ID   A1AT_MUSCR              Reviewed;         412 AA.
AC   P26595;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Alpha-1-antiproteinase;
DE   AltName: Full=Alpha-1-antitrypsin;
DE            Short=AAT;
DE   AltName: Full=Alpha-1-proteinase inhibitor;
DE   AltName: Full=Serpin A1;
DE   Flags: Precursor;
GN   Name=Serpina1;
OS   Mus caroli (Ryukyu mouse) (Ricefield mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10089;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1689000; DOI=10.1128/mcb.10.2.760-769.1990;
RA   Latimer J.J., Berger F.G., Baumann H.;
RT   "Highly conserved upstream regions of the alpha 1-antitrypsin gene in two
RT   mouse species govern liver-specific expression by different mechanisms.";
RL   Mol. Cell. Biol. 10:760-769(1990).
CC   -!- FUNCTION: Inhibitor of serine proteases. Its primary target is
CC       elastase, but it also has a moderate affinity for plasmin and thrombin.
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   -!- TISSUE SPECIFICITY: Expressed not only in liver but also in kidney
CC       tubule cells, where it is regulated by androgens during development.
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; M33567; AAA37128.1; -; mRNA.
DR   PIR; A34730; ITMSC.
DR   AlphaFoldDB; P26595; -.
DR   SMR; P26595; -.
DR   ChEMBL; CHEMBL1795142; -.
DR   MEROPS; I04.001; -.
DR   MGI; MGI:98376; Serpina1.
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; 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; Secreted;
KW   Serine protease inhibitor; Signal.
FT   SIGNAL          1..24
FT   CHAIN           25..412
FT                   /note="Alpha-1-antiproteinase"
FT                   /id="PRO_0000032394"
FT   REGION          367..386
FT                   /note="RCL"
FT   SITE            376..377
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         33
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P01009"
FT   MOD_RES         377
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P01009"
FT   CARBOHYD        100
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        133
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        264
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        313
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   412 AA;  45872 MW;  C1A167063CDAF4BD CRC64;
     MTPSISWGLL LLAGLFCLVP SFLAEDVQET DTSRRDSVPA SHDTPYNLEL SISLYRELGH
     KSTTSNIFFS QVSIATAFAM LSLGEKGDTH TQILEGLQFN LTQTSEADIH KAFQHLLQTL
     NRPDSELQLS TGNGSLLNND LKLVEKFLEE AKNNYHSEVF SVNFAESEEA KKVINDFVEK
     GTQGKIAEAV KDPDEDTVFA LANYILFKGK WKKPFDPKHT EEAEFHVDTV TTVKVPMMTL
     TGMLDVHHCS TLSSWVLLMD YLGNRTAVFL LPDDGKMQHL EQTLNKELIS KFLLNRHRRL
     AQVHLPRLSL SGNYTLNTLM SHLGITRIFN NGADLSGITE ENAPLKLSKA ADKAVLTMDE
     TGTEAAAATV LQAVPMSMPP ILNFNKPFIF IIVEEHTQSP LFVGKVVDPT RK