ID   AACT_PONAB              Reviewed;         423 AA.
AC   Q5R536;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Alpha-1-antichymotrypsin;
DE            Short=ACT;
DE   AltName: Full=Serpin A3;
DE   Flags: Precursor;
GN   Name=SERPINA3; Synonyms=AACT;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Although its physiological function is unclear, it can
CC       inhibit neutrophil cathepsin G and mast cell chymase, both of which can
CC       convert angiotensin-1 to the active angiotensin-2. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with DNAJC1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
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; CR861039; CAH93130.1; -; mRNA.
DR   RefSeq; NP_001126852.1; NM_001133380.1.
DR   AlphaFoldDB; Q5R536; -.
DR   SMR; Q5R536; -.
DR   STRING; 9601.ENSPPYP00000006946; -.
DR   MEROPS; I04.002; -.
DR   PRIDE; Q5R536; -.
DR   GeneID; 100173860; -.
DR   KEGG; pon:100173860; -.
DR   CTD; 12; -.
DR   eggNOG; KOG2392; Eukaryota.
DR   HOGENOM; CLU_023330_2_1_1; -.
DR   InParanoid; Q5R536; -.
DR   OMA; PDEGRME; -.
DR   OrthoDB; 1124079at2759; -.
DR   TreeFam; TF343201; -.
DR   Proteomes; UP000001595; Chromosome 14.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
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; Protease inhibitor; Reference proteome;
KW   Secreted; Serine protease inhibitor; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..423
FT                   /note="Alpha-1-antichymotrypsin"
FT                   /id="PRO_0000032413"
FT   REGION          369..394
FT                   /note="RCL"
FT   SITE            383..384
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        93
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        106
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        127
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        186
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        271
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   423 AA;  47815 MW;  AFE7039CB3752BF3 CRC64;
     MERMLPFLAL GLLVAGFCPA VLCHPNCPLD EENPTQENQD RGTHVDLGLA STNVDFAFSL
     YKQLVLKAPD KNVIFSPLSI STALAFLSLG AHNTTLTEIL TGLRFNLTET SEAEIHQSFQ
     HLLRTLNQSS DELQLSMGNA MFVEEQLSLL DRFMEDAKRL YGSEAFATDF QDSAAAKKLI
     NDYVKNRTRG KITDLIKDLD SQTMMVLVNY IFFKAKWKMP FDPQDTHQSR FYLSKKKWVM
     VPMMSLHHLT TPYFRDEELS CTVVELKYTG NASALFILPD QDKMEEVEAM LLPETLKRWR
     DSLEFRRIDE LYLPKFSISR AFNLENILLQ LGIVEAFTSK ADLSGITGAR NLVVSQVVHK
     AVLDVFEEGT EASAATAVKI TLLSALVDPM TIVRFNRPFL MIIVPTDTQN LLFISKVINP
     KQA