ID   A1AF_RABIT              Reviewed;         413 AA.
AC   P23035;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   25-MAY-2022, entry version 98.
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;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2016265; DOI=10.1093/oxfordjournals.jbchem.a123338;
RA   Saito A., Sinohara H.;
RT   "Cloning and sequencing of cDNA coding for rabbit alpha-1-antiproteinase F:
RT   amino acid sequence comparison of alpha-1-antiproteinases of six mammals.";
RL   J. Biochem. 109:158-162(1991).
RN   [2]
RP   PROTEIN SEQUENCE OF 25-41.
RX   PubMed=3259574; DOI=10.1093/oxfordjournals.jbchem.a122255;
RA   Saito A., Sinohara H.;
RT   "Differential interactions of rabbit plasma alpha-1-antiproteinases S and F
RT   with porcine trypsin.";
RL   J. Biochem. 103:247-253(1988).
RN   [3]
RP   PROTEIN SEQUENCE OF 374-380.
RX   PubMed=2229014; DOI=10.1093/oxfordjournals.jbchem.a123167;
RA   Saito A., Sinohara H.;
RT   "Amino acid sequence at the reactive site of rabbit alpha-1-
RT   antiproteinases.";
RL   J. Biochem. 108:80-85(1990).
CC   -!- FUNCTION: Inhibitor of serine proteases. The primary target is
CC       elastase, but also has a moderate affinity for plasmin and thrombin.
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; X57710; CAA40881.1; -; mRNA.
DR   EMBL; D00853; BAA00728.1; -; mRNA.
DR   PIR; JX0154; JX0154.
DR   RefSeq; NP_001075654.1; NM_001082185.1.
DR   AlphaFoldDB; P23035; -.
DR   SMR; P23035; -.
DR   STRING; 9986.ENSOCUP00000015803; -.
DR   MEROPS; I04.001; -.
DR   GeneID; 100008973; -.
DR   KEGG; ocu:100008973; -.
DR   eggNOG; KOG2392; Eukaryota.
DR   OrthoDB; 1124079at2759; -.
DR   Proteomes; UP000001811; Unplaced.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Protease inhibitor;
KW   Reference proteome; Secreted; Serine protease inhibitor; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000269|PubMed:3259574"
FT   CHAIN           25..413
FT                   /note="Alpha-1-antiproteinase F"
FT                   /id="PRO_0000032397"
FT   REGION          368..387
FT                   /note="RCL"
FT   SITE            377..378
FT                   /note="Reactive bond"
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        230
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   413 AA;  45867 MW;  E851F5DE63A592DF CRC64;
     MPPSVSRALL LLAGLGCLLP GFLADEAQET AVSSHEQDHP ACHRIAPSLA EFALSLYREV
     AHESNTTNIF FSPVSIALAF AMLSLGAKGD THTQVLEGLK FNLTETAEAQ IHDGFRHLLH
     TVNRPDSELQ LAARNALVVH ENLKLQHKFL EDAKNLYQSE AFLVDFRDPE QAKTKINSHV
     EKGTRGKIVD LVQELDARTL LALVNYVFFK GKWEKPFEPE NTKEEDFHVN ATTTVRVPMM
     SRLGRYDLFH CSTLASTVLR MDYKGNATAL FLLPDEGKLQ HLEDTLTTEL ITKFLAKSSL
     RSVTVHFPKL SISGTYDLKP LLGKLGITQV FSDNADLSGI TEQEPLKASQ ALHKAVLTID
     ERGTEAAGAT YMEIIPMSLP DSITLDRPFL FVIYSHEIKS PLFVGKVVDP TQH