ID   A1AT_CHLAE              Reviewed;         396 AA.
AC   O00394;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   25-MAY-2022, entry version 76.
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; Fragment;
GN   Name=SERPINA1;
OS   Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Chlorocebus.
OX   NCBI_TaxID=9534;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Kidney;
RA   Yoshida K., Suzuki Y., Yamamoto K., Watanabe M., Sinohara H.;
RT   "Cloning and sequencing of complementary DNAs encoding alpha-2-HS
RT   glycoprotein, alpha-1-antitrypsin, and beta-actin from African green
RT   monkey, Cercopithecus aethiops.";
RL   Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
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; AB004044; BAA20264.1; -; mRNA.
DR   AlphaFoldDB; O00394; -.
DR   SMR; O00394; -.
DR   MEROPS; I04.001; -.
DR   PRIDE; O00394; -.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; NAS:UniProtKB.
DR   GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
DR   GO; GO:0030162; P:regulation of proteolysis; NAS:UniProtKB.
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; Secreted;
KW   Serine protease inhibitor; Signal.
FT   SIGNAL          <1..2
FT                   /evidence="ECO:0000255"
FT   CHAIN           3..396
FT                   /note="Alpha-1-antitrypsin"
FT                   /id="PRO_0000032376"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          351..370
FT                   /note="RCL"
FT   SITE            360..361
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         16
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P01009"
FT   MOD_RES         361
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P01009"
FT   CARBOHYD        48
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        85
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        123
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        249
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
SQ   SEQUENCE   396 AA;  44587 MW;  1042EABFAA0A2825 CRC64;
     HVEDPQGDAA QKTDTSHHDQ EHSTFNKITP SLAEFAFSLY RQLAHQSNST NIFFSPVSIA
     TAFAMLSLGT KADTHSEILE GLNFNLTEIP EAQIHEGFQE LLHTLNKPDS QLQLTTGNGL
     FLNKSVKVVD KFLEDVKKLY HSEAFSVNFE DTEEAKKQIN NYVEKGTQGK IVDLVKELDR
     DTVFALVNYI FFKGKWERPF EVEATKEEDF HVDQATTVKV PMMRRLGMFN IYHCEKLSSW
     VLLMKYLGNA TAIFFLPDEG KLQHLENELT HDIITKFLEN ENRRSANLHL PKLAITGTYD
     LKTVLGHLGI TKVFSNGADL SGVTEDAPLK LSKAVHKAVL TIDEKGTEAA GAMFLEAIPM
     SIPPEVKFNK PFVFLMIEQN TKSPLFMGKV VNPTQK