ID   A1AS_CAVPO              Reviewed;         405 AA.
AC   P22325;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Alpha-1-antiproteinase S;
DE            Short=APS;
DE   AltName: Full=Alpha-1-antitrypsin;
DE   AltName: Full=Alpha-1-proteinase inhibitor;
DE   Flags: Precursor;
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 25-44 AND 75-93.
RX   PubMed=1985973; DOI=10.1016/s0021-9258(17)35262-6;
RA   Suzuki Y., Yoshida K., Honda E., Sinohara H.;
RT   "Molecular cloning and sequence analysis of cDNAs coding for guinea pig
RT   alpha 1-antiproteinases S and F and contrapsin.";
RL   J. Biol. Chem. 266:928-932(1991).
CC   -!- FUNCTION: Inhibits elastase, chymotrypsin, cathepsin G, plasmin, and
CC       trypsin.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- INDUCTION: APS rose several hundred-fold during the acute phase
CC       reaction.
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; M57270; AAA62805.1; -; mRNA.
DR   PIR; A39088; A39088.
DR   RefSeq; NP_001166205.1; NM_001172734.1.
DR   AlphaFoldDB; P22325; -.
DR   SMR; P22325; -.
DR   STRING; 10141.ENSCPOP00000011412; -.
DR   MEROPS; I04.001; -.
DR   Ensembl; ENSCPOT00000012808; ENSCPOP00000011412; ENSCPOG00000012686.
DR   GeneID; 100379265; -.
DR   KEGG; cpoc:100379265; -.
DR   CTD; 10603; -.
DR   eggNOG; KOG2392; Eukaryota.
DR   GeneTree; ENSGT00940000154493; -.
DR   HOGENOM; CLU_023330_2_1_1; -.
DR   InParanoid; P22325; -.
DR   OMA; MEAIPMS; -.
DR   OrthoDB; 1124079at2759; -.
DR   TreeFam; TF343201; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   Bgee; ENSCPOG00000012686; Expressed in liver and 4 other tissues.
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   1: Evidence at protein level;
KW   Acute phase; Direct protein sequencing; Glycoprotein; Protease inhibitor;
KW   Reference proteome; Secreted; Serine protease inhibitor; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000269|PubMed:1985973"
FT   CHAIN           25..405
FT                   /note="Alpha-1-antiproteinase S"
FT                   /id="PRO_0000032382"
FT   REGION          360..379
FT                   /note="RCL"
FT   SITE            369..370
FT                   /note="Reactive bond"
FT   CARBOHYD        57
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        94
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        157
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        258
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   405 AA;  45125 MW;  5D41D48E1E078AA8 CRC64;
     MPSAIPRGLL LLAGLCCLVF GIMAEDAQVA QGPSQQIPRS LAHFAHSMYR VLTQQSNTSN
     IFFSPVSIAT ALAMVSVGAK GDTHTQILRG LEFNLTEIAE ADIHNGFQNL LHTLNRPHSE
     HQLTTGNGLF LDQKLKLKEK FSEDVKTLYH AEAFPTNFSN PKEAEKQINA YVEKGTQGKI
     VDLVKDLSAD TVLALVNYIF FRGKWEKPFD VKHTTQEDFH VDTSTTVKVP MMKREGKYKA
     FHCSTIQSWV LLLDYEGNVT ALFLLPEEGK MQHLEETLTP ELIFKFARKT ERMFANVHLP
     KLSISGTYDL KEVLGHLGIT NVFSDAADLS GVTEDIPLKI SKGLHKALLT IDEKGTEAAG
     ATMMEFMPMS LPEDLSFNKP FLFLIIDHST DTPLFVGKVM DPTKK