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UniProtKB/Swiss-Prot entry P08697


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name A2AP_HUMAN
Primary accession number P08697
Secondary accession numbers Q8N5U7 Q9UCG2 Q9UCG3
Integrated into Swiss-Prot on January 1, 1988
Sequence was last modified on November 1, 1990 (Sequence version 3)
Annotations were last modified on    December 16, 2008 (Entry version 104)
Name and origin of the protein
Protein name Alpha-2-antiplasmin [Precursor]
Synonyms Alpha-2-AP
Alpha-2-plasmin inhibitor
Alpha-2-PI
Gene name
Name: SERPINF2
Synonyms: AAP, PLI
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=2830248 [NCBI, ExPASy, EBI, Israel, Japan]
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].
PubMed=3166140 [NCBI, ExPASy, EBI, Israel, Japan]
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], AND VARIANT VAL-2.
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 4-491.
PubMed=2433286 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[6]
PROTEIN SEQUENCE OF 28-58.
TISSUE=Plasma;
PubMed=8484741 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[7]
PROTEIN SEQUENCE OF 28-52.
TISSUE=Plasma;
DOI=10.1016/0014-5793(92)81419-M; PubMed=1385210 [NCBI, ExPASy, EBI, Israel, Japan]
Christensen S., Sottrup-Jensen L.;
"Bovine alpha 2-antiplasmin. N-terminal and reactive site sequence.";
FEBS Lett. 312:100-104(1992).
[8]
PROTEIN SEQUENCE OF 40-491.
DOI=10.1111/j.1432-1033.1987.tb13551.x; PubMed=2440681 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[9]
PROTEIN SEQUENCE OF 40-43.
DOI=10.1111/j.1432-1033.1977.tb11709.x; PubMed=21075 [NCBI, ExPASy, EBI, Israel, Japan]
Wiman B., Collen D.;
"Purification and characterization of human antiplasmin, the fast-acting plasmin inhibitor in plasma.";
Eur. J. Biochem. 78:19-26(1977).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 218-491.
PubMed=3818581 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[11]
PROTEIN SEQUENCE OF 481-491, AND SULFATION.
PubMed=2434496 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[12]
ACTIVE SITES.
PubMed=2456616 [NCBI, ExPASy, EBI, Israel, Japan]
Potempa J., Shieh B.-H., Travis J.;
"Alpha-2-antiplasmin: a serpin with two separate but overlapping reactive sites.";
Science 241:699-700(1988).
[13]
DISULFIDE BOND.
PubMed=9169621 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[14]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-126; ASN-295 AND ASN-309, AND MASS SPECTROMETRY.
TISSUE=Plasma;
DOI=10.1021/pr0502065; PubMed=16335952 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[15]
VARIANT APLID GLU-176 DEL.
PubMed=2572590 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[16]
VARIANT APLID MET-411, AND VARIANTS VAL-27; TRP-33 AND LYS-434.
DOI=10.1046/j.1365-2141.1999.01708.x; PubMed=10583218 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
  • FUNCTION: The major targets of this inhibitor are plasmin and trypsin, but it also inactivates chymotrypsin.
  • SUBCELLULAR LOCATION: Secreted.
  • TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
  • DISEASE: Defects in SERPINF2 are the cause of alpha-2-plasmin inhibitor deficiency (APLID) [MIM:262850]. APLID is an autosomal recessive disorder resulting in severe hemorrhagic diathesis.
  • SIMILARITY: Belongs to the serpin family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
D00174; BAA00124.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M20786; AAA51554.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M20782; AAA51554.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M20783; AAA51554.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M20784; AAA51554.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M20785; AAA51554.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC031592; AAH31592.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J02654; AAA35543.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D00116; BAA00070.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A31402; ITHUA2.
RefSeq NP_000925.2; -.
UniGene Hs.159509
3D structure databases
HSSP P01008; 1ANT. [HSSP ENTRY / PDB]
ModBase P08697.
Protein family/group databases
MEROPS I04.023; -.
Enzyme and pathway databases
Reactome REACT_604; Hemostasis.
2D gel databases
SWISS-2DPAGE P08697; -.
Organism-specific databases
GeneCards GC17P001593; -.
H-InvDB HIX0013407; -.
HGNC HGNC:9075; SERPINF2.
GenAtlas SERPINF2.
HPA HPA001885; -.
MIM 262850; gene+phenotype. [NCBI / EBI]
PharmGKB PA35522; -.
GeneCards P08697.
Gene expression databases
ArrayExpress P08697; -.
CleanEx HS_SERPINF2; -.
Ontologies
GO
GO:0005576; Cellular component: extracellular region (non-traceable author statement from UniProtKB).
GO:0005634; Cellular component: nucleus (inferred from direct assay from HPA).
GO:0031093; Cellular component: platelet alpha granule lumen (inferred from experiment from Reactome).
GO:0002020; Molecular function: protease binding (inferred from physical interaction from UniProtKB).
GO:0004867; Molecular function: serine-type endopeptidase inhibitor activity (non-traceable author statement from UniProtKB).
GO:0006953; Biological process: acute-phase response (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR000215; Protease_inhib_I4_serpin.
Graphical view of domain structure.
PANTHER PTHR11461; Prot_inh_serpin; 1.
Pfam PF00079; Serpin; 1.
Pfam graphical view of domain structure.
SMART SM00093; SERPIN; 1.
SMART graphical view of domain structure.
PROSITE PS00284; SERPIN; 1.
Proteomics databases
PRIDE P08697; -.
Genome annotation databases
Ensembl ENSG00000167711; Homo sapiens. [Contig view]
GeneID 5345; -.
KEGG hsa:5345; -.
Phylogenomic databases
HOGENOM P08697; -.
HOVERGEN P08697; -.
Other
DrugBank DB00086; Streptokinase.
NextBio 20714; -.
SOURCE SERPINF2; Homo sapiens.
ProtoNet P08697.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acute phase; Direct protein sequencing; Disease mutation; Glycoprotein; Polymorphism; Protease inhibitor; Secreted; Serine protease inhibitor; Signal; Sulfation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    27  27      
PROPEP   28    39  12      PRO_0000032511
CHAIN   40   491  452     Alpha-2-antiplasmin. PRO_0000032512
SITE   403   404  2     Reactive bond for plasmin. 
SITE   404   405  2     Reactive bond for chymotrypsin. 
MOD_RES   484   484        Sulfotyrosine. 
CARBOHYD   126   126        N-linked (GlcNAc...). 
CARBOHYD   295   295        N-linked (GlcNAc...). 
CARBOHYD   309   309        N-linked (GlcNAc...). 
CARBOHYD   316   316        N-linked (GlcNAc...) (Potential). 
DISULFID   70   143         
CROSSLNK   41    41        Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-322 in alpha-fibrinogen). 
VARIANT   2     2  1     A -> V (in dbSNP:rs2070862 [NCBI]). VAR_047951 
VARIANT   27    27  1     A -> V. VAR_013252 
VARIANT   33    33  1     R -> W (in dbSNP:rs2070863 [NCBI]). VAR_013253 
VARIANT   98    98  1     A -> G (in dbSNP:rs36021516 [NCBI]). VAR_051956 
VARIANT   176   176  1     Missing (in APLID; variant Okinawa; probably blocks intracellular transport of alpha-2-plasmin inhibitor). VAR_013254
VARIANT   411   411  1     V -> M (in APLID). VAR_013255 
VARIANT   434   434  1     R -> K (in dbSNP:rs1057335 [NCBI]). VAR_013256 
CONFLICT   49    49        L -> G (in Ref. 8; AA sequence). 
CONFLICT   105   105        N -> D (in Ref. 8; AA sequence). 
CONFLICT   289   289        H -> D (in Ref. 5; AAA35543). 
CONFLICT   408   408        S -> G (in Ref. 8; AA sequence). 
CONFLICT   455   455        D -> N (in Ref. 8; AA sequence). 
Sequence information
Length: 491 AA [This is the length of the unprocessed precursor] Molecular weight: 54566 Da [This is the MW of the unprocessed precursor] CRC64: 385A1C90E91A63CB [This is a checksum on the sequence]
        10         20         30         40         50         60 
MALLWGLLVL SWSCLQGPCS VFSPVSAMEP LGRQLTSGPN QEQVSPLTLL KLGNQEPGGQ 

