P07758 (A1AT1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alpha-1-antitrypsin 1-1
Short name=AAT

Alternative name(s):
Alpha-1 protease inhibitor 1
Alpha-1-antiproteinase
Serine protease inhibitor 1-1
Serine protease inhibitor A1a
Short name=Serpin A1a

Gene names

Name:	Serpina1a
Synonyms:	Dom1, Spi1-1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	413 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin. Ref.6 Ref.7
Subcellular location	Secreted Ref.6 Ref.7.
Domain	The reactive center loop (RCL) extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site within the RCL, establishing a covalent linkage between the carboxyl group of the serpin reactive site and the serine hydroxyl of the protease. The resulting inactive serpin-protease complex is highly stable By similarity. Variability within the reactive center loop (RCL) sequences of Serpina1-related genes may determine target protease specificity.
Miscellaneous	Murine alpha-1-antitrypsin is represented by a cluster of up to 6 individual Serpina1-related genes. The precise complement of Serpina1-related genes present varies according to the strain of the animal.
Sequence similarities	Belongs to the serpin family.

Ontologies

Keywords
Biological process	Acute phase
Cellular component	Secreted
Domain	Signal
Molecular function	Protease inhibitor Serine protease inhibitor
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	acute-phase response Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	serine-type endopeptidase inhibitor activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 24	24	By similarity
	Chain	25 – 413	389	Alpha-1-antitrypsin 1-1		PRO_0000032388
Regions
	Region	368 – 387	20	RCL
Sites
	Site	377 – 378	2	Reactive bond By similarity
Amino acid modifications
	Glycosylation	64	1	N-linked (GlcNAc...) Ref.9
	Glycosylation	101	1	N-linked (GlcNAc...) Ref.9
	Glycosylation	265	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	246	1	H → D in AAM47488. Ref.2
	Sequence conflict	246	1	H → D in AAH11040. Ref.4
	Sequence conflict	246	1	H → D in AAH37007. Ref.4
	Sequence conflict	246	1	H → D in AAH49970. Ref.4
	Sequence conflict	246	1	H → D in AAH57982. Ref.4
	Sequence conflict	246	1	H → D in AAH57984. Ref.4
	Sequence conflict	246	1	H → D in AAH57989. Ref.4
	Sequence conflict	246	1	H → D in AAA51624. Ref.5
	Sequence conflict	323	1	P → L in AAA51624. Ref.5
	Sequence conflict	404	1	L → V in AAM47488. Ref.2
	Sequence conflict	404	1	L → V in AAH11040. Ref.4
	Sequence conflict	404	1	L → V in AAH37007. Ref.4
	Sequence conflict	404	1	L → V in AAH49970. Ref.4
	Sequence conflict	404	1	L → V in AAH57982. Ref.4
	Sequence conflict	404	1	L → V in AAH57984. Ref.4
	Sequence conflict	404	1	L → V in AAH57989. Ref.4
	Sequence conflict	404	1	L → V in AAA51624. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P07758 [UniParc]. Last modified October 1, 1996. Version 4. Checksum: 1124B2CC356232F4	FASTA	413	46,003
	10 20 30 40 50 60 MTPSISWGLL LLAGLCCLVP SFLAEDVQET DTSQKDQSPA SHEIATNLGD FAISLYRELV 70 80 90 100 110 120 HQSNTSNIFF SPVSIATAFA MLSLGSKGDT HTQILEGLQF NLTQTSEADI HKSFQHLLQT 130 140 150 160 170 180 LNRPDSELQL STGNGLFVNN DLKLVEKFLE EAKNHYQAEV FSVNFAESEE AKKVINDFVE 190 200 210 220 230 240 KGTQGKIAEA VKKLDQDTVF ALANYILFKG KWKKPFDPEN TEEAEFHVDE STTVKVPMMT 250 260 270 280 290 300 LSGMLHVHHC STLSSWVLLM DYAGNATAVF LLPDDGKMQH LEQTLSKELI SKFLLNRRRR 310 320 330 340 350 360 LAQIHFPRLS ISGEYNLKTL MSPLGITRIF NNGADLSGIT EENAPLKLSQ AVHKAVLTID 370 380 390 400 410 ETGTEAAAVT VLQMVPMSMP PILRFDHPFL FIIFEEHTQS PIFLGKVVDP THK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Multiple murine alpha 1-protease inhibitor genes show unusual evolutionary divergence." Borriello F., Krauter K.S. Proc. Natl. Acad. Sci. U.S.A. 88:9417-9421(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C57BL/6. Tissue: Liver.
