorsen S.;
"Different N-terminal forms of alpha 2-plasmin inhibitor in human
plasma.";
Biochem. J. 291:623-625(1993).
[9]
PROTEIN SEQUENCE OF 28-52.
TISSUE=Plasma;
PubMed=1385210; DOI=10.1016/0014-5793(92)81419-M;
Christensen S., Sottrup-Jensen L.;
"Bovine alpha 2-antiplasmin. N-terminal and reactive site sequence.";
FEBS Lett. 312:100-104(1992).
[10]
PROTEIN SEQUENCE OF 40-491.
PubMed=2440681; DOI=10.1111/j.1432-1033.1987.tb13551.x;
Lijnen H.R., Holmes W.E., van Hoef B., Wiman B., Rodriguez H.,
Collen D.;
"Amino-acid sequence of human alpha 2-antiplasmin.";
Eur. J. Biochem. 166:565-574(1987).
[11]
PROTEIN SEQUENCE OF 40-43.
PubMed=21075; DOI=10.1111/j.1432-1033.1977.tb11709.x;
Wiman B., Collen D.;
"Purification and characterization of human antiplasmin, the fast-
acting plasmin inhibitor in plasma.";
Eur. J. Biochem. 78:19-26(1977).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 218-491.
PubMed=3818581;
Sumi Y., Nakamura Y., Aoki N., Sakai M., Muramatsu M.;
"Structure of the carboxyl-terminal half of human alpha 2-plasmin
inhibitor deduced from that of cDNA.";
J. Biochem. 100:1399-1402(1986).
[13]
PROTEIN SEQUENCE OF 481-491, AND SULFATION AT TYR-484.
PubMed=2434496;
Hortin G., Fok K.F., Toren P.C., Strauss A.W.;
"Sulfation of a tyrosine residue in the plasmin-binding domain of
alpha 2-antiplasmin.";
J. Biol. Chem. 262:3082-3085(1987).
[14]
REACTIVE SITES.
PubMed=2456616; DOI=10.1126/science.2456616;
Potempa J., Shieh B.-H., Travis J.;
"Alpha-2-antiplasmin: a serpin with two separate but overlapping
reactive sites.";
Science 241:699-700(1988).
[15]
DISULFIDE BOND.
PubMed=9169621; DOI=10.1042/bj3230847;
Christensen S., Valnickova Z., Thogersen I.B., Olsen E.H.,
Enghild J.J.;
"Assignment of a single disulphide bridge in human alpha2-antiplasmin:
implications for the structural and functional properties.";
Biochem. J. 323:847-852(1997).
[16]
CLEAVAGE BY SOLUBLE FAP FORM, AND CLEAVAGE SITE.
PubMed=14751930; DOI=10.1182/blood-2003-12-4240;
Lee K.N., Jackson K.W., Christiansen V.J., Chung K.H., McKee P.A.;
"A novel plasma proteinase potentiates alpha2-antiplasmin inhibition
of fibrin digestion.";
Blood 103:3783-3788(2004).
[17]
FUNCTION IN MEMBRANE-ANCHORED SERINE PROTEASE TMPRSS7 INHIBITION, AND
HETERODIMER WITH TMPRSS7.
PubMed=15853774; DOI=10.1042/BJ20050299;
Szabo R., Netzel-Arnett S., Hobson J.P., Antalis T.M., Bugge T.H.;
"Matriptase-3 is a novel phylogenetically preserved membrane-anchored
serine protease with broad serpin reactivity.";
Biochem. J. 390:231-242(2005).
[18]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-126; ASN-295 AND ASN-309.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[19]
CLEAVAGE BY PLASMA MEMBRANE AND SOLUBLE FAP FORMS, AND CLEAVAGE SITE.
PubMed=16223769; DOI=10.1182/blood-2005-08-3452;
Lee K.N., Jackson K.W., Christiansen V.J., Lee C.S., Chun J.G.,
McKee P.A.;
"Antiplasmin-cleaving enzyme is a soluble form of fibroblast
activation protein.";
Blood 107:1397-1404(2006).
