ID   A1AT_MUSSA              Reviewed;         413 AA.
AC   Q63969;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Alpha-1-antiproteinase;
DE   AltName: Full=Alpha-1-antitrypsin;
DE   AltName: Full=Alpha-1-proteinase inhibitor;
DE   AltName: Full=Serpin A1;
DE   Flags: Precursor;
GN   Name=Serpina1;
OS   Mus saxicola (Brown spiny mouse) (Rock-loving mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Pyromys.
OX   NCBI_TaxID=10094;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8169957; DOI=10.1007/bf00166159;
RA   Rheaume C., Goodwin R.L., Latimer J.J., Baumann H., Berger F.G.;
RT   "Evolution of murine alpha 1-proteinase inhibitors: gene amplification and
RT   reactive center divergence.";
RL   J. Mol. Evol. 38:121-131(1994).
CC   -!- FUNCTION: Inhibitor of serine proteases. The primary target is
CC       elastase, but also has a moderate affinity for plasmin and thrombin (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   -!- 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; S70316; AAB30633.1; -; mRNA.
DR   PIR; I56481; I56481.
DR   AlphaFoldDB; Q63969; -.
DR   SMR; Q63969; -.
DR   MEROPS; I04.001; -.
DR   PRIDE; Q63969; -.
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                   /evidence="ECO:0000255"
FT   CHAIN           25..413
FT                   /note="Alpha-1-antiproteinase"
FT                   /id="PRO_0000032395"
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        64
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        101
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        265
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   413 AA;  46260 MW;  B02CE28E691D32E0 CRC64;
     MTPSISWRLL LLAGLCCLVP SYLAEDVQET DTSQKDQSPA SHEMATNLGD FAFSLYRELV
     HQSNTSNIFF SPVSIATAFA LLSLGSKGDT QTQILEGLQF NLTQTSEADI HKVFQHLLQT
     LNRPDSELQL STGNGLFVNN DLKLVEKFLE EAKNHYQSEV FSVNFAKSEE ARKMINDFVE
     KGTQGKIVDA VKDLDEDTVF ALANYIFFQG KWKTPFDPEH TTEADFHVNE STTVRVPMMN
     LMRMLDVHYC STLSSWVLMM DYLGNATAVF LLPDDGKMQH LEQTLNKELI SKFLLNRHRS
     LAEIHFPRLS ISGSYNLKAL MAPLGITRVF NNGADLSGIT EENAPLRLSK AVHKAVLTID
     ERGTEAAATT IVEAVFMSLP PILHFNHPFV FTIVETHTQT PLFVGKVVDP TRK