A1AT6_MOUSE
ID A1AT6_MOUSE Reviewed; 411 AA.
AC Q9DCQ7; Q3LFT1; Q3TNC2;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Alpha-1-antitrypsin 1-6 {ECO:0000250|UniProtKB:P01009};
DE AltName: Full=Alpha-1 protease inhibitor 6 {ECO:0000250|UniProtKB:P01009};
DE AltName: Full=Alpha-1-antiproteinase {ECO:0000250|UniProtKB:P01009};
DE AltName: Full=Serine protease inhibitor 1-6;
DE AltName: Full=Serine protease inhibitor A1f {ECO:0000303|PubMed:16707773};
DE Short=Serpin A1f;
DE Flags: Precursor;
GN Name=Serpina1f {ECO:0000312|MGI:MGI:1915598};
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] {ECO:0000305, ECO:0000312|EMBL:BAE45638.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND INDUCTION.
RC TISSUE=Epididymis {ECO:0000312|EMBL:BAE45638.1};
RX PubMed=16707773; DOI=10.1095/biolreprod.105.048058;
RA Yamazaki K., Adachi T., Sato K., Yanagisawa Y., Fukata H., Seki N.,
RA Mori C., Komiyama M.;
RT "Identification and characterization of novel and unknown mouse epididymis-
RT specific genes by complementary DNA microarray technology.";
RL Biol. Reprod. 75:462-468(2006).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAB22199.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB22199.1};
RC TISSUE=Kidney {ECO:0000312|EMBL:BAB22199.1};
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).
CC -!- FUNCTION: Inhibitor of serine proteases.
CC {ECO:0000250|UniProtKB:P07758}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P07758}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:16141072};
CC IsoId=Q9DCQ7-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:16141072};
CC IsoId=Q9DCQ7-2; Sequence=VSP_052895;
CC -!- TISSUE SPECIFICITY: Expressed predominantly in epididymis where it is
CC found in the epithelial cells of the caput, corpus and cauda
CC epididymis. {ECO:0000269|PubMed:16707773}.
CC -!- DEVELOPMENTAL STAGE: Expression increases gradually from post-natal day
CC 1 to week 2, increases significantly from week 2 to week 4 and remains
CC high thereafter. {ECO:0000269|PubMed:16707773}.
CC -!- INDUCTION: Expression decreases following castration. Administration of
CC testosterone restores expression levels. {ECO:0000269|PubMed:16707773}.
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. Variability within the reactive
CC center loop (RCL) sequences of Serpina1-related genes may determine
CC target protease specificity (By similarity).
CC {ECO:0000250|UniProtKB:P01009, ECO:0000250|UniProtKB:P07758}.
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. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the serpin family. {ECO:0000255}.
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DR EMBL; AB233454; BAE45638.1; -; mRNA.
DR EMBL; AK002574; BAB22199.1; -; mRNA.
DR EMBL; AK165409; BAE38167.1; -; mRNA.
DR CCDS; CCDS26137.1; -. [Q9DCQ7-1]
DR CCDS; CCDS49155.1; -. [Q9DCQ7-2]
DR RefSeq; NP_001158214.1; NM_001164742.1.
DR RefSeq; NP_080963.2; NM_026687.2.
DR AlphaFoldDB; Q9DCQ7; -.
DR SMR; Q9DCQ7; -.
DR BioGRID; 212815; 1.
DR STRING; 10090.ENSMUSP00000021490; -.
DR MEROPS; I04.968; -.
DR GlyGen; Q9DCQ7; 4 sites.
DR PhosphoSitePlus; Q9DCQ7; -.
DR PaxDb; Q9DCQ7; -.
DR PRIDE; Q9DCQ7; -.
DR ProteomicsDB; 285741; -. [Q9DCQ7-1]
DR ProteomicsDB; 285742; -. [Q9DCQ7-2]
DR DNASU; 68348; -.
DR GeneID; 68348; -.
DR KEGG; mmu:68348; -.
DR CTD; 68348; -.
DR MGI; MGI:1915598; Serpina1f.
DR eggNOG; KOG2392; Eukaryota.
DR InParanoid; Q9DCQ7; -.
DR OrthoDB; 1124079at2759; -.
DR PhylomeDB; Q9DCQ7; -.
DR BioGRID-ORCS; 68348; 3 hits in 74 CRISPR screens.
DR PRO; PR:Q9DCQ7; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9DCQ7; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO: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:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Alternative splicing; Glycoprotein; Protease inhibitor; Reference proteome;
KW Secreted; Serine protease inhibitor; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..411
FT /note="Alpha-1-antitrypsin 1-6"
FT /evidence="ECO:0000255"
FT /id="PRO_0000347280"
FT SITE 376..377
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 89
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 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 210..264
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052895"
FT CONFLICT 127
FT /note="T -> P (in Ref. 1; BAE45638 and 2; BAE38167)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="E -> D (in Ref. 1; BAE45638 and 2; BAE38167)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="I -> K (in Ref. 1; BAE45638 and 2; BAE38167)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="A -> E (in Ref. 2; BAE38167)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="A -> G (in Ref. 1; BAE45638)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="G -> E (in Ref. 1; BAE45638)"
FT /evidence="ECO:0000305"
FT CONFLICT 281
FT /note="K -> R (in Ref. 2; BAE38167)"
FT /evidence="ECO:0000305"
FT CONFLICT 307
FT /note="I -> T (in Ref. 1; BAE45638)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="N -> D (in Ref. 1; BAE45638)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 411 AA; 46337 MW; C33B7876BA07367E CRC64;
MTTPFSSHGL LLLVGLCCLL LITKTKHEKL YEDPSIDPFQ CRKVALTICN VSITLFKKMA
QLSGNGNILF SPIRVIAAIS MLSLGSNGNL SKHILETLRF NKTGLPEAEI HKCFWYLLHS
IHQTEETSSL QTGSSVFIHQ DLTSVDKFVK GVKELYHSDM ISINFTDSSQ AKTQINNYVM
EISQKAIVNI VKNLESDTFL AVVNYIIWNA KLDSNFGCRS VKVKDYHLGY GMTIKVPMIH
NMAMHYLFRV GDLSSTVLML TLLTGNFATY FIIPDPGKMQ KVEQSLTYPH FRRMRRQLLT
RLVDLEIPEL SLSETHDLES MMSLLGITYV FNSGTNSSDM NDTLQKSFKV VSKAVLTIDE
KGSKPSTNSC FKKLGSTDMG RMQLNRPFLI FIQDHTNDVP LFLGRVVNPQ N
