A1AT3_MOUSE
ID A1AT3_MOUSE Reviewed; 412 AA.
AC Q00896; P81105; Q91V74; Q91WH5; Q91XC1;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 25-MAY-2022, entry version 154.
DE RecName: Full=Alpha-1-antitrypsin 1-3;
DE AltName: Full=Alpha-1 protease inhibitor 3;
DE AltName: Full=Alpha-1 protease inhibitor 6;
DE AltName: Full=Alpha-1-antitrypsin 1-6;
DE AltName: Full=Serine protease inhibitor 1-3;
DE AltName: Full=Serine protease inhibitor 1-6;
DE AltName: Full=Serine protease inhibitor A1c;
DE Short=Serpin A1c;
DE Flags: Precursor;
GN Name=Serpina1c; Synonyms=Dom3, Dom6, Spi1-3, Spi1-6;
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].
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=1946354; DOI=10.1073/pnas.88.21.9417;
RA Borriello F., Krauter K.S.;
RT "Multiple murine alpha 1-protease inhibitor genes show unusual evolutionary
RT divergence.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:9417-9421(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver, and Salivary gland;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 203-412.
RX PubMed=6547997; DOI=10.1038/311175a0;
RA Hill R.E., Shaw P.H., Boyd P.A., Baumann H., Hastie N.D.;
RT "Plasma protease inhibitors in mouse and man: divergence within the
RT reactive centre regions.";
RL Nature 311:175-177(1984).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8619829; DOI=10.1006/bbrc.1996.0182;
RA Paterson T., Moore S.;
RT "The expression and characterization of five recombinant murine alpha 1-
RT protease inhibitor proteins.";
RL Biochem. Biophys. Res. Commun. 219:64-69(1996).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND REGION RCL.
RX PubMed=11961105; DOI=10.1093/oxfordjournals.molbev.a004130;
RA Barbour K.W., Goodwin R.L., Guillonneau F., Wang Y., Baumann H.,
RA Berger F.G.;
RT "Functional diversification during evolution of the murine alpha(1)-
RT proteinase inhibitor family: role of the hypervariable reactive center
RT loop.";
RL Mol. Biol. Evol. 19:718-727(2002).
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 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-265.
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 -!- FUNCTION: Inhibitor of serine proteases. Can inhibit trypsin and
CC chymotrypsin; relatively ineffective against elastase.
CC {ECO:0000269|PubMed:11961105, ECO:0000269|PubMed:8619829}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11961105,
CC ECO:0000269|PubMed:8619829}.
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 carboxyl group of the serpin reactive site
CC and the serine hydroxyl of the protease. The resulting inactive serpin-
CC protease complex is highly stable (By similarity). Variability within
CC the reactive center loop (RCL) sequences of Serpina1-related genes may
CC determine target protease specificity. {ECO:0000250}.
CC -!- MISCELLANEOUS: Murine alpha-1-antitrypsin is represented by a cluster
CC of up to 6 individual Serpina1-related genes. The precise complement of
CC Serpina1-related genes present varies according to the strain of the
CC animal.
CC -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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DR EMBL; M75720; AAC28868.1; -; mRNA.
DR EMBL; BC009818; AAH09818.1; -; mRNA.
DR EMBL; BC010984; AAH10984.1; -; mRNA.
DR EMBL; BC010988; AAH10988.1; -; mRNA.
DR EMBL; BC011041; AAH11041.1; -; mRNA.
DR EMBL; BC015266; AAH15266.1; -; mRNA.
DR EMBL; BC021325; AAH21325.1; -; mRNA.
DR EMBL; BC021780; AAH21780.1; -; mRNA.
DR EMBL; BC024108; AAH24108.1; -; mRNA.
DR EMBL; BC031707; AAH31707.1; -; mRNA.
DR EMBL; X00945; CAA25457.1; -; Genomic_DNA.
DR PIR; I49472; I49472.
DR RefSeq; NP_033271.1; NM_009245.2.
DR AlphaFoldDB; Q00896; -.
DR SMR; Q00896; -.
DR BioGRID; 423617; 11.
DR STRING; 10090.ENSMUSP00000073695; -.
