SPA3M_MOUSE
ID SPA3M_MOUSE Reviewed; 418 AA.
AC Q03734; E9Q926; Q62260;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Serine protease inhibitor A3M;
DE Short=Serpin A3M;
DE Flags: Precursor;
GN Name=Serpina3m;
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].
RX PubMed=2049065; DOI=10.1042/bj2760337;
RA Ohkubo K., Ogata S., Misumi Y., Takami N., Sinohara H., Ikehara Y.;
RT "Cloning, structure and expression of cDNA for mouse contrapsin and a
RT related protein.";
RL Biochem. J. 276:337-342(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon, and 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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 145-418.
RC TISSUE=Liver;
RA Inglis J.D.;
RL Submitted (DEC-1992) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PROTEIN SEQUENCE OF 338-358, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [6]
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 [7]
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 [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-104 AND ASN-269.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=16944957; DOI=10.1021/pr060186m;
RA Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.;
RT "Proteome-wide characterization of N-glycosylation events by diagonal
RT chromatography.";
RL J. Proteome Res. 5:2438-2447(2006).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in liver and testis.
CC {ECO:0000269|PubMed:15638460}.
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; X55148; CAA38949.1; -; mRNA.
DR EMBL; AC117194; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC011158; AAH11158.1; -; mRNA.
DR EMBL; BC053337; AAH53337.1; -; mRNA.
DR EMBL; X69832; CAA49486.1; -; mRNA.
DR CCDS; CCDS36538.1; -.
DR PIR; S23675; S23675.
DR RefSeq; NP_033279.2; NM_009253.2.
DR AlphaFoldDB; Q03734; -.
DR SMR; Q03734; -.
DR STRING; 10090.ENSMUSP00000130979; -.
DR MEROPS; I04.029; -.
DR GlyGen; Q03734; 3 sites.
DR iPTMnet; Q03734; -.
DR PhosphoSitePlus; Q03734; -.
DR SwissPalm; Q03734; -.
DR CPTAC; non-CPTAC-3946; -.
DR jPOST; Q03734; -.
DR MaxQB; Q03734; -.
DR PaxDb; Q03734; -.
DR PeptideAtlas; Q03734; -.
DR PRIDE; Q03734; -.
DR ProteomicsDB; 263307; -.
DR DNASU; 20717; -.
DR Ensembl; ENSMUST00000101078; ENSMUSP00000098639; ENSMUSG00000079012.
DR Ensembl; ENSMUST00000168797; ENSMUSP00000130979; ENSMUSG00000079012.
DR GeneID; 20717; -.
DR KEGG; mmu:20717; -.
DR UCSC; uc007oxf.2; mouse.
DR CTD; 20717; -.
DR MGI; MGI:98378; Serpina3m.
DR VEuPathDB; HostDB:ENSMUSG00000079012; -.
DR eggNOG; KOG2392; Eukaryota.
DR GeneTree; ENSGT00940000154392; -.
DR HOGENOM; CLU_023330_2_1_1; -.
DR InParanoid; Q03734; -.
DR OMA; CNEGTIL; -.
DR OrthoDB; 1124079at2759; -.
DR PhylomeDB; Q03734; -.
DR TreeFam; TF343201; -.
DR BioGRID-ORCS; 20717; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Serpina3m; mouse.
DR PRO; PR:Q03734; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q03734; protein.
DR Bgee; ENSMUSG00000079012; Expressed in left lobe of liver and 41 other tissues.
DR Genevisible; Q03734; MM.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
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 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 Direct protein sequencing; 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 A3M"
FT /id="PRO_0000032418"
FT REGION 367..392
FT /note="RCL"
FT SITE 381..382
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957"
FT CONFLICT 61..63
FT /note="KMA -> ELV (in Ref. 1; CAA38949 and 3; AAH11158/
FT AAH53337)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="T -> A (in Ref. 1; CAA38949, 3; AAH11158/AAH53337
FT and 4; CAA49486)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="Q -> K (in Ref. 1; CAA38949, 3; AAH11158/AAH53337
FT and 4; CAA49486)"
FT /evidence="ECO:0000305"
FT CONFLICT 175..176
FT /note="TK -> KN (in Ref. 1; CAA38949, 3; AAH11158/AAH53337
FT and 4; CAA49486)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="K -> E (in Ref. 1; CAA38949, 3; AAH11158/AAH53337
FT and 4; CAA49486)"
FT /evidence="ECO:0000305"
FT CONFLICT 199..200
FT /note="DR -> TD (in Ref. 1; CAA38949, 3; AAH11158/AAH53337
FT and 4; CAA49486)"
FT /evidence="ECO:0000305"
FT CONFLICT 313
FT /note="K -> R (in Ref. 4; CAA49486)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 418 AA; 47064 MW; 1B4EF79A7C433FC0 CRC64;
MAFIAALGIL MAGICPTVLC FSDDTWGIDI LLHKNQESGT PDDSLTLASI NTDFAFSLYK
KMALKNPDKN IVFSPLSISA ALALVSLGAK GNTLEEILEG LKFNLTETSE ADIHQGFGHL
LQRLSQPEDQ DQINIGNAMF IEKDLQILAE FHEKTRALYQ TEAFTADFQQ PTEATKLIND
YVSNQTQGMI KKLISELDDR TLMVLVNYIY FKGKWKISFD PQDTFESEFY LDEKRSVKVP
MMKMKFLTTR HFRDEELSCS VLELKYTGNA SALFILPDQG RMQQVEASLQ PETLRKWWKS
LKTRKIGELY LPKFSISTDY NLKDILPELG IKEIFSKQAD LSGITGTKDL SVSQVVHKAV
LDVAETGTEA AAATGFIFGF RSRRLQTMTV QFNRPFLMVI SHTGVQTTLF MAKVTNPK
