ID   A1AT_MESAU              Reviewed;         413 AA.
AC   P97277;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Alpha-1-antitrypsin;
DE   AltName: Full=Alpha-1 protease inhibitor;
DE   AltName: Full=Alpha-1-antiproteinase;
DE   Flags: Precursor;
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=7548212; DOI=10.1016/0167-4781(95)00140-c;
RA   Nakatani T., Suzuki Y., Yoshida K., Sinohara H.;
RT   "Molecular cloning and sequence analysis of cDNA encoding plasma alpha-1-
RT   antiproteinase from Syrian hamster: implications for the evolution of
RT   Rodentia.";
RL   Biochim. Biophys. Acta 1263:245-248(1995).
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 {ECO:0000250}.
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 serpin reactive site and the active site
CC       of the protease. The resulting inactive serpin-protease complex is
CC       highly stable (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; D49709; BAA08557.1; -; mRNA.
DR   PIR; S60036; S60036.
DR   RefSeq; NP_001268583.1; NM_001281654.1.
DR   AlphaFoldDB; P97277; -.
DR   SMR; P97277; -.
DR   STRING; 10036.XP_005068423.1; -.
DR   MEROPS; I04.001; -.
DR   PRIDE; P97277; -.
DR   GeneID; 101841330; -.
DR   CTD; 5265; -.
DR   eggNOG; KOG2392; Eukaryota.
DR   OrthoDB; 1124079at2759; -.
DR   Proteomes; UP000189706; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; 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   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..413
FT                   /note="Alpha-1-antitrypsin"
FT                   /id="PRO_0000032387"
FT   REGION          368..387
FT                   /note="RCL"
FT   SITE            377..378
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         33
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P01009"
FT   MOD_RES         378
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P01009"
FT   CARBOHYD        65
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        102
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        165
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        266
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   413 AA;  45819 MW;  71D192E106A1EB36 CRC64;
     MKPSISWGIL LLAGLCCLVP SFLAEDAQET DASKQDQEHQ ACCKIAPNLA DFSFNLYREL
     VHQSNTTNIF FSPVSIATAF AMLSLGTKGV THTQILEGLG FNLTEIAEAE VHKGFHNLLQ
     TFNRPDNELQ LTTGNGLFIH NNLKLVDKFL EEVKNDYHSE AFSVNFTDSE EAKKVINGFV
     EKGTQGKIVD LVKDLDKDTV LALVNYIFFK GKWKKPFDAD NTEEADFHVD KTTTVKVPMM
     SRLGMFDVHY VSTLSSWVLL MDYLGNATAI FILPDDGKMQ HLEQTLNKEI IGKFLKDRHT
     RSANVHFPKL SISGTYNLKT ALDPLGITQV FSNGADLSGI TEDVPLKLGK AVHKAVLTID
     ERGTEAAGAT FMEIIPMSVP PEVNFNSPFI AIIYDRQTAK SPLFVGKVVD PTR