        70         80         90        100        110        120 
TALKSPPGVC SRDPTPEQTH RLARAMMAFT ADLFSLVAQT STCPNLILSP LSVALALSHL 

       130        140        150        160        170        180 
ALGAQNHTLQ RLQQVLHAGS GPCLPHLLSR LCQDLGPGAF RLAARMYLQK GFPIKEDFLE 

       190        200        210        220        230        240 
QSEQLFGAKP VSLTGKQEDD LANINQWVKE ATEGKIQEFL SGLPEDTVLL LLNAIHFQGF 

       250        260        270        280        290        300 
WRNKFDPSLT QRDSFHLDEQ FTVPVEMMQA RTYPLRWFLL EQPEIQVAHF PFKNNMSFVV 

       310        320        330        340        350        360 
LVPTHFEWNV SQVLANLSWD TLHPPLVWER PTKVRLPKLY LKHQMDLVAT LSQLGLQELF 

       370        380        390        400        410        420 
QAPDLRGISE QSLVVSGVQH QSTLELSEVG VEAAAATSIA MSRMSLSSFS VNRPFLFFIF 

       430        440        450        460        470        480 
EDTTGLPLFV GSVRNPNPSA PRELKEQQDS PGNKDFLQSL KGFPRGDKLF GPDLKLVPPM 

       490 
EEDYPQFGSP K 

P08697 in FASTA format

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