[2]	"The murine alpha(1)-proteinase inhibitor gene family: polymorphism, chromosomal location, and structure." Barbour K.W., Wei F., Brannan C., Flotte T.R., Baumann H., Berger F.G. Genomics 80:515-522(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 129/J.
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Amnion.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Liver.
[5]	"Isolation and characterization of the alpha 1-antitrypsin gene of mice." Krauter K.S., Citron B.A., Hsu M.T., Powell D., Darnell J.E. Jr. DNA 5:29-36(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 211-413.
[6]	"The expression and characterization of five recombinant murine alpha 1-protease inhibitor proteins." Paterson T., Moore S. Biochem. Biophys. Res. Commun. 219:64-69(1996) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[7]	"Functional diversification during evolution of the murine alpha(1)-proteinase inhibitor family: role of the hypervariable reactive center loop." Barbour K.W., Goodwin R.L., Guillonneau F., Wang Y., Baumann H., Berger F.G. Mol. Biol. Evol. 19:718-727(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, REGION RCL.
[8]	"A review and comparison of the murine alpha1-antitrypsin and alpha1-antichymotrypsin multigene clusters with the human clade A serpins." Forsyth S., Horvath A., Coughlin P. Genomics 81:336-345(2003) [PubMed] [Europe PMC] [Abstract] Cited for: GENE FAMILY, NOMENCLATURE.
[9]	"Enhanced analysis of the mouse plasma proteome using cysteine-containing tryptic glycopeptides." Bernhard O.K., Kapp E.A., Simpson R.J. J. Proteome Res. 6:987-995(2007) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-64 AND ASN-101, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Plasma.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M75721 mRNA. Translation: AAC28869.1. AF481949 Genomic DNA. Translation: AAM47488.1. AK146619 mRNA. Translation: BAE27308.1. BC011040 mRNA. Translation: AAH11040.1. BC037007 mRNA. Translation: AAH37007.2. BC049970 mRNA. Translation: AAH49970.2. BC057982 mRNA. Translation: AAH57982.1. BC057984 mRNA. Translation: AAH57984.1. BC057989 mRNA. Translation: AAH57989.1. AH002568 mRNA. Translation: AAA51624.1.
IPI	IPI00406302.
PIR	I49470.
RefSeq	NP_033269.1. NM_009243.4. XP_003945711.1. XM_003945662.1. XP_003945714.1. XM_003945665.1. XP_003945715.1. XM_003945666.1.
UniGene	Mm.439692.
3D structure databases
ProteinModelPortal	P07758.
SMR	P07758. Positions 42-412.
ModBase	Search...
PTM databases
PhosphoSite	P07758.
Proteomic databases
PaxDb	P07758.
PRIDE	P07758.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000072876; ENSMUSP00000072652; ENSMUSG00000066366. ENSMUST00000085056; ENSMUSP00000082132; ENSMUSG00000066366.
GeneID	20700. 20703.
KEGG	mmu:20700. mmu:20703.
UCSC	uc007owe.1. mouse.
Organism-specific databases
CTD	20700. 20703.
MGI	MGI:891971. Serpina1a.
Phylogenomic databases
eggNOG	COG4826.
GeneTree	ENSGT00700000104184.
HOGENOM	HOG000238521.
HOVERGEN	HBG005957.
InParanoid	P07758.
KO	K03984.
OMA	HEDEIHE.
OrthoDB	EOG4FR0S4.
Gene expression databases
ArrayExpress	P07758.
Bgee	P07758.
Genevestigator	P07758.
GermOnline	ENSMUSG00000066366. Mus musculus.
Family and domain databases
InterPro	IPR023795. Protease_inhib_I4_serpin_CS. IPR023796. Serpin_dom. IPR000215. Serpin_fam. [Graphical view]
PANTHER	PTHR11461. PTHR11461. 1 hit.
Pfam	PF00079. Serpin. 1 hit. [Graphical view]
SMART	SM00093. SERPIN. 1 hit. [Graphical view]
SUPFAM	SSF56574. Prot_inh_serpin. 1 hit.
PROSITE	PS00284. SERPIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	299247.
SOURCE	Search...

Entry information

Entry name

A1AT1_MOUSE

Accession

Primary (citable) accession number: P07758
Secondary accession number(s): Q3UJ47 , Q80YB8, Q8JZV6, Q91XB8

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 119 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program