ID   A1AT_PAPAN              Reviewed;         409 AA.
AC   P01010;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Alpha-1-antitrypsin;
DE            Short=AAT;
DE   AltName: Full=Alpha-1 protease inhibitor;
DE   AltName: Full=Alpha-1-antiproteinase;
DE   AltName: Full=Serpin A1;
DE   Flags: Precursor; Fragment;
GN   Name=SERPINA1; Synonyms=PI;
OS   Papio anubis (Olive baboon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Papio.
OX   NCBI_TaxID=9555;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7031661; DOI=10.1073/pnas.78.11.6826;
RA   Kurachi K., Chandra T., Friezner Degen S.J., White T.T., Marchioro T.L.,
RA   Woo S.L.C., Davie E.W.;
RT   "Cloning and sequence of cDNA coding for alpha 1-antitrypsin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 78:6826-6830(1981).
CC   -!- FUNCTION: Inhibitor of serine proteases. Its primary target is
CC       elastase, but it also has a moderate affinity for plasmin and thrombin.
CC       Inhibits trypsin, chymotrypsin and plasminogen activator (By
CC       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 {ECO:0000250}.
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; J00321; AAA35377.1; -; mRNA.
DR   AlphaFoldDB; P01010; -.
DR   SMR; P01010; -.
DR   STRING; 9555.ENSPANP00000013142; -.
DR   MEROPS; I04.001; -.
DR   PRIDE; P01010; -.
DR   eggNOG; KOG2392; Eukaryota.
DR   Proteomes; UP000028761; Unplaced.
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; 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   Acute phase; Glycoprotein; Phosphoprotein; Protease inhibitor;
KW   Reference proteome; Secreted; Serine protease inhibitor; Signal.
FT   SIGNAL          <1..15
FT   CHAIN           16..409
FT                   /note="Alpha-1-antitrypsin"
FT                   /id="PRO_0000032378"
FT   REGION          18..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          364..383
FT                   /note="RCL"
FT   SITE            373..374
FT                   /note="Reactive bond"
FT   MOD_RES         374
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P01009"
FT   CARBOHYD        61
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        98
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        136
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        262
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
SQ   SEQUENCE   409 AA;  45694 MW;  E19B0B7450FDBA9B CRC64;
     LLLAGLCCLL PGSLAEDPQG DAAQKTDTPP HDQNHPTLNK ITPSLAEFAF SLYRQLAHQS
     NSTNIFFSPV SIATAFAMLS LGTKADTHSE ILEGLNFNLT EIPEAQVHEG FQELLRTLNK
     PDSQLQLTTG NGLFLNKSLK VVDKFLEDVK NLYHSEAFSV NFEDTEEAKK QINNYVEKGT
     QGKVVDLVKE LDRDTVFALV NYIFFKGKWE RPFEVEATEE EDFHVDQATT VKVPMMRRLG
     MFNIYHCEKL SSWVLLMKYL GNATAIFFLP DEGKLQHLEN ELTHDIITKF LENENRRSAN
     LHLPKLAITG TYDLKTVLGH LGITKVFSNG ADLSGVTEDA PLKLSKAVHK AVLTIDEKGT
     EAAGAMFLEA IPMSIPPEVK FNKPFVFLMI EQNTKSPLFI GKVVNPTQK