ID   A1AT_PIG                Reviewed;         421 AA.
AC   P50447;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=Alpha-1-antitrypsin;
DE   AltName: Full=Alpha-1 protease inhibitor;
DE   AltName: Full=Alpha-1-antiproteinase;
DE   AltName: Full=Serpin A1;
DE   Flags: Precursor;
GN   Name=SERPINA1; Synonyms=PI;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=8856896; DOI=10.1111/j.1365-2052.1996.tb00472.x;
RA   Archibald A.L., Couperwhite S., Mellink C.H.M., Lahbib-Mansais Y.,
RA   Gellin J.;
RT   "Porcine alpha-1-antitrypsin (PI): cDNA sequence, polymorphism and
RT   assignment to chromosome 7q2.4-q2.6.";
RL   Anim. Genet. 27:85-89(1996).
CC   -!- FUNCTION: Inhibitor of serine proteases. Its primary target is
CC       elastase, but it also has a moderate affinity for plasmin and thrombin
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with CELA2A (By similarity). Interacts with ERGIC3
CC       and LMAN1/ERGIC53 (By similarity). Interacts with PRSS1/Trypsin (By
CC       similarity). {ECO:0000250|UniProtKB:P01009}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
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; X88780; CAA61259.1; -; mRNA.
DR   RefSeq; NP_999560.1; NM_214395.1.
DR   AlphaFoldDB; P50447; -.
DR   SMR; P50447; -.
DR   STRING; 9823.ENSSSCP00000002681; -.
DR   MEROPS; I04.001; -.
DR   PaxDb; P50447; -.
DR   PeptideAtlas; P50447; -.
DR   PRIDE; P50447; -.
DR   GeneID; 397688; -.
DR   KEGG; ssc:397688; -.
DR   CTD; 5265; -.
DR   eggNOG; KOG2392; Eukaryota.
DR   InParanoid; P50447; -.
DR   OrthoDB; 1124079at2759; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR   GO; GO:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
DR   Gene3D; 2.30.39.10; -; 1.
DR   Gene3D; 3.30.497.10; -; 1.
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; PTHR11461; 1.
DR   Pfam; PF00079; Serpin; 1.
DR   SMART; SM00093; SERPIN; 1.
DR   SUPFAM; SSF56574; SSF56574; 1.
DR   PROSITE; PS00284; SERPIN; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Phosphoprotein; Protease inhibitor; Reference proteome;
KW   Secreted; Serine protease inhibitor; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..421
FT                   /note="Alpha-1-antitrypsin"
FT                   /id="PRO_0000032396"
FT   REGION          376..395
FT                   /note="RCL"
FT   SITE            385..386
FT                   /note="Reactive bond"
FT   MOD_RES         386
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P01009"
FT   CARBOHYD        73
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        110
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   421 AA;  47194 MW;  08A4AB2A9E600690 CRC64;
     MASSSTWGLL LLAGLCCLVP ISLAEGLQGH AVQETDVPRH DHEQHQEAAC HRIAPNLADF
     AFSLYRQVAR QSNTSNIFLS PVTIARAFAM LSLGTKGATH AEILEGLQFN LTEKAEAEIH
     EGFQHLLHTL NQPDNQLQLT TGNGLFIDEK AKLVPKFLED VKNLYHSEAF SINFRDTEEA
     KKCINDYVEK GSQGKIVDLV DELDKDTVFA LVNYIFFKGK WEKPFEVEQT TEEDFHVDEE
     TTVKVPMMNR LGMFDLHHCD KLSSWVLLMD YVATATAFFI LPDQGKLHQL EDMLTKEIRA
     KFLEKRYPSS ANLHLPKLTI SGTYDLKSLL GNLGITKVFS DEADLSGVTE EQPLKLSKAL
     HRAVLTIDEK GTEATGATIL EAIPMSIPPN VKFNKPFLFL IYDTKTKAVL FMGKVMNPTQ
     K