ID   A1AT_DIDVI              Reviewed;         410 AA.
AC   Q03044;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Alpha-1-antiproteinase;
DE   AltName: Full=Alpha-1-antitrypsin;
DE   AltName: Full=Alpha-1-proteinase inhibitor;
DE   Flags: Precursor;
OS   Didelphis virginiana (North American opossum) (Didelphis marsupialis
OS   virginiana).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Didelphimorphia; Didelphidae; Didelphis.
OX   NCBI_TaxID=9267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 22-37 AND 127-146.
RC   TISSUE=Liver;
RX   PubMed=8422360; DOI=10.1021/bi00053a015;
RA   Catanese J.J., Kress L.F.;
RT   "Opossum serum alpha 1-proteinase inhibitor: purification, linear sequence,
RT   and resistance to inactivation by rattlesnake venom metalloproteinases.";
RL   Biochemistry 32:509-515(1993).
CC   -!- FUNCTION: Inhibitor of serine proteases. The primary target is
CC       elastase, but also has a moderate affinity for plasmin and thrombin.
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   -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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DR   EMBL; Z18906; CAA79343.1; -; mRNA.
DR   EMBL; L06824; AAC02630.1; -; mRNA.
DR   PIR; A45457; A45457.
DR   AlphaFoldDB; Q03044; -.
DR   SMR; Q03044; -.
DR   MEROPS; I04.001; -.
DR   PRIDE; Q03044; -.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
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   Gene3D; 2.30.39.10; -; 1.
DR   Gene3D; 3.30.497.10; -; 1.
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; PTHR11461; 1.
DR   Pfam; PF00079; Serpin; 1.
DR   SMART; SM00093; SERPIN; 1.
DR   SUPFAM; SSF56574; SSF56574; 1.
PE   1: Evidence at protein level;
KW   Acute phase; Direct protein sequencing; Glycoprotein; Phosphoprotein;
KW   Protease inhibitor; Secreted; Serine protease inhibitor; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|PubMed:8422360"
FT   CHAIN           22..410
FT                   /note="Alpha-1-antiproteinase"
FT                   /id="PRO_0000032384"
FT   REGION          365..384
FT                   /note="RCL"
FT   SITE            374..375
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         375
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P01009"
FT   CARBOHYD        63
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        100
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        264
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   410 AA;  46441 MW;  2A6718C1B2FAA389 CRC64;
     MMPSTLSLCL MLAGLCSLVT SHLTEEIQAS NDTENEYSST RRISPYMTDF SIDFYRLLVS
     KSNTTNIFFS PISIYTAFTL LALGAKSATR DQILTGLRFN RTEISEEHIF EGFQQLLNTF
     NLPENELQLT TSNGLFIDKN LKLVAKFLED SKRLYASDTF STNFEDNMAA KKQINDYVEK
     ETQGKIVDLI QNLDSNVVFV LVNCIFFKGK WEKPFMTELT TECPFHVDSK TTVPVQTMRR
     LGMFNVFYDQ DLSCWVLKMK YMGNATALFI LPDTGKIEKV ENALNKMLFH KWTRNLKRRA
     ISLYFPKVSI SGNYDLKILR ELGITDVFGS NADLSGITEE TNLKLSQAVH KAVVNIDEKG
     TEASGATFAE GIPMSIPPTV EFLRPFIFII LEENTKSVLF MGKVMNPTGN