ID   A1AT_CHILA              Reviewed;          30 AA.
AC   P38026;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Alpha-1-antiproteinase;
DE   AltName: Full=Alpha-1-antitrypsin;
DE   AltName: Full=Alpha-1-proteinase inhibitor;
DE   Flags: Fragment;
OS   Chinchilla lanigera (Long-tailed chinchilla) (Chinchilla villidera).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha;
OC   Chinchillidae; Chinchilla.
OX   NCBI_TaxID=34839;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Plasma;
RX   PubMed=2184987; DOI=10.1016/0305-0491(90)90245-o;
RA   Diven W.F., Vietmeier B., Hempel J., Chambers J.;
RT   "Purification and N-terminal characterization of Chinchilla villidera
RT   alpha-1-antitrypsin.";
RL   Comp. Biochem. Physiol. 95B:39-44(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 bi- and triantennary glycans.
CC   -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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DR   Proteomes; UP000694398; 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.
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..>30
FT                   /note="Alpha-1-antiproteinase"
FT                   /id="PRO_0000094091"
FT   NON_TER         30
SQ   SEQUENCE   30 AA;  3411 MW;  C590F933E9B1E5DE CRC64;
     EDAQVTDLPD HEQEHLAXHK IAPXLAEFAY