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 27-MAR-2024, entry version 191. 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=10.1016/s0888-7543(02)96864-3; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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.ENSMUSP00000072652; -. DR MEROPS; I04.001; -. DR GlyCosmos; P07758; 3 sites, No reported glycans. DR GlyGen; P07758; 5 sites, 1 O-linked glycan (2 sites). DR iPTMnet; P07758; -. DR PhosphoSitePlus; P07758; -. DR jPOST; P07758; -. DR MaxQB; P07758; -. DR PaxDb; 10090-ENSMUSP00000082132; -. DR PeptideAtlas; P07758; -. DR ProteomicsDB; 285740; -. DR DNASU; 20700; -. DR DNASU; 20703; -. DR Ensembl; ENSMUST00000085056.8; ENSMUSP00000082132.7; ENSMUSG00000066366.15. DR GeneID; 20700; -. DR KEGG; mmu:20700; -. DR UCSC; uc007owh.1; mouse. DR AGR; MGI:891971; -. DR CTD; 20700; -. 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; YDWSEMI; -. DR OrthoDB; 3218836at2759; -. DR PhylomeDB; P07758; -. DR TreeFam; TF343201; -. DR BioGRID-ORCS; 20700; 4 hits in 38 CRISPR screens. DR BioGRID-ORCS; 20703; 2 hits in 74 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 cell types or tissues. DR ExpressionAtlas; P07758; baseline and differential. DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL. 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:0006953; P:acute-phase response; IEA:UniProtKB-KW. 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 CDD; cd02056; serpinA1_A1AT; 1. DR Gene3D; 2.30.39.10; Alpha-1-antitrypsin, domain 1; 1. DR Gene3D; 3.30.497.10; Antithrombin, subunit I, domain 2; 1. DR Gene3D; 2.10.310.10; Serpins superfamily; 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:SF165; ALPHA-1-ANTITRYPSIN; 1. DR PANTHER; PTHR11461; SERINE PROTEASE INHIBITOR, SERPIN; 1. DR Pfam; PF00079; Serpin; 1. DR SMART; SM00093; SERPIN; 1. DR SUPFAM; SSF56574; Serpins; 1. DR PROSITE; PS00284; SERPIN; 1. DR Genevisible; P07758; MM. 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; FT AAH11040/AAH37007/AAH49970/AAH57982/AAH57984/AAH57989 and FT 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; FT AAH11040/AAH37007/AAH49970/AAH57982/AAH57984/AAH57989 and FT 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 //