[20]
VARIANT APLID GLU-176 DEL.
PubMed=2572590;
Miura O., Sugahara Y., Aoki N.;
"Hereditary alpha 2-plasmin inhibitor deficiency caused by a
transport-deficient mutation (alpha 2-PI-Okinawa). Deletion of Glu137
by a trinucleotide deletion blocks intracellular transport.";
J. Biol. Chem. 264:18213-18219(1989).
[21]
VARIANT APLID MET-411, AND VARIANTS VAL-27; TRP-33 AND LYS-434.
PubMed=10583218; DOI=10.1046/j.1365-2141.1999.01708.x;
Lind B., Thorsen S.;
"A novel missense mutation in the human plasmin inhibitor (alpha2-
antiplasmin) gene associated with a bleeding tendency.";
Br. J. Haematol. 107:317-322(1999).
-!- FUNCTION: Serine protease inhibitor. The major targets of this
inhibitor are plasmin and trypsin, but it also inactivates
matriptase-3/TMPRSS7 and chymotrypsin.
{ECO:0000269|PubMed:15853774}.
-!- SUBUNIT: Forms protease inhibiting heterodimer with TMPRSS7.
-!- SUBCELLULAR LOCATION: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P08697-1; Sequence=Displayed;
Name=2;
IsoId=P08697-2; Sequence=VSP_043833, VSP_043834;
-!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
-!- PTM: Proteolytically cleaved at Pro-39 by both the prolyl
endopeptidase FAP form and antiplasmin-cleaving enzyme FAP soluble
form to generate mature alpha-2-antiplasmin.
{ECO:0000269|PubMed:14751930, ECO:0000269|PubMed:16223769}.
-!- DISEASE: Alpha-2-plasmin inhibitor deficiency (APLID)
[MIM:262850]: An autosomal recessive disorder resulting in severe
hemorrhagic diathesis. {ECO:0000269|PubMed:10583218,
ECO:0000269|PubMed:2572590}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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EMBL; D00174; BAA00124.1; -; mRNA.
EMBL; M20786; AAA51554.1; -; Genomic_DNA.
EMBL; M20782; AAA51554.1; JOINED; Genomic_DNA.
EMBL; M20783; AAA51554.1; JOINED; Genomic_DNA.
EMBL; M20784; AAA51554.1; JOINED; Genomic_DNA.
EMBL; M20785; AAA51554.1; JOINED; Genomic_DNA.
EMBL; AK303763; BAG64729.1; -; mRNA.
EMBL; AC130343; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC031592; AAH31592.1; -; mRNA.
EMBL; J02654; AAA35543.1; -; mRNA.
EMBL; D00116; BAA00070.1; -; mRNA.
CCDS; CCDS11011.1; -. [P08697-1]
CCDS; CCDS54064.1; -. [P08697-2]
PIR; A31402; ITHUA2.
RefSeq; NP_000925.2; NM_000934.3. [P08697-1]
RefSeq; NP_001159392.1; NM_001165920.1. [P08697-1]
RefSeq; NP_001159393.1; NM_001165921.1. [P08697-2]
UniGene; Hs.159509; -.
ProteinModelPortal; P08697; -.
SMR; P08697; -.
BioGrid; 111360; 10.
IntAct; P08697; 2.
STRING; 9606.ENSP00000321853; -.
DrugBank; DB08888; Ocriplasmin.
MEROPS; I04.023; -.
GlyConnect; 1002; -.
iPTMnet; P08697; -.
PhosphoSitePlus; P08697; -.
BioMuta; SERPINF2; -.
DMDM; 112907; -.
SWISS-2DPAGE; P08697; -.
MaxQB; P08697; -.
PaxDb; P08697; -.
PeptideAtlas; P08697; -.
PRIDE; P08697; -.
