ID   A1AF_CAVPO              Reviewed;         403 AA.
AC   P22324;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=Alpha-1-antiproteinase F;
DE            Short=APF;
DE   AltName: Full=Alpha-1-antitrypsin;
DE   AltName: Full=Alpha-1-proteinase inhibitor;
DE   Flags: Precursor; Fragment;
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 23-42 AND 73-91.
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: APF rose about 2-fold during the acute phase 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; M57271; AAA62804.1; -; mRNA.
DR   PIR; B39088; B39088.
DR   AlphaFoldDB; P22324; -.
DR   SMR; P22324; -.
DR   STRING; 10141.ENSCPOP00000013843; -.
DR   MEROPS; I04.001; -.
DR   eggNOG; KOG2392; Eukaryota.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
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..22
FT                   /evidence="ECO:0000269|PubMed:1985973"
FT   CHAIN           23..403
FT                   /note="Alpha-1-antiproteinase F"
FT                   /id="PRO_0000032381"
FT   REGION          358..377
FT                   /note="RCL"
FT   SITE            367..368
FT                   /note="Reactive bond; unorthodox type"
FT   CARBOHYD        55
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        92
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        155
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        222
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        256
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
SQ   SEQUENCE   403 AA;  44920 MW;  C39729EB364D909B CRC64;
     SAIPRGLLLL AGLCCLVFGI MAEDAQVAQG PSQQIPRSLA HFAHSMYRVL TQQSNTSNIF
     FSPVSIATAL AMVSLGAKGD THTQILWGLE FNLTEIAEAD IHDGFQNLLH TLNRPHSEHE
     LTTGNGLFLD QKLKLKEKFS EDVKTLYHAE AFPTNFSNPK EAEKQINAYV EKGTQGKIVD
     LVKDLSADTV LALVNYIFFR GKWEKPFDVK HTTQEDFLVD MNTTVNVPMM KRQGMYKAFH
     CSTIQSWVLL LDYEGNVTTL FLLPDKGKMQ HLEETLTPEL IFKFARKTER MFANVHLPKL
     SISGTYDLKE VLGHLGITNV FSGAADLSGI TEDMPLKISK GLHKALLTID EKGTEAAGAT
     ELEITPHSVP QDLFFNKPFL FLIIDHSTDT PLFVGKVMDP TKK