ID   SPA3N_RAT               Reviewed;         418 AA.
AC   P09006; Q03312;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 3.
DT   02-SEP-2026, entry version 163.
DE   RecName: Full=Serine protease inhibitor A3N;
DE            Short=Serpin A3N;
DE   AltName: Full=CPI-26;
DE   AltName: Full=Contrapsin-like protease inhibitor 6;
DE   AltName: Full=SPI-2.2;
DE   AltName: Full=Serine protease inhibitor 3;
DE            Short=SPI-3;
DE   Flags: Precursor;
GN   Name=Serpina3n; Synonyms=Spin2c;
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], INDUCTION, AND GLYCOSYLATION.
RC   TISSUE=Liver;
RX   PubMed=1694763; DOI=10.1111/j.1432-1033.1990.tb15587.x;
RA   Pages G., Rouayrenc J.F., le Cam G., Mariller M., le Cam A.;
RT   "Molecular characterization of three rat liver serine-protease inhibitors
RT   affected by inflammation and hypophysectomy. Protein and mRNA analysis and
RT   cDNA cloning.";
RL   Eur. J. Biochem. 190:385-391(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Liver;
RX   PubMed=1864837; DOI=10.1093/oxfordjournals.jbchem.a123369;
RA   Ohkubo K., Ogata S., Misumi Y., Takami N., Ikehara Y.;
RT   "Molecular cloning and characterization of rat contrapsin-like protease
RT   inhibitor and related proteins.";
RL   J. Biochem. 109:243-250(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 203-408.
RX   PubMed=3493437; DOI=10.1038/326096a0;
RA   Hill R.E., Hastie N.D.;
RT   "Accelerated evolution in the reactive centre regions of serine protease
RT   inhibitors.";
RL   Nature 326:96-99(1987).
RN   [5]
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).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Liver. {ECO:0000269|PubMed:1864837}.
CC   -!- INDUCTION: By acute inflammation. {ECO:0000269|PubMed:1694763}.
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   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:1694763}.
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}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-11 is the initiator.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH78796.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAA34408.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAA34408.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; X16359; CAA34408.1; ALT_SEQ; mRNA.
DR   EMBL; D00753; BAA00650.1; -; mRNA.
DR   EMBL; BC078796; AAH78796.2; ALT_INIT; mRNA.
DR   EMBL; X13150; CAA31548.1; -; mRNA.
DR   PIR; B26423; B26423.
DR   RefSeq; NP_113719.3; NM_031531.3.
DR   AlphaFoldDB; P09006; -.
DR   SMR; P09006; -.
DR   FunCoup; P09006; 62.
DR   MEROPS; I04.078; -.
DR   GlyCosmos; P09006; 3 sites, No reported glycans.
DR   GlyGen; P09006; 4 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site).
DR   iPTMnet; P09006; -.
DR   PhosphoSitePlus; P09006; -.
DR   Ensembl; ENSRNOT00055054855; ENSRNOP00055045337; ENSRNOG00055031674.
DR   Ensembl; ENSRNOT00060007613; ENSRNOP00060005707; ENSRNOG00060004529.
DR   Ensembl; ENSRNOT00065023367; ENSRNOP00065018188; ENSRNOG00065014139.
DR   GeneID; 24795; -.
DR   KEGG; rno:24795; -.
DR   UCSC; RGD:3747; rat.
DR   AGR; RGD:3747; -.
DR   CTD; 20716; -.
DR   RGD; 3747; Serpina3n.
DR   eggNOG; KOG2392; Eukaryota.
DR   HOGENOM; CLU_023330_2_1_1; -.
DR   InParanoid; P09006; -.
DR   OMA; RHIDELY; -.
DR   OrthoDB; 671595at2759; -.
DR   PhylomeDB; P09006; -.
DR   Reactome; R-RNO-114608; Platelet degranulation.
DR   Reactome; R-RNO-6798695; Neutrophil degranulation.
DR   PRO; PR:P09006; -.
DR   Proteomes; UP000002494; Chromosome 6.