ProteomicsDB; 52156; -.
ProteomicsDB; 52157; -. [P08697-2]
DNASU; 5345; -.
Ensembl; ENST00000324015; ENSP00000321853; ENSG00000167711. [P08697-1]
Ensembl; ENST00000382061; ENSP00000371493; ENSG00000167711. [P08697-1]
Ensembl; ENST00000450523; ENSP00000403877; ENSG00000167711. [P08697-2]
Ensembl; ENST00000618883; ENSP00000479005; ENSG00000276838.
Ensembl; ENST00000622842; ENSP00000481874; ENSG00000276838.
GeneID; 5345; -.
KEGG; hsa:5345; -.
UCSC; uc002ftk.1; human. [P08697-1]
CTD; 5345; -.
DisGeNET; 5345; -.
EuPathDB; HostDB:ENSG00000167711.13; -.
GeneCards; SERPINF2; -.
H-InvDB; HIX0013407; -.
HGNC; HGNC:9075; SERPINF2.
HPA; CAB024863; -.
HPA; HPA001885; -.
MalaCards; SERPINF2; -.
MIM; 262850; phenotype.
MIM; 613168; gene.
neXtProt; NX_P08697; -.
OpenTargets; ENSG00000167711; -.
Orphanet; 79; Congenital alpha2 antiplasmin deficiency.
PharmGKB; PA35522; -.
eggNOG; KOG2392; Eukaryota.
eggNOG; COG4826; LUCA.
GeneTree; ENSGT00920000149046; -.
HOGENOM; HOG000231761; -.
HOVERGEN; HBG000043; -.
InParanoid; P08697; -.
KO; K03983; -.
OMA; WRSKFDP; -.
OrthoDB; EOG091G066U; -.
PhylomeDB; P08697; -.
TreeFam; TF317350; -.
Reactome; R-HSA-114608; Platelet degranulation.
Reactome; R-HSA-75205; Dissolution of Fibrin Clot.
ChiTaRS; SERPINF2; human.
GeneWiki; Alpha_2-antiplasmin; -.
GenomeRNAi; 5345; -.
PMAP-CutDB; P08697; -.
PRO; PR:P08697; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000167711; Expressed in 108 organ(s), highest expression level in right lobe of liver.
CleanEx; HS_SERPINF2; -.
ExpressionAtlas; P08697; baseline and differential.
Genevisible; P08697; HS.
GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005577; C:fibrinogen complex; IDA:BHF-UCL.
GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
GO; GO:0004866; F:endopeptidase inhibitor activity; TAS:ProtInc.
GO; GO:0002020; F:protease binding; IPI:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL.
GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:BHF-UCL.
GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
GO; GO:0048514; P:blood vessel morphogenesis; ISS:BHF-UCL.
GO; GO:0030199; P:collagen fibril organization; ISS:BHF-UCL.
GO; GO:0042730; P:fibrinolysis; TAS:Reactome.
GO; GO:0051918; P:negative regulation of fibrinolysis; IDA:BHF-UCL.
GO; GO:0010757; P:negative regulation of plasminogen activation; IDA:BHF-UCL.
GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
GO; GO:0045597; P:positive regulation of cell differentiation; IDA:BHF-UCL.
GO; GO:2000049; P:positive regulation of cell-cell adhesion mediated by cadherin; TAS:BHF-UCL.
GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IDA:BHF-UCL.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:BHF-UCL.
GO; GO:0046330; P:positive regulation of JNK cascade; IDA:BHF-UCL.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISS:BHF-UCL.
GO; GO:0051496; P:positive regulation of stress fiber assembly; IDA:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
GO; GO:0071636; P:positive regulation of transforming growth factor beta production; IDA:BHF-UCL.
GO; GO:0002034; P:regulation of blood vessel diameter by renin-angiotensin; ISS:BHF-UCL.
GO; GO:0010033; P:response to organic substance; IEA:Ensembl.
CDD; cd02053; alpha2AP; 1.
