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P07758

- A1AT1_MOUSE

UniProt

P07758 - A1AT1_MOUSE

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Protein

Alpha-1-antitrypsin 1-1

Gene

Serpina1a

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei377 – 3782Reactive bondBy similarity

GO - Molecular functioni

  1. serine-type endopeptidase inhibitor activity Source: RefGenome

GO - Biological processi

  1. acute-phase response Source: UniProtKB-KW
  2. negative regulation of endopeptidase activity Source: RefGenome
  3. protein N-linked glycosylation Source: MGI
  4. regulation of proteolysis Source: RefGenome
  5. response to cytokine Source: MGI
  6. response to peptide hormone Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Serine protease inhibitor

Keywords - Biological processi

Acute phase

Protein family/group databases

MEROPSiI04.001.

Names & Taxonomyi

Protein namesi
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 namesi
Name:Serpina1a
Synonyms:Dom1, Spi1-1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 12

Organism-specific databases

MGIiMGI:891971. Serpina1a.

Subcellular locationi

Secreted 2 Publications

GO - Cellular componenti

  1. extracellular region Source: MGI
  2. extracellular space Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424By similarityAdd
BLAST
Chaini25 – 413389Alpha-1-antitrypsin 1-1PRO_0000032388Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi64 – 641N-linked (GlcNAc...)1 Publication
Glycosylationi101 – 1011N-linked (GlcNAc...)1 Publication
Glycosylationi265 – 2651N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiP07758.
PRIDEiP07758.

PTM databases

PhosphoSiteiP07758.

Expressioni

Gene expression databases

BgeeiP07758.
ExpressionAtlasiP07758. baseline and differential.
GenevestigatoriP07758.

Interactioni

Protein-protein interaction databases

BioGridi203427. 3 interactions.
IntActiP07758. 5 interactions.
MINTiMINT-4086354.

Structurei

3D structure databases

ProteinModelPortaliP07758.
SMRiP07758. Positions 42-412.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni368 – 38720RCLAdd
BLAST

Domaini

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.By similarity

Sequence similaritiesi

Belongs to the serpin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG4826.
GeneTreeiENSGT00760000118839.
HOGENOMiHOG000238521.
HOVERGENiHBG005957.
InParanoidiP07758.
KOiK03984.
OMAiTHEDEIH.
OrthoDBiEOG7QC7W9.
PhylomeDBiP07758.
TreeFamiTF343201.

Family and domain databases

InterProiIPR023795. Serpin_CS.
IPR023796. Serpin_dom.
IPR000215. Serpin_fam.
[Graphical view]
PANTHERiPTHR11461. PTHR11461. 1 hit.
PfamiPF00079. Serpin. 1 hit.
[Graphical view]
SMARTiSM00093. SERPIN. 1 hit.
[Graphical view]
SUPFAMiSSF56574. SSF56574. 1 hit.
PROSITEiPS00284. SERPIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P07758-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTPSISWGLL LLAGLCCLVP SFLAEDVQET DTSQKDQSPA SHEIATNLGD
60 70 80 90 100
FAISLYRELV HQSNTSNIFF SPVSIATAFA MLSLGSKGDT HTQILEGLQF
110 120 130 140 150
NLTQTSEADI HKSFQHLLQT LNRPDSELQL STGNGLFVNN DLKLVEKFLE
160 170 180 190 200
EAKNHYQAEV FSVNFAESEE AKKVINDFVE KGTQGKIAEA VKKLDQDTVF
210 220 230 240 250
ALANYILFKG KWKKPFDPEN TEEAEFHVDE STTVKVPMMT LSGMLHVHHC
260 270 280 290 300
STLSSWVLLM DYAGNATAVF LLPDDGKMQH LEQTLSKELI SKFLLNRRRR
310 320 330 340 350
LAQIHFPRLS ISGEYNLKTL MSPLGITRIF NNGADLSGIT EENAPLKLSQ
360 370 380 390 400
AVHKAVLTID ETGTEAAAVT VLQMVPMSMP PILRFDHPFL FIIFEEHTQS
410
PIFLGKVVDP THK
Length:413
Mass (Da):46,003
Last modified:October 1, 1996 - v4
Checksum:i1124B2CC356232F4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti246 – 2461H → D in AAM47488. (PubMed:12408969)Curated
Sequence conflicti246 – 2461H → D in AAH11040. (PubMed:15489334)Curated
Sequence conflicti246 – 2461H → D in AAH37007. (PubMed:15489334)Curated
Sequence conflicti246 – 2461H → D in AAH49970. (PubMed:15489334)Curated
Sequence conflicti246 – 2461H → D in AAH57982. (PubMed:15489334)Curated
Sequence conflicti246 – 2461H → D in AAH57984. (PubMed:15489334)Curated
Sequence conflicti246 – 2461H → D in AAH57989. (PubMed:15489334)Curated
Sequence conflicti246 – 2461H → D in AAA51624. (PubMed:3007061)Curated
Sequence conflicti323 – 3231P → L in AAA51624. (PubMed:3007061)Curated
Sequence conflicti404 – 4041L → V in AAM47488. (PubMed:12408969)Curated
Sequence conflicti404 – 4041L → V in AAH11040. (PubMed:15489334)Curated
Sequence conflicti404 – 4041L → V in AAH37007. (PubMed:15489334)Curated
Sequence conflicti404 – 4041L → V in AAH49970. (PubMed:15489334)Curated
Sequence conflicti404 – 4041L → V in AAH57982. (PubMed:15489334)Curated
Sequence conflicti404 – 4041L → V in AAH57984. (PubMed:15489334)Curated
Sequence conflicti404 – 4041L → V in AAH57989. (PubMed:15489334)Curated
Sequence conflicti404 – 4041L → V in AAA51624. (PubMed:3007061)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS26140.1.
PIRiI49470.
RefSeqiNP_033269.1. NM_009243.4.
UniGeneiMm.439692.

