A1AT1_MOUSE
ID A1AT1_MOUSE Reviewed; 413 AA.
AC P07758; Q3UJ47; Q80YB8; Q8JZV6; Q91XB8;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 4.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Alpha-1-antitrypsin 1-1;
DE Short=AAT;
DE AltName: Full=Alpha-1 protease inhibitor 1;
DE AltName: Full=Alpha-1-antiproteinase;
DE AltName: Full=Serine protease inhibitor 1-1;
DE AltName: Full=Serine protease inhibitor A1a;
DE Short=Serpin A1a;
DE Flags: Precursor;
GN Name=Serpina1a; Synonyms=Dom1, Spi1-1;
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 [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=C57BL/6J; TISSUE=Amnion;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 211-413.
RX PubMed=3007061; DOI=10.1089/dna.1986.5.29;
RA Krauter K.S., Citron B.A., Hsu M.T., Powell D., Darnell J.E. Jr.;
RT "Isolation and characterization of the alpha 1-antitrypsin gene of mice.";
RL DNA 5:29-36(1986).
RN [6]
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 [7]
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 [8]
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 [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-64 AND ASN-101.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=17330941; DOI=10.1021/pr0604559;
RA Bernhard O.K., Kapp E.A., Simpson R.J.;
RT "Enhanced analysis of the mouse plasma proteome using cysteine-containing
RT tryptic glycopeptides.";
RL J. Proteome Res. 6:987-995(2007).
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; M75721; AAC28869.1; -; mRNA.
DR EMBL; AF481949; AAM47488.1; -; Genomic_DNA.
DR EMBL; AK146619; BAE27308.1; -; mRNA.
DR EMBL; BC011040; AAH11040.1; -; mRNA.
DR EMBL; BC037007; AAH37007.2; -; mRNA.
DR EMBL; BC049970; AAH49970.2; -; mRNA.
DR EMBL; BC057982; AAH57982.1; -; mRNA.
DR EMBL; BC057984; AAH57984.1; -; mRNA.
DR EMBL; BC057989; AAH57989.1; -; mRNA.
DR EMBL; AH002568; AAA51624.1; -; mRNA.
DR CCDS; CCDS26140.1; -.
DR PIR; I49470; I49470.
DR RefSeq; NP_033269.1; NM_009243.4.
DR RefSeq; XP_017174431.1; XM_017318942.1.
DR AlphaFoldDB; P07758; -.
DR SMR; P07758; -.
DR BioGRID; 203427; 4.
DR STRING; 10090.ENSMUSP00000082132; -.
DR MEROPS; I04.001; -.
DR GlyGen; P07758; 3 sites.
DR iPTMnet; P07758; -.
DR PhosphoSitePlus; P07758; -.
DR jPOST; P07758; -.
DR MaxQB; P07758; -.
DR PaxDb; P07758; -.
DR PeptideAtlas; P07758; -.
DR PRIDE; P07758; -.
DR ProteomicsDB; 285740; -.
DR DNASU; 20700; -.
DR DNASU; 20703; -.
DR Ensembl; ENSMUST00000085056; ENSMUSP00000082132; ENSMUSG00000066366.
DR GeneID; 20700; -.
DR GeneID; 20703; -.
DR KEGG; mmu:20700; -.
DR UCSC; uc007owh.1; mouse.
DR CTD; 20700; -.
DR CTD; 20703; -.
DR MGI; MGI:891971; Serpina1a.
DR VEuPathDB; HostDB:ENSMUSG00000066366; -.
DR eggNOG; KOG2392; Eukaryota.
DR GeneTree; ENSGT00940000154493; -.
DR HOGENOM; CLU_023330_2_1_1; -.
DR InParanoid; P07758; -.
DR OMA; NMIVIST; -.
DR OrthoDB; 1124079at2759; -.
DR PhylomeDB; P07758; -.
DR TreeFam; TF343201; -.
DR BioGRID-ORCS; 20700; 4 hits in 33 CRISPR screens.
DR BioGRID-ORCS; 20703; 2 hits in 69 CRISPR screens.
DR ChiTaRS; Serpina1a; mouse.
DR PRO; PR:P07758; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; P07758; protein.
DR Bgee; ENSMUSG00000066366; Expressed in left lobe of liver and 92 other tissues.
DR ExpressionAtlas; P07758; baseline and differential.
DR Genevisible; P07758; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005576; C:extracellular region; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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:0006487; P:protein N-linked glycosylation; IDA: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 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 1-1"
FT /id="PRO_0000032388"
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:0000269|PubMed:17330941"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17330941"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 246
FT /note="H -> D (in Ref. 2; AAM47488, 4; AAH11040/AAH37007/
FT AAH49970/AAH57982/AAH57984/AAH57989 and 5; AAA51624)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="P -> L (in Ref. 5; AAA51624)"
FT /evidence="ECO:0000305"
FT CONFLICT 404
FT /note="L -> V (in Ref. 2; AAM47488, 4; AAH11040/AAH37007/
FT AAH49970/AAH57982/AAH57984/AAH57989 and 5; AAA51624)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 413 AA; 46003 MW; 1124B2CC356232F4 CRC64;
MTPSISWGLL LLAGLCCLVP SFLAEDVQET DTSQKDQSPA SHEIATNLGD FAISLYRELV
HQSNTSNIFF SPVSIATAFA MLSLGSKGDT HTQILEGLQF NLTQTSEADI HKSFQHLLQT
LNRPDSELQL STGNGLFVNN DLKLVEKFLE EAKNHYQAEV FSVNFAESEE AKKVINDFVE
KGTQGKIAEA VKKLDQDTVF ALANYILFKG KWKKPFDPEN TEEAEFHVDE STTVKVPMMT
LSGMLHVHHC STLSSWVLLM DYAGNATAVF LLPDDGKMQH LEQTLSKELI SKFLLNRRRR
LAQIHFPRLS ISGEYNLKTL MSPLGITRIF NNGADLSGIT EENAPLKLSQ AVHKAVLTID
ETGTEAAAVT VLQMVPMSMP PILRFDHPFL FIIFEEHTQS PIFLGKVVDP THK
