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P07758 (A1AT1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length413 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 processAcute phase
   Cellular componentSecreted
   DomainSignal
   Molecular functionProtease inhibitor
Serine protease inhibitor
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processacute-phase response

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular space

Inferred from electronic annotation. Source: InterPro

   Molecular_functionserine-type endopeptidase inhibitor activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 By similarity
Chain25 – 413389Alpha-1-antitrypsin 1-1
PRO_0000032388

Regions

Region368 – 38720RCL

Sites

Site377 – 3782Reactive bond By similarity

Amino acid modifications

Glycosylation641N-linked (GlcNAc...) Ref.9
Glycosylation1011N-linked (GlcNAc...) Ref.9
Glycosylation2651N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict2461H → D in AAM47488. Ref.2
Sequence conflict2461H → D in AAH11040. Ref.4
Sequence conflict2461H → D in AAH37007. Ref.4
Sequence conflict2461H → D in AAH49970. Ref.4
Sequence conflict2461H → D in AAH57982. Ref.4
Sequence conflict2461H → D in AAH57984. Ref.4
Sequence conflict2461H → D in AAH57989. Ref.4
Sequence conflict2461H → D in AAA51624. Ref.5
Sequence conflict3231P → L in AAA51624. Ref.5
Sequence conflict4041L → V in AAM47488. Ref.2
Sequence conflict4041L → V in AAH11040. Ref.4
Sequence conflict4041L → V in AAH37007. Ref.4
Sequence conflict4041L → V in AAH49970. Ref.4
Sequence conflict4041L → V in AAH57982. Ref.4
Sequence conflict4041L → V in AAH57984. Ref.4
Sequence conflict4041L → V in AAH57989. Ref.4
Sequence conflict4041L → V in AAA51624. Ref.5

Sequences

Sequence LengthMass (Da)Tools
P07758 [UniParc].

Last modified October 1, 1996. Version 4.
Checksum: 1124B2CC356232F4

FASTA41346,003
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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.
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.
PIRI49470.
RefSeqNP_033269.1. NM_009243.4.
UniGeneMm.439692.

3D structure databases

ProteinModelPortalP07758.
SMRP07758. Positions 42-412.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid203427. 3 interactions.
IntActP07758. 5 interactions.
MINTMINT-4086354.

Protein family/group databases

MEROPSI04.001.

PTM databases

PhosphoSiteP07758.

Proteomic databases

PaxDbP07758.
PRIDEP07758.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000072876; ENSMUSP00000072652; ENSMUSG00000066366.
ENSMUST00000085056; ENSMUSP00000082132; ENSMUSG00000066366.
GeneID20700.
KEGGmmu:20700.
mmu:20703.
UCSCuc007owh.1. mouse.

Organism-specific databases

CTD20700.
20703.
MGIMGI:891971. Serpina1a.

Phylogenomic databases

eggNOGCOG4826.
GeneTreeENSGT00750000117448.
HOGENOMHOG000238521.
HOVERGENHBG005957.
InParanoidP07758.
KOK03984.
OMAGLFINEN.
OrthoDBEOG7QC7W9.
PhylomeDBP07758.
TreeFamTF343201.

Gene expression databases

ArrayExpressP07758.
BgeeP07758.
GenevestigatorP07758.

Family and domain databases

InterProIPR023795. Serpin_CS.
IPR023796. Serpin_dom.
IPR000215. Serpin_fam.
[Graphical view]
PANTHERPTHR11461. PTHR11461. 1 hit.
PfamPF00079. Serpin. 1 hit.
[Graphical view]
SMARTSM00093. SERPIN. 1 hit.
[Graphical view]
SUPFAMSSF56574. SSF56574. 1 hit.
PROSITEPS00284. SERPIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio299247.
PROP07758.
SOURCESearch...

Entry information

Entry nameA1AT1_MOUSE
AccessionPrimary (citable) accession number: P07758
Secondary accession number(s): Q3UJ47 expand/collapse secondary AC list , Q80YB8, Q8JZV6, Q91XB8
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 128 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot