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P17475 (A1AT_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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-antiproteinase
Alternative name(s):
Alpha-1-antitrypsin
Alpha-1-proteinase inhibitor
Serpin A1
Gene names
Name:Serpina1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length411 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. The primary target is elastase, but also has a moderate affinity for plasmin and thrombin.

Subcellular location

Secreted.

Tissue specificity

Plasma. Ref.3

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.

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
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processacute-phase response

Inferred from electronic annotation. Source: UniProtKB-KW

inflammatory response

Inferred from expression pattern PubMed 20118217. Source: RGD

negative regulation of endopeptidase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of serine-type endopeptidase activity

Inferred from direct assay PubMed 19240864. Source: RGD

regulation of proteolysis

Inferred from Biological aspect of Ancestor. Source: RefGenome

response to chromate

Inferred from direct assay PubMed 12122574. Source: RGD

response to cytokine

Inferred from expression pattern PubMed 9533938. Source: RGD

response to estradiol

Inferred from expression pattern PubMed 1466268. Source: RGD

response to hypoxia

Inferred from expression pattern PubMed 12121987. Source: RGD

response to inorganic substance

Inferred from expression pattern PubMed 9950889. Source: RGD

response to lead ion

Inferred from direct assay PubMed 11392791. Source: RGD

response to lipopolysaccharide

Inferred from expression pattern PubMed 1466268. Source: RGD

response to methanol

Inferred from direct assay PubMed 10478824. Source: RGD

response to organic cyclic compound

Inferred from expression pattern PubMed 8502664. Source: RGD

response to triglyceride

Inferred from expression pattern PubMed 10362649. Source: RGD

   Cellular_componentendoplasmic reticulum

Inferred from electronic annotation. Source: Ensembl

extracellular space

Inferred from direct assay PubMed 17634200. Source: RGD

   Molecular_functionendopeptidase inhibitor activity

Inferred from direct assay PubMed 11917148. Source: RGD

protein binding

Inferred from physical interaction PubMed 11917148. Source: RGD

serine-type endopeptidase inhibitor activity

Inferred from direct assay PubMed 19240864. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Ref.3
Chain25 – 411387Alpha-1-antiproteinase
PRO_0000032398

Regions

Region367 – 38620RCL

Sites

Site376 – 3772Reactive bond

Amino acid modifications

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

Experimental info

Sequence conflict141A → G in BAA00579. Ref.1
Sequence conflict141A → G in AAH78824. Ref.2
Sequence conflict841L → V in BAA00579. Ref.1
Sequence conflict2471M → I in CAA34349. Ref.5
Sequence conflict2481H → Y in BAA00579. Ref.1
Sequence conflict3181K → N in BAA00579. Ref.1
Sequence conflict3221S → D in CAA34349. Ref.5

Sequences

Sequence LengthMass (Da)Tools
P17475 [UniParc].

Last modified February 1, 1991. Version 2.
Checksum: B4245CFE21C5C761

FASTA41146,136
        10         20         30         40         50         60 
MAPSISRGLL LLAALCCLAP SFLAEDAQET DTSQQDQSPT YRKISSNLAD FAFSLYRELV 

        70         80         90        100        110        120 
HQSNTSNIFF SPMSITTAFA MLSLGSKGDT RKQILEGLEF NLTQIPEADI HKAFHHLLQT 

       130        140        150        160        170        180 
LNRPDSELQL NTGNGLFVNK NLKLVEKFLE EVKNNYHSEA FSVNFADSEE AKKVINDYVE 

       190        200        210        220        230        240 
KGTQGKIVDL MKQLDEDTVF ALVNYIFFKG KWKRPFNPEH TRDADFHVDK STTVKVPMMN 

       250        260        270        280        290        300 
RLGMFDMHYC STLSSWVLMM DYLGNATAIF LLPDDGKMQH LEQTLTKDLI SRFLLNRQTR 

       310        320        330        340        350        360 
SAILYFPKLS ISGTYNLKTL LSSLGITRVF NNDADLSGIT EDAPLKLSQA VHKAVLTLDE 

       370        380        390        400        410 
RGTEAAGATV VEAVPMSLPP QVKFDHPFIF MIVESETQSP LFVGKVIDPT R 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and sequencing of the cDNA of rat alpha 1-protease inhibitor and its expression in COS-1 cells."
Misumi Y., Sohda M., Ohkubo K., Takami N., Oda K., Ikehara Y.
J. Biochem. 108:230-234(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Wistar.
Tissue: Liver.
[2]"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].
Tissue: Testis.
[3]"Molecular cloning and primary structure of rat alpha 1-antitrypsin."
Chao S., Chai K.X., Chao L., Chao J.
Biochemistry 29:323-329(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-411, PROTEIN SEQUENCE OF 25-57, TISSUE SPECIFICITY.
Tissue: Liver.
[4]Lubec G., Afjehi-Sadat L., Kang S.U., Lubec S.
Submitted (SEP-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 44-57; 148-172; 174-181; 187-192; 278-287 AND 301-328, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Brain and Spinal cord.
[5]Flink I.L., Bailey T., Morkin E.
Submitted (AUG-1989) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 188-389.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D00675 mRNA. Translation: BAA00579.1.
BC078824 mRNA. Translation: AAH78824.1.
M32247 mRNA. Translation: AAA40788.1.
X16273 mRNA. Translation: CAA34349.1.
PIRITRT. A33892.
RefSeqNP_