SPA3N_MOUSE
ID SPA3N_MOUSE Reviewed; 418 AA.
AC Q91WP6; Q62258;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=Serine protease inhibitor A3N;
DE Short=Serpin A3N;
DE Flags: Precursor;
GN Name=Serpina3n; Synonyms=Spi2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=129;
RX PubMed=1718822; DOI=10.1016/0378-1119(91)90201-l;
RA Inglis J.D., Lee M., Davidson D.R., Hill R.E.;
RT "Isolation of two cDNAs encoding novel alpha-1-antichymotrypsin-like
RT proteins in a murine chondrocytic cell line.";
RL Gene 106:213-220(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
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 [3]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12659817; DOI=10.1016/s0888-7543(02)00041-1;
RA Forsyth S., Horvath A., Coughlin P.;
RT "A review and comparison of the murine alpha1-antitrypsin and alpha1-
RT antichymotrypsin multigene clusters with the human clade A serpins.";
RL Genomics 81:336-345(2003).
RN [4]
RP TISSUE SPECIFICITY, AND 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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 21-418.
RX PubMed=16141197; DOI=10.1074/jbc.m505598200;
RA Horvath A.J., Irving J.A., Rossjohn J., Law R.H., Bottomley S.P.,
RA Quinsey N.S., Pike R.N., Coughlin P.B., Whisstock J.C.;
RT "The murine orthologue of human antichymotrypsin: a structural paradigm for
RT clade A3 serpins.";
RL J. Biol. Chem. 280:43168-43178(2005).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in brain, heart, liver,
CC lung, spleen, testis and thymus, and at low levels in bone marrow,
CC kidney and skeletal muscle. {ECO:0000269|PubMed:15638460,
CC ECO:0000269|PubMed:1718822}.
CC -!- INDUCTION: Expression is induced by bacterial lipopolysaccharide (LPS).
CC {ECO:0000269|PubMed:1718822}.
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 14 individual murine paralogs.
CC -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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DR EMBL; M64086; AAA40130.1; -; mRNA.
DR EMBL; BC013651; AAH13651.1; -; mRNA.
DR CCDS; CCDS26152.1; -.
DR PIR; JH0494; JH0494.
DR PDB; 1YXA; X-ray; 2.10 A; A/B=21-418.
DR PDBsum; 1YXA; -.
DR AlphaFoldDB; Q91WP6; -.
DR SMR; Q91WP6; -.
DR IntAct; Q91WP6; 1.
DR STRING; 10090.ENSMUSP00000021506; -.
DR MEROPS; I04.078; -.
DR GlyGen; Q91WP6; 3 sites.
DR iPTMnet; Q91WP6; -.
DR PhosphoSitePlus; Q91WP6; -.
DR CPTAC; non-CPTAC-3878; -.
DR jPOST; Q91WP6; -.
DR MaxQB; Q91WP6; -.
DR PaxDb; Q91WP6; -.
DR PeptideAtlas; Q91WP6; -.
DR PRIDE; Q91WP6; -.
DR ProteomicsDB; 263308; -.
DR MGI; MGI:105045; Serpina3n.
DR eggNOG; KOG2392; Eukaryota.
DR InParanoid; Q91WP6; -.
DR PhylomeDB; Q91WP6; -.
DR ChiTaRS; Serpina3n; mouse.
DR EvolutionaryTrace; Q91WP6; -.
DR PRO; PR:Q91WP6; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q91WP6; protein.
DR GO; GO:0005576; C:extracellular region; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR GO; GO:0034097; P:response to cytokine; IDA:MGI.
DR GO; GO:0043434; P:response to peptide hormone; IDA:MGI.
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 3D-structure; Acute phase; Glycoprotein; Protease inhibitor;
KW Reference proteome; Secreted; Serine protease inhibitor; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..418
FT /note="Serine protease inhibitor A3N"
FT /id="PRO_0000032419"
FT REGION 367..392
FT /note="RCL"
FT SITE 381..382
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 104
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 231
FT /note="A -> C (in Ref. 1; AAA40130)"
FT /evidence="ECO:0000305"
FT HELIX 48..65
FT /evidence="ECO:0007829|PDB:1YXA"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:1YXA"
FT HELIX 75..86
FT /evidence="ECO:0007829|PDB:1YXA"
FT HELIX 91..100
FT /evidence="ECO:0007829|PDB:1YXA"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:1YXA"
FT HELIX 110..124
FT /evidence="ECO:0007829|PDB:1YXA"
FT STRAND 131..142
FT /evidence="ECO:0007829|PDB:1YXA"
FT HELIX 149..159
FT /evidence="ECO:0007829|PDB:1YXA"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:1YXA"
FT HELIX 171..185
FT /evidence="ECO:0007829|PDB:1YXA"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:1YXA"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:1YXA"
FT STRAND 203..212
FT /evidence="ECO:0007829|PDB:1YXA"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:1YXA"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:1YXA"
FT STRAND 225..229
FT /evidence="ECO:0007829|PDB:1YXA"
FT STRAND 237..254
FT /evidence="ECO:0007829|PDB:1YXA"
FT TURN 255..258
FT /evidence="ECO:0007829|PDB:1YXA"
FT STRAND 259..277
FT /evidence="ECO:0007829|PDB:1YXA"
FT HELIX 282..287
FT /evidence="ECO:0007829|PDB:1YXA"
FT HELIX 291..300
FT /evidence="ECO:0007829|PDB:1YXA"
FT STRAND 302..312
FT /evidence="ECO:0007829|PDB:1YXA"
FT STRAND 314..321
FT /evidence="ECO:0007829|PDB:1YXA"
FT HELIX 323..328
FT /evidence="ECO:0007829|PDB:1YXA"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:1YXA"
FT HELIX 342..345
FT /evidence="ECO:0007829|PDB:1YXA"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:1YXA"
FT STRAND 354..363
FT /evidence="ECO:0007829|PDB:1YXA"
FT STRAND 365..369
FT /evidence="ECO:0007829|PDB:1YXA"
FT STRAND 389..391
FT /evidence="ECO:0007829|PDB:1YXA"
FT STRAND 396..402
FT /evidence="ECO:0007829|PDB:1YXA"
FT TURN 403..405
FT /evidence="ECO:0007829|PDB:1YXA"
FT STRAND 409..415
FT /evidence="ECO:0007829|PDB:1YXA"
SQ SEQUENCE 418 AA; 46718 MW; 4BF21BBE10A81F6C CRC64;
MAFIAALGLL MAGICPAVLC FPDGTLGMDA AVQEDHDNGT QLDSLTLASI NTDFAFSLYK
ELVLKNPDKN IVFSPLSISA ALAVMSLGAK GNTLEEILEG LKFNLTETSE ADIHQGFGHL
LQRLNQPKDQ VQISTGSALF IEKRQQILTE FQEKAKTLYQ AEAFTADFQQ PRQAKKLIND
YVRKQTQGMI KELVSDLDKR TLMVLVNYIY FKAKWKVPFD PLDTFKSEFY AGKRRPVIVP
MMSMEDLTTP YFRDEELSCT VVELKYTGNA SALFILPDQG RMQQVEASLQ PETLRKWKNS
LKPRMIDELH LPKFSISTDY SLEDVLSKLG IREVFSTQAD LSAITGTKDL RVSQVVHKAV
LDVAETGTEA AAATGVKFVP MSAKLYPLTV YFNRPFLIMI FDTETEIAPF IAKIANPK
