A1AT5_MOUSE
ID A1AT5_MOUSE Reviewed; 413 AA.
AC Q00898; Q3UJ83; Q545P1;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Alpha-1-antitrypsin 1-5;
DE AltName: Full=Alpha-1 protease inhibitor 5;
DE AltName: Full=Serine protease inhibitor 1-5;
DE AltName: Full=Serine protease inhibitor A1e;
DE Short=Serpin A1e;
DE Flags: Precursor;
GN Name=Serpina1e; Synonyms=Dom5, Spi1-5;
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=C57BL/6J; TISSUE=Liver, and Stomach;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC 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 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 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 [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-64.
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: Does not inhibit elastase or chymotrypsin. No target protease
CC has been identified to date.
CC -!- SUBCELLULAR LOCATION: Secreted {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 serpin reactive site and the active site
CC of the protease. The resulting inactive serpin-protease complex is
CC highly stable (By similarity). Variability within the reactive center
CC loop (RCL) sequences of Serpina1-related genes may determine target
CC 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 -!- SEQUENCE CAUTION:
CC Sequence=BAE27272.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M75717; AAC28866.1; -; mRNA.
DR EMBL; BC061176; AAH61176.1; -; mRNA.
DR EMBL; AK004999; BAB23733.1; -; mRNA.
DR EMBL; AK146576; BAE27272.1; ALT_INIT; mRNA.
DR CCDS; CCDS26142.1; -.
DR PIR; I49474; I49474.
DR RefSeq; NP_033273.1; NM_009247.2.
DR AlphaFoldDB; Q00898; -.
DR SMR; Q00898; -.
DR BioGRID; 203430; 1.
DR IntAct; Q00898; 1.
DR STRING; 10090.ENSMUSP00000082130; -.
DR MEROPS; I04.001; -.
DR GlyGen; Q00898; 3 sites.
DR iPTMnet; Q00898; -.
DR PhosphoSitePlus; Q00898; -.
DR CPTAC; non-CPTAC-3889; -.
DR EPD; Q00898; -.
DR jPOST; Q00898; -.
DR MaxQB; Q00898; -.
DR PaxDb; Q00898; -.
DR PeptideAtlas; Q00898; -.
DR PRIDE; Q00898; -.
DR ProteomicsDB; 285695; -.
DR DNASU; 20704; -.
DR Ensembl; ENSMUST00000085054; ENSMUSP00000082130; ENSMUSG00000072849.
DR Ensembl; ENSMUST00000122229; ENSMUSP00000113606; ENSMUSG00000072849.
DR GeneID; 20704; -.
DR KEGG; mmu:20704; -.
DR UCSC; uc007owl.1; mouse.
DR CTD; 20704; -.
DR MGI; MGI:891967; Serpina1e.
DR VEuPathDB; HostDB:ENSMUSG00000072849; -.
DR eggNOG; KOG2392; Eukaryota.
DR GeneTree; ENSGT00940000154493; -.
DR HOGENOM; CLU_023330_2_1_1; -.
DR InParanoid; Q00898; -.
DR OMA; KSTIMSW; -.
DR OrthoDB; 1124079at2759; -.
DR PhylomeDB; Q00898; -.
DR TreeFam; TF343201; -.
DR BioGRID-ORCS; 20704; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Serpina1e; mouse.
DR PRO; PR:Q00898; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q00898; protein.
DR Bgee; ENSMUSG00000072849; Expressed in liver and 46 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO: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..413
FT /note="Alpha-1-antitrypsin 1-5"
FT /id="PRO_0000032392"
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:16944957"
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:0000255"
SQ SEQUENCE 413 AA; 45891 MW; 42331F107CA06C55 CRC64;
MTPSISWCLL LLAGLCCLVP SFLAEDVQET DTSQKDQSPA SHEIATNLGD FAISLYRELV
HQSNTSNIFF SPVSIATAFA MLSLGSKGDT HTQILEGLQF NLTQTSEADI HNSFQHLLQT
LNRPDSELQL STGNGLFVNN DLKLVEKFLE EAKNHYQAEV FSVNFAESEE AKKVINDFVE
KGTQGKIVEA VKKLEQDTVF VLANYILFKG KWKKPFDPEN TKQAEFHVDE STTVKVPMMT
LSGMLDVHHC STLSSWVLLM DYAGNATAVF LLPDDGKMQH LEQTLNKELI SKFLLNRRRR
LAQIHIPRLS ISGNYNLETL MSPLGITRIF NSGADLSGIT EENAPLKLSQ AVHKAVLTID
ETGTEAAAAT VLQGGFLSMP PILHFNRPFL FIIFEEHSQS PLFVGKVVDP THK
