ID   A1AT1_HORSE             Reviewed;          53 AA.
AC   P38028;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   02-JUN-2021, entry version 82.
DE   RecName: Full=Alpha-1-antiproteinase 1;
DE   AltName: Full=Alpha-1-antitrypsin 1;
DE   AltName: Full=Alpha-1-proteinase inhibitor 1;
DE   AltName: Full=SPI1;
DE   Flags: Fragments;
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Plasma;
RX   PubMed=1772402; DOI=10.1007/bf02399689;
RA   Patterson S.D., Bell K., Shaw D.C.;
RT   "The equine major plasma serpin multigene family: partial characterization
RT   including sequence of the reactive-site regions.";
RL   Biochem. Genet. 29:477-499(1991).
RN   [2]
RP   STRUCTURE OF CARBOHYDRATES.
RX   PubMed=2111994;
RA   Patterson S.D., Bell K.;
RT   "The carbohydrate side chains of the major plasma serpins of horse and
RT   wallaby: analyses of enzymatic and chemically treated (including 'Smith
RT   degradation') protein blots by lectin binding.";
RL   Biochem. Int. 20:429-436(1990).
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Plasma.
CC   -!- DOMAIN: The reactive center loop (RCL) extends out from the body of the
CC       protein and directs binding to the target protease. The protease
CC       cleaves the serpin at the reactive site within the RCL, establishing a
CC       covalent linkage between the carboxyl group of the serpin reactive site
CC       and the serine hydroxyl of the protease. The resulting inactive serpin-
CC       protease complex is highly stable (By similarity). {ECO:0000250}.
CC   -!- PTM: N-glycosylated; contains biantennary glycans.
CC   -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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DR   PIR; A61219; A61219.
DR   Proteomes; UP000002281; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
DR   InterPro; IPR023795; Serpin_CS.
DR   InterPro; IPR036186; Serpin_sf.
DR   SUPFAM; SSF56574; SSF56574; 1.
DR   PROSITE; PS00284; SERPIN; 1.
PE   1: Evidence at protein level;
KW   Acute phase; Direct protein sequencing; Glycoprotein; Protease inhibitor;
KW   Reference proteome; Secreted; Serine protease inhibitor.
FT   CHAIN           1..>53
FT                   /note="Alpha-1-antiproteinase 1"
FT                   /id="PRO_0000094092"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            26..27
FT                   /note="Reactive bond"
FT   NON_CONS        21..22
FT                   /evidence="ECO:0000305"
FT   NON_TER         53
SQ   SEQUENCE   53 AA;  5943 MW;  1C3AE978C390AB0B CRC64;
     EDLQGDAVPE TSATKDDNEX PEMIPMSLPP ELEINKPFIL IIYDDNTKSP LFV