A1AT2_MOUSE
ID A1AT2_MOUSE Reviewed; 413 AA.
AC P22599; Q61283; Q80ZH5; Q8VC20;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Alpha-1-antitrypsin 1-2;
DE Short=AAT;
DE AltName: Full=Alpha-1 protease inhibitor 2;
DE AltName: Full=Alpha-1-antiproteinase;
DE AltName: Full=Serine protease inhibitor 1-2;
DE AltName: Full=Serine protease inhibitor A1b;
DE Short=Serpin A1b;
DE Flags: Precursor;
GN Name=Serpina1b; Synonyms=Aat2, Dom2, Spi1-2;
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=2303252; DOI=10.1016/0888-7543(90)90453-2;
RA Sifers R.N., Ledley F.D., Reed-Fourquet L., Ledbetter D.H., Ledbetter S.A.,
RA Woo S.L.C.;
RT "Complete cDNA sequence and chromosomal localization of mouse alpha 1-
RT antitrypsin.";
RL Genomics 6:100-104(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/J;
RX PubMed=12408969; DOI=10.1006/geno.2002.6864;
RA Barbour K.W., Wei F., Brannan C., Flotte T.R., Baumann H., Berger F.G.;
RT "The murine alpha(1)-proteinase inhibitor gene family: polymorphism,
RT chromosomal location, and structure.";
RL Genomics 80:515-522(2002).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 12-413.
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 [5]
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 [6]
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 [7]
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 [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-101 AND 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).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and 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).
CC -!- FUNCTION: Inhibitor of serine proteases. Its primary target is
CC elastase, but it also has a moderate affinity for plasmin and thrombin.
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; M25529; AAA37132.1; -; mRNA.
DR EMBL; AF481949; AAM47489.1; -; Genomic_DNA.
DR EMBL; BC022109; AAH22109.1; -; mRNA.
DR EMBL; BC025445; AAH25445.1; -; mRNA.
DR EMBL; BC049255; AAH49255.2; -; mRNA.
DR EMBL; M75716; AAC28865.1; -; mRNA.
DR CCDS; CCDS26138.1; -.
DR PIR; I49452; I49452.
DR PIR; I49471; I49471.
DR RefSeq; NP_033270.3; NM_009244.4.
DR AlphaFoldDB; P22599; -.
DR SMR; P22599; -.
DR BioGRID; 203428; 14.
DR IntAct; P22599; 1.
DR STRING; 10090.ENSMUSP00000093101; -.
DR MEROPS; I04.001; -.
DR GlyConnect; 799; 2 N-Linked glycans (2 sites).
DR GlyGen; P22599; 3 sites, 4 N-linked glycans (2 sites).
DR iPTMnet; P22599; -.
DR PhosphoSitePlus; P22599; -.
DR CPTAC; non-CPTAC-3556; -.
DR EPD; P22599; -.
DR jPOST; P22599; -.
DR MaxQB; P22599; -.
DR PaxDb; P22599; -.
DR PeptideAtlas; P22599; -.
DR PRIDE; P22599; -.
DR ProteomicsDB; 285946; -.
DR DNASU; 20701; -.
DR Ensembl; ENSMUST00000095450; ENSMUSP00000093101; ENSMUSG00000071178.
DR Ensembl; ENSMUST00000164454; ENSMUSP00000127266; ENSMUSG00000071178.
DR Ensembl; ENSMUST00000186166; ENSMUSP00000139941; ENSMUSG00000071178.
DR GeneID; 20701; -.
DR KEGG; mmu:20701; -.
DR UCSC; uc007owe.1; mouse.
DR CTD; 20701; -.
DR MGI; MGI:891970; Serpina1b.
DR VEuPathDB; HostDB:ENSMUSG00000071178; -.
DR eggNOG; KOG2392; Eukaryota.
DR GeneTree; ENSGT00940000154493; -.
DR HOGENOM; CLU_023330_2_1_1; -.
DR InParanoid; P22599; -.
DR OMA; ISKGCRM; -.
DR OrthoDB; 1124079at2759; -.
DR PhylomeDB; P22599; -.
DR TreeFam; TF343201; -.
DR BioGRID-ORCS; 20701; 3 hits in 33 CRISPR screens.
DR ChiTaRS; Serpina1b; mouse.
DR PRO; PR:P22599; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; P22599; protein.
DR Bgee; ENSMUSG00000071178; Expressed in left lobe of liver and 104 other tissues.
DR ExpressionAtlas; P22599; baseline and differential.
DR Genevisible; P22599; MM.
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; IMP:MGI.
DR GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
DR GO; GO:0001701; P:in utero embryonic development; IMP: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:0006487; P:protein N-linked glycosylation; IDA: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 Acute phase; Glycoprotein; Protease inhibitor; Reference proteome;
KW Secreted; Serine protease inhibitor; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000250"
FT CHAIN 25..413
FT /note="Alpha-1-antitrypsin 1-2"
FT /id="PRO_0000032389"
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:0000269|PubMed:16944957"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957"
FT CONFLICT 18
FT /note="M -> L (in Ref. 1, 2 and 3; AAH22109/AAH25445/
FT AAH49255)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="A -> G (in Ref. 1; AAA37132)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="M -> T (in Ref. 1, 2 and 3; AAH22109/AAH25445/
FT AAH49255)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="I -> T (in Ref. 1, 2 and 3; AAH22109/AAH25445/
FT AAH49255)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="A -> V (in Ref. 2; AAM47489 and 3; AAH22109/
FT AAH25445/AAH49255)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="N -> S (in Ref. 2; AAM47489 and 3; AAH22109/
FT AAH25445/AAH49255)"
FT /evidence="ECO:0000305"
FT CONFLICT 298
FT /note="R -> H (in Ref. 2; AAM47489 and 3; AAH22109/
FT AAH25445/AAH49255)"
FT /evidence="ECO:0000305"
FT CONFLICT 314
FT /note="D -> E (in Ref. 1; AAA37132)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 413 AA; 45975 MW; 92BD12B6D4768D7B CRC64;
MTPSISWGLL LLAGLCCMVP SFLAEDVQET DTSQKDQSPA SHEIATNLGD FAISLYRELV
HQSNTSNIFF SPVSIATAFA MLSLGSKGDT HTQILEGLQF NLTQTSEADI HKSFQHLLQT
LNRPDSELQL STGNGLFVNN DLKLVEKFLE EAKNHYQAEV FSVNFAESEE AKKVINDFVE
KGTQGKIVEA VKELDQDTVF ALANYILFKG KWKKPFDPEN TEEAEFHVDK STTVKVPMMM
LSGMLDVHHC SILSSWVLLM DYAGNASAVF LLPEDGKMQH LEQTLNKELI SKILLNRRRR
LVQIHIPRLS ISGDYNLKTL MSPLGITRIF NNGADLSGIT EENAPLKLSK AVHKAVLTID
ETGTEAAAAT VFEAVPMSMP PILRFDHPFL FIIFEEHTQS PIFVGKVVDP THK
