ID A0A091F218_CORBR Unreviewed; 436 AA.
AC A0A091F218;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 22-FEB-2023, entry version 22.
DE SubName: Full=Alpha-2-antiplasmin {ECO:0000313|EMBL:KFO64188.1};
DE Flags: Fragment;
GN ORFNames=N302_16383 {ECO:0000313|EMBL:KFO64188.1};
OS Corvus brachyrhynchos (American crow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Corvoidea; Corvidae;
OC Corvus.
OX NCBI_TaxID=85066 {ECO:0000313|EMBL:KFO64188.1, ECO:0000313|Proteomes:UP000052976};
RN [1] {ECO:0000313|EMBL:KFO64188.1, ECO:0000313|Proteomes:UP000052976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N302 {ECO:0000313|EMBL:KFO64188.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the serpin family.
CC {ECO:0000256|RuleBase:RU000411}.
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DR EMBL; KK719555; KFO64188.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091F218; -.
DR STRING; 85066.A0A091F218; -.
DR MEROPS; I04.023; -.
DR Proteomes; UP000052976; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR GO; GO:0051918; P:negative regulation of fibrinolysis; IEA:InterPro.
DR CDD; cd02053; serpinF2_A2AP; 1.
DR Gene3D; 2.30.39.10; Alpha-1-antitrypsin, domain 1; 1.
DR Gene3D; 3.30.497.10; Antithrombin, subunit I, domain 2; 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:SF20; ALPHA-2-ANTIPLASMIN; 1.
DR PANTHER; PTHR11461; SERINE PROTEASE INHIBITOR, SERPIN; 1.
DR Pfam; PF00079; Serpin; 1.
DR SMART; SM00093; SERPIN; 1.
DR SUPFAM; SSF56574; Serpins; 1.
DR PROSITE; PS00284; SERPIN; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000052976}.
FT DOMAIN 65..409
FT /note="Serpin"
FT /evidence="ECO:0000259|SMART:SM00093"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO64188.1"
FT NON_TER 436
FT /evidence="ECO:0000313|EMBL:KFO64188.1"
SQ SEQUENCE 436 AA; 49107 MW; 2C9E699A037DF92C CRC64;
STLPDTRDDW NSEDEAVAGA GGCRGKKSPE EKASSEEEGE AGDKGCEMTW KKSQRLADGL
MRFSIDLLRE VQLESNRTNV ILSPLSIALA LSHLALGAAN QTEKHLLEVM HLESVPCLHH
MLGTLRRRLT ESTLSLGARL YLQKGFEVKQ KFLEDSEKFY GAKPMTLSGI SQDDLVAINN
WVKEATHGQI PSFLQQLPEN TVMLLLNAVY FHGFWRNKFN ASFTGPDVFH LDHEFVVPVE
MMKAHQYPLS WFTLESQDIQ VAKFPFKSNV SFVVIVPNRY TRNTSHVLEN FPYRQLCRLF
PREVPTTVKI PKIKLDYQLE LNQVLSQMGL QELFTSPNLQ KITEEPLFVS SVQHQATLEL
KEDGVEASAA TSVMLSRSVS VFSLDRPFVF IIFEDETGVP LFIGSVQNPS PDAAPQVREP
QDSSEATDAN EHRMPK
//
