ID   A1AT_CALCN              Reviewed;         412 AA.
AC   O54763;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Alpha-1-antiproteinase;
DE   AltName: Full=Alpha-1-antitrypsin;
DE   AltName: Full=Alpha-1-proteinase inhibitor;
DE   Flags: Precursor;
OS   Callosciurus caniceps (Gray-bellied squirrel).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC   Callosciurinae; Callosciurini; Callosciurus.
OX   NCBI_TaxID=64664;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=9434174; DOI=10.1016/s0378-1119(97)00532-5;
RA   Takamatsu N., Kojima M., Taniyama M., Ohba K., Uematsu T., Segawa C.,
RA   Tsutou S., Watanabe M., Kondo J., Kondo N., Shiba T.;
RT   "Expression of multiple alpha1-antitrypsin-like genes in hibernating
RT   species of the squirrel family.";
RL   Gene 204:127-132(1997).
CC   -!- FUNCTION: Inhibitor of serine proteases. {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.
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; AB000552; BAA24422.1; -; mRNA.
DR   AlphaFoldDB; O54763; -.
DR   SMR; O54763; -.
DR   MEROPS; I04.001; -.
DR   PRIDE; O54763; -.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0006953; P:acute-phase response; 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   Acute phase; Glycoprotein; Phosphoprotein; Protease inhibitor; Secreted;
KW   Serine protease inhibitor; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..412
FT                   /note="Alpha-1-antiproteinase"
FT                   /id="PRO_0000032383"
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   412 AA;  45729 MW;  7235668E9EE8FCC6 CRC64;
     MPSSISWGLL LLAGLCCLAP GSLAGDAQET DASKDDHEHP ACHKIAPNLA EFAFDLYRVL
     ARQSNTTNIF FSPVSVATAL AALSLGTKGD THTQILEGLD FNLTEMAETD IHQGFQHLLQ
     TLNRPNNQLQ LTTGNGLFID QSLKLADKFL EDVKNLYHSE AFSTNFTDSE EAKKQINGYV
     EKGTQGKIVD AVKTLDKNTV FALVNYIFFK GKWEKPFEVE HTTEGDFHVD QATTVKVPMM
     NRLGRFDLLY CTTLASWVLQ MDYLGNATAI FLLPDEGKLQ HLEDTITKEI LSKFLKNRHT
     RTVNLYFPKL SITGTYDLRS VLSTLGITKV FSNEADLSGV TEEAPLKLSK GVHKAVLTID
     ERGTEAAGVT VLEAIPMSLP PDVRFDRPFL IIIYEHYTKS PLFVGKVVNP TQ