A1AT4_MOUSE
ID A1AT4_MOUSE Reviewed; 413 AA.
AC Q00897;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Alpha-1-antitrypsin 1-4;
DE AltName: Full=Alpha-1 protease inhibitor 4;
DE AltName: Full=Serine protease inhibitor 1-4;
DE AltName: Full=Serine protease inhibitor A1d;
DE Short=Serpin A1d;
DE Flags: Precursor;
GN Name=Serpina1d; Synonyms=Dom4, Spi1-4;
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=Kidney;
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 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 [4]
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 [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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Liver, Lung, 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. 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; M75718; AAC28867.1; -; mRNA.
DR EMBL; AK002537; BAB22173.1; -; mRNA.
DR CCDS; CCDS26139.1; -.
DR PIR; I49473; I49473.
DR RefSeq; NP_033272.1; NM_009246.3.
DR AlphaFoldDB; Q00897; -.
DR SMR; Q00897; -.
DR STRING; 10090.ENSMUSP00000077909; -.
DR MEROPS; I04.001; -.
DR GlyGen; Q00897; 3 sites.
DR iPTMnet; Q00897; -.
DR PhosphoSitePlus; Q00897; -.
DR CPTAC; non-CPTAC-3529; -.
DR CPTAC; non-CPTAC-3530; -.
DR EPD; Q00897; -.
DR jPOST; Q00897; -.
DR MaxQB; Q00897; -.
DR PaxDb; Q00897; -.
DR PeptideAtlas; Q00897; -.
DR PRIDE; Q00897; -.
DR ProteomicsDB; 285947; -.
DR DNASU; 20703; -.
DR Ensembl; ENSMUST00000078869; ENSMUSP00000077909; ENSMUSG00000071177.
DR GeneID; 20703; -.
DR KEGG; mmu:20703; -.
DR UCSC; uc007owg.1; mouse.
DR CTD; 20703; -.
DR MGI; MGI:891968; Serpina1d.
DR VEuPathDB; HostDB:ENSMUSG00000071177; -.
DR eggNOG; KOG2392; Eukaryota.
DR GeneTree; ENSGT00940000154493; -.
DR HOGENOM; CLU_023330_2_1_1; -.
DR InParanoid; Q00897; -.
DR OMA; YQEPASW; -.
DR OrthoDB; 1124079at2759; -.
DR PhylomeDB; Q00897; -.
DR TreeFam; TF343201; -.
DR BioGRID-ORCS; 20703; 2 hits in 69 CRISPR screens.
DR ChiTaRS; Serpina1d; mouse.
DR PRO; PR:Q00897; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q00897; protein.
DR Bgee; ENSMUSG00000071177; Expressed in proximal tubule and 36 other tissues.
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..413
FT /note="Alpha-1-antitrypsin 1-4"
FT /id="PRO_0000032391"
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:0000255"
SQ SEQUENCE 413 AA; 45998 MW; D8A90477F371A902 CRC64;
MTPSISWSLL LLAGLCCLVP SFLAEDVQET DTSQKDQSPA SHEIATNLGD FALRLYRELV
HQSNTSNIFF SPVSIATAFA MLSLGSKGDT HTQILEGLQF NLTQTSEADI HKSFQHLLQT
LNRPDSELQL STGNGLFVNN DLKLVEKFLE EAKNHYQAEV FSVNFAESEE AKKVINDFVE
KGTQGKIVEA VKKLDQDTVF ALANYILFKG KWKQPFDPEN TEEAEFHVDE STTVKVPMMT
LSGMLDVHHC SMLSSWVLLM DYAGNTTAVF LLPDDGKMQH LEQTLNKELI SQFLLNRRRS
DAQIHIPRLS ISGNYNLKTL MSPLGITRIF NNGADLSGIT EENAPLKLSK AVHKAVLTID
ETGTEAAAAT VLQVATYSMP PIVRFDHPFL FIIFEEHTQS PIFVGKVVDP THK