Genome annotation databases

EnsembliENSMUST00000085056; ENSMUSP00000082132; ENSMUSG00000066366.
GeneIDi20700.
KEGGimmu:20700.
UCSCiuc007owh.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS26140.1.
PIRi I49470.
RefSeqi NP_033269.1. NM_009243.4.
UniGenei Mm.439692.

3D structure databases

ProteinModelPortali P07758.
SMRi P07758. Positions 42-412.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 203427. 3 interactions.
IntActi P07758. 5 interactions.
MINTi MINT-4086354.

Protein family/group databases

MEROPSi I04.001.

PTM databases

PhosphoSitei P07758.

Proteomic databases

PaxDbi P07758.
PRIDEi P07758.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000085056 ; ENSMUSP00000082132 ; ENSMUSG00000066366 .
GeneIDi 20700.
KEGGi mmu:20700.
UCSCi uc007owh.1. mouse.

Organism-specific databases

CTDi 20700.
MGIi MGI:891971. Serpina1a.

Phylogenomic databases

eggNOGi COG4826.
GeneTreei ENSGT00760000118839.
HOGENOMi HOG000238521.
HOVERGENi HBG005957.
InParanoidi P07758.
KOi K03984.
OMAi THEDEIH.
OrthoDBi EOG7QC7W9.
PhylomeDBi P07758.
TreeFami TF343201.

Miscellaneous databases

NextBioi 299247.
PROi P07758.
SOURCEi Search...

Gene expression databases

Bgeei P07758.
ExpressionAtlasi P07758. baseline and differential.
Genevestigatori P07758.

Family and domain databases

InterProi IPR023795. Serpin_CS.
IPR023796. Serpin_dom.
IPR000215. Serpin_fam.
[Graphical view ]
PANTHERi PTHR11461. PTHR11461. 1 hit.
Pfami PF00079. Serpin. 1 hit.
[Graphical view ]
SMARTi SM00093. SERPIN. 1 hit.
[Graphical view ]
SUPFAMi SSF56574. SSF56574. 1 hit.
PROSITEi PS00284. SERPIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    Strain: C57BL/6.
    Tissue: Plasma.

Entry informationi

Entry nameiA1AT1_MOUSE
AccessioniPrimary (citable) accession number: P07758
Secondary accession number(s): Q3UJ47
, Q80YB8, Q8JZV6, Q91XB8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: October 1, 1996
Last modified: October 29, 2014
This is version 133 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3