DR MEROPS; I04.001; -.
DR GlyGen; Q00896; 3 sites.
DR iPTMnet; Q00896; -.
DR PhosphoSitePlus; Q00896; -.
DR REPRODUCTION-2DPAGE; Q00896; -.
DR CPTAC; non-CPTAC-3682; -.
DR jPOST; Q00896; -.
DR MaxQB; Q00896; -.
DR PaxDb; Q00896; -.
DR PeptideAtlas; Q00896; -.
DR PRIDE; Q00896; -.
DR ProteomicsDB; 285694; -.
DR DNASU; 20702; -.
DR GeneID; 20702; -.
DR KEGG; mmu:20702; -.
DR UCSC; uc007owk.1; mouse.
DR CTD; 20702; -.
DR MGI; MGI:891969; Serpina1c.
DR eggNOG; KOG2392; Eukaryota.
DR InParanoid; Q00896; -.
DR OrthoDB; 1124079at2759; -.
DR PhylomeDB; Q00896; -.
DR TreeFam; TF343201; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR Reactome; R-MMU-204005; COPII-mediated vesicle transport.
DR Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-MMU-5694530; Cargo concentration in the ER.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR BioGRID-ORCS; 20702; 2 hits in 36 CRISPR screens.
DR ChiTaRS; Serpina1c; mouse.
DR PRO; PR:Q00896; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q00896; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0002020; F:protease binding; ISO:MGI.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; ISO:MGI.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
DR GO; GO:1900004; P:negative regulation of serine-type endopeptidase activity; ISO:MGI.
DR GO; GO:0046687; P:response to chromate; ISO:MGI.
DR GO; GO:0034097; P:response to cytokine; IDA:MGI.
DR GO; GO:0010288; P:response to lead ion; ISO:MGI.
DR GO; GO:0033986; P:response to methanol; ISO: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 Glycoprotein; Protease inhibitor; Reference proteome; Secreted;
KW Serine protease inhibitor; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..412
FT /note="Alpha-1-antitrypsin 1-3"
FT /id="PRO_0000032390"
FT REGION 368..387
FT /note="RCL"
FT SITE 377..378
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957"
FT CONFLICT 1
FT /note="M -> HASGDLELADAWV (in Ref. 2; AAH10988)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="V -> A (in Ref. 1; AAC28868 and 2; AAH10988)"
FT /evidence="ECO:0000305"
FT CONFLICT 296..298
FT /note="NRR -> KRP (in Ref. 1; AAC28868)"
FT /evidence="ECO:0000305"
FT CONFLICT 359
FT /note="I -> M (in Ref. 1; AAC28868)"
FT /evidence="ECO:0000305"
FT CONFLICT 369
FT /note="V -> A (in Ref. 1; AAC28868)"
FT /evidence="ECO:0000305"
FT CONFLICT 383
FT /note="L -> V (in Ref. 1; AAC28868)"
FT /evidence="ECO:0000305"
FT CONFLICT 412
FT /note="H -> HK (in Ref. 1; AAC28868)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 412 AA; 45823 MW; FFA3BF10ABC1B8AE CRC64;
MTPSISWGLL LLAGLCCLVP SFLAEDVQET DTSQKDQSPA SHEIATNLGD FAISLYRELV
HQSNTSNIFF SPVSIATAFA MLSLGSKGDT HTQILEGLQF NLTQTSEADI HKSFQHLLQT
LNRPDSELQL STGNGLFVNN DLKLVEKFLE EAKNHYQAEV FSVNFAESEE AKKVINDFVE
KGTQGKIVEA VKKLDQDTVF ALANYILFKG KWKKPFDPEN TEEAEFHVDE STTVKVPMMT
LSGMLDVHHC STLSSWVLLM DYAGNATAVF LLPDDGKMQH LEQTLSKELI SKFLLNRRRR
LAQIHFPRLS ISGEYNLKTL MSPLGITRIF NNGADLSGIT EENAPLKLSQ AVHKAVLTID
ETGTEAAAVT VLLAVPYSMP PILRFDHPFL FIIFEEHTQS PLFVGKVVDP TH