InterPro; IPR033833; Alpha2AP.
InterPro; IPR023795; Serpin_CS.
InterPro; IPR023796; Serpin_dom.
InterPro; IPR000215; Serpin_fam.
InterPro; IPR036186; Serpin_sf.
PANTHER; PTHR11461; PTHR11461; 1.
Pfam; PF00079; Serpin; 1.
SMART; SM00093; SERPIN; 1.
SUPFAM; SSF56574; SSF56574; 1.
PROSITE; PS00284; SERPIN; 1.
1: Evidence at protein level;
Acute phase; Alternative splicing; Complete proteome;
Direct protein sequencing; Disease mutation; Disulfide bond;
Glycoprotein; Isopeptide bond; Polymorphism; Protease inhibitor;
Reference proteome; Secreted; Serine protease inhibitor; Signal;
Sulfation.
SIGNAL 1 27 {ECO:0000269|PubMed:1385210,
ECO:0000269|PubMed:8484741}.
PROPEP 28 39 {ECO:0000269|PubMed:14751930,
ECO:0000269|PubMed:16223769,
ECO:0000269|PubMed:21075,
ECO:0000269|PubMed:2440681}.
/FTId=PRO_0000032511.
CHAIN 40 491 Alpha-2-antiplasmin.
/FTId=PRO_0000032512.
SITE 39 40 Cleavage; by prolyl endopeptidase FAP,
antiplasmin-cleaving enzyme FAP soluble
form. {ECO:0000269|PubMed:14751930,
ECO:0000269|PubMed:16223769}.
SITE 403 404 Reactive bond for plasmin.
SITE 404 405 Reactive bond for chymotrypsin.
MOD_RES 484 484 Sulfotyrosine.
{ECO:0000269|PubMed:2434496}.
CARBOHYD 126 126 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
CARBOHYD 295 295 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
CARBOHYD 309 309 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
CARBOHYD 316 316 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 70 143 {ECO:0000269|PubMed:9169621}.
CROSSLNK 41 41 Isoglutamyl lysine isopeptide (Gln-Lys)
(interchain with K-322 in alpha-
fibrinogen).
VAR_SEQ 56 119 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043833.
VAR_SEQ 120 122 LAL -> VQP (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043834.
VARIANT 2 2 A -> V (in dbSNP:rs2070862).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_047951.
VARIANT 27 27 A -> V. {ECO:0000269|PubMed:10583218}.
/FTId=VAR_013252.
VARIANT 33 33 R -> W (in dbSNP:rs2070863).
{ECO:0000269|PubMed:10583218}.
/FTId=VAR_013253.
VARIANT 98 98 A -> G (in dbSNP:rs36021516).
/FTId=VAR_051956.
VARIANT 176 176 Missing (in APLID; variant Okinawa;
probably blocks intracellular transport
of alpha-2-plasmin inhibitor).
{ECO:0000269|PubMed:2572590}.
/FTId=VAR_013254.
VARIANT 411 411 V -> M (in APLID; dbSNP:rs121965062).
{ECO:0000269|PubMed:10583218}.
/FTId=VAR_013255.
VARIANT 434 434 R -> K (in dbSNP:rs1057335).
{ECO:0000269|PubMed:10583218}.
/FTId=VAR_013256.
VARIANT 451 451 P -> S (in dbSNP:rs57360598).
/FTId=VAR_061792.
CONFLICT 49 49 L -> G (in Ref. 10; AA sequence).
{ECO:0000305}.
CONFLICT 105 105 N -> D (in Ref. 10; AA sequence).
{ECO:0000305}.
CONFLICT 289 289 H -> D (in Ref. 7; AAA35543).
{ECO:0000305}.
CONFLICT 408 408 S -> G (in Ref. 10; AA sequence).
{ECO:0000305}.
CONFLICT 455 455 D -> N (in Ref. 10; AA sequence).
{ECO:0000305}.
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


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