DR   ExpressionAtlas; P09006; baseline.
DR   GO; GO:0005576; C:extracellular region; IDA:RGD.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR   GO; GO:0071320; P:cellular response to cAMP; IEP:RGD.
DR   GO; GO:0071385; P:cellular response to glucocorticoid stimulus; IEP:RGD.
DR   GO; GO:0071347; P:cellular response to interleukin-1; IEP:RGD.
DR   GO; GO:0071354; P:cellular response to interleukin-6; IEP:RGD.
DR   GO; GO:0071346; P:cellular response to type II interferon; IEP:RGD.
DR   GO; GO:0009617; P:response to bacterium; ISO:RGD.
DR   GO; GO:0034097; P:response to cytokine; ISO:RGD.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR   GO; GO:0043434; P:response to peptide hormone; ISO:RGD.
DR   GO; GO:0034516; P:response to vitamin B6; IEP:RGD.
DR   CDD; cd19551; serpinA3_A1AC; 1.
DR   FunFam; 3.30.497.10:FF:000001; Serine protease inhibitor; 1.
DR   FunFam; 2.30.39.10:FF:000002; Serpin family D member 1; 1.
DR   Gene3D; 2.30.39.10; Alpha-1-antitrypsin, domain 1; 1.
DR   Gene3D; 3.30.497.10; Antithrombin, subunit I, domain 2; 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:SF145; ALPHA-1-ANTICHYMOTRYPSIN; 1.
DR   PANTHER; PTHR11461; SERINE PROTEASE INHIBITOR, SERPIN; 1.
DR   Pfam; PF00079; Serpin; 1.
DR   SMART; SM00093; SERPIN; 1.
DR   SUPFAM; SSF56574; Serpins; 1.
DR   PROSITE; PS00284; SERPIN; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Phosphoprotein; Protease inhibitor; Reference proteome;
KW   Secreted; Serine protease inhibitor; Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000250"
FT   CHAIN           30..418
FT                   /note="Serine protease inhibitor A3N"
FT                   /id="PRO_0000032423"
FT   REGION          367..394
FT                   /note="RCL"
FT   SITE            381..382
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         93
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   CARBOHYD        104
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        258
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        269
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        12
FT                   /note="A -> D (in Ref. 3; CAA34408)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        20
FT                   /note="C -> S (in Ref. 3; CAA34408)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        68
FT                   /note="D -> H (in Ref. 3; CAA34408)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        92
FT                   /note="N -> S (in Ref. 3; CAA34408)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        236
FT                   /note="P -> S (in Ref. 3; CAA34408)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        323
FT                   /note="E -> EE (in Ref. 4; CAA31548)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        334
FT                   /note="V -> A (in Ref. 4; CAA31548)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        353
FT                   /note="S -> F (in Ref. 3; CAA34408)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        354
FT                   /note="Q -> E (in Ref. 4; CAA31548)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        381
FT                   /note="M -> V (in Ref. 4; CAA31548)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   418 AA;  46652 MW;  AADEFF087190B44F CRC64;
     MTRLVTLELL MAGIGSALLC FPDCILGEDT LFHEDQDKGT QLDSLTLASI NTDFAFSLYK
     KLALRNPDKN VVFSPLSISA ALAVVSLGAK GNSMEEILEG LKFNLTETPE TEIHRGFGHL
     LQRLSQPRDE IQISTGNALF IEKRLQVLAE FQEKAKALYQ AEAFTADFQQ SREAKKLIND
     YVSKQTQGKI QGLITNLAKK TSMVLVNYIY FKGKWKVPFD PRDTFQSEFY SGKRRPVKVP
     MMKLEDLTTP YVRDEELNCT VVELKYTGNA SALFILPDQG KMQQVEASLQ PETLRRWKDS
     LRPSMIDELY LPKFSISADY NLEDVLPELG IKEVFSTQAD LSGITGDKDL MVSQVVHKAV
     LDVAETGTEA AAATGVKFVP MSAKLDPLII AFDRPFLMII SDTETAIAPF LAKIFNPK
//