ID   SPA3M_RAT               Reviewed;         412 AA.
AC   Q63556;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=Serine protease inhibitor A3M;
DE            Short=Serpin A3M;
DE   AltName: Full=Serine protease inhibitor 2.4;
DE            Short=SPI-2.4;
DE   Flags: Precursor; Fragment;
GN   Name=Serpina3m;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RA   Inglis J.D.;
RL   Submitted (DEC-1992) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   REGION RCL.
RX   PubMed=15638460; DOI=10.1007/s00239-004-2640-9;
RA   Horvath A.J., Forsyth S.L., Coughlin P.B.;
RT   "Expression patterns of murine antichymotrypsin-like genes reflect
RT   evolutionary divergence at the Serpina3 locus.";
RL   J. Mol. Evol. 59:488-497(2004).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
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 serpin reactive site and the protease. The
CC       resulting inactive serpin-protease complex is highly stable (By
CC       similarity). Variability within the reactive center loop (RCL)
CC       sequences of Serpina3 paralogs may determine target protease
CC       specificity. {ECO:0000250}.
CC   -!- MISCELLANEOUS: The single human alpha1-antichymotrypsin gene (SERPINA3)
CC       is represented by a cluster of 6 individual rat paralogs.
CC   -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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DR   EMBL; X69834; CAA49488.1; -; mRNA.
DR   PIR; S31505; S31505.
DR   AlphaFoldDB; Q63556; -.
DR   SMR; Q63556; -.
DR   STRING; 10116.ENSRNOP00000013175; -.
DR   MEROPS; I04.058; -.
DR   GlyGen; Q63556; 3 sites.
DR   PaxDb; Q63556; -.
DR   PRIDE; Q63556; -.
DR   UCSC; RGD:735068; rat.
DR   RGD; 735068; Serpina3m.
DR   eggNOG; KOG2392; Eukaryota.
DR   InParanoid; Q63556; -.
DR   PhylomeDB; Q63556; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR   GO; GO:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
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   Glycoprotein; Protease inhibitor; Reference proteome; Secreted;
KW   Serine protease inhibitor; Signal.
FT   SIGNAL          <1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..412
FT                   /note="Serine protease inhibitor A3M"
FT                   /id="PRO_0000032420"
FT   REGION          360..386
FT                   /note="RCL"
FT   SITE            374..375
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        97
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        177
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        262
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
SQ   SEQUENCE   412 AA;  46095 MW;  CC6F4DBA7F118CF1 CRC64;
     FLLMAGICPA VLGFPDGTLG NDTLLHKDQD KGTQLDSLTL ESINTDFAFS LYKMLALKNP
     DKNVVFSPLS ISAALAIVSL GAKGNTLEEI LEVLRFNLTE SYETDIHQGF GHLLQRLSQP
     GDQVKIITGN ALFIDKNLQV LAEFQEKTRA LYQVEAFTAS FQQPRVTEKL INDSVRNQTQ
     GKIQELVSGL KERTSMVLVN ILLFRGKWKV PFDPDYTFES EFYVDEKRSV KVSMMKIEEL
     TTPYFRDEEL SCSVLELKYT GNSSALFILP DKGRMQQVEA SLQPETLKKW KDSLRPRKID
     ELYLPRLSIS TDYSLEEVLP ELGIRDVFSQ QADLSRITGA KDLSVSQVVH KVVLDVNETG
     TEAAAATGAN LVPRSGRPPM IVWFNRPFLI AVSHTHGQHI LFMAKVINPV GA