ID   A1AT_MERUN              Reviewed;         406 AA.
AC   Q64118;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Alpha-1-antitrypsin;
DE   AltName: Full=Alpha-1 protease inhibitor;
DE   AltName: Full=Alpha-1-antiproteinase;
DE   Flags: Precursor;
OS   Meriones unguiculatus (Mongolian jird) (Gerbillus unguiculatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Gerbillinae; Meriones.
OX   NCBI_TaxID=10047;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 25-44 AND 77-96, FUNCTION,
RP   AND TISSUE SPECIFICITY.
RC   TISSUE=Plasma;
RX   PubMed=7852275; DOI=10.1093/oxfordjournals.jbchem.a124564;
RA   Goto K., Suzuki Y., Yoshida K., Yamamoto K., Sinohara H.;
RT   "Plasma alpha-1-antiproteinase from the Mongolian gerbil, Meriones
RT   unguiculatus: isolation, partial characterization, sequencing of cDNA, and
RT   implications for molecular evolution.";
RL   J. Biochem. 116:582-588(1994).
CC   -!- FUNCTION: Inhibitor of serine proteases. Can inhibit elastase, trypsin,
CC       chymotrypsin and plasmin. {ECO:0000269|PubMed:7852275}.
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. {ECO:0000269|PubMed:7852275}.
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}.
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DR   EMBL; S77822; AAB33367.1; -; mRNA.
DR   PIR; JX0346; JX0346.
DR   AlphaFoldDB; Q64118; -.
DR   SMR; Q64118; -.
DR   MEROPS; I04.001; -.
DR   PRIDE; Q64118; -.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Phosphoprotein;
KW   Protease inhibitor; Secreted; Serine protease inhibitor; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..406
FT                   /note="Alpha-1-antitrypsin"
FT                   /id="PRO_0000032386"
FT   REGION          362..381
FT                   /note="RCL"
FT   SITE            371..372
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         33
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P01009"
FT   MOD_RES         372
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P01009"
FT   CARBOHYD        59
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        96
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        260
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   406 AA;  45127 MW;  814613E44C7AA469 CRC64;
     MTSSISWGLL LLAGLCCLVP SFLAEDAEKT DSSHQDHIMA SNLADFAFGL YRVLSHQSNT
     TNIFLSPLSI ATALAMLSLG SKDDTKAQLL QGLHFNLTET SEADIHKGFQ HLLKTLNRPD
     NELQLTTGSS LFVNNSLNLV EKFLEEVKNH YHSEAFFVNF ADSEEAKKTI NSFVEKATHG
     KIVDLVKDLE IDTVLALVNY IFFRGKWEKP FDPELTEEAD FHVDKSTTVK VPMMNRMGMF
     DVHYCDTLSS WVLLMDYLGN ATAIFILPDE GKMQHLEQTL TKEHIYKFLQ NRHTRSANVH
     LPKLSISGTY NLKKVLSPLG ITQVFSNGAD LSGITTDVPL KLSKAVHKAV LTLDERGTEA
     AGTTVLEAVP MSIPPDVCFK NPFVVIICDK HTQSPLFVGK VVNPTQ