SPA3N_RAT
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 03-AUG-2022, entry version 146.
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;
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_113719.1; NM_031531.1.
DR AlphaFoldDB; P09006; -.
DR SMR; P09006; -.
DR STRING; 10116.ENSRNOP00000014073; -.
DR MEROPS; I04.078; -.
DR GlyGen; P09006; 3 sites.
DR iPTMnet; P09006; -.
DR PhosphoSitePlus; P09006; -.
DR PaxDb; P09006; -.
DR PRIDE; P09006; -.
DR Ensembl; ENSRNOT00000014073; ENSRNOP00000014073; ENSRNOG00000029949.
DR GeneID; 24795; -.
DR KEGG; rno:24795; -.
DR UCSC; RGD:3747; rat.
DR CTD; 20716; -.
DR RGD; 3747; Serpina3n.
DR eggNOG; KOG2392; Eukaryota.
DR GeneTree; ENSGT00940000154392; -.
DR HOGENOM; CLU_023330_2_1_1; -.
DR InParanoid; P09006; -.
DR OrthoDB; 1124079at2759; -.
DR PhylomeDB; P09006; -.
DR TreeFam; TF343201; -.
DR PRO; PR:P09006; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Genevisible; P09006; RN.
DR GO; GO:0005576; C:extracellular region; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; 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:0071346; P:cellular response to interferon-gamma; 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:0006954; P:inflammatory response; IEP:RGD.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
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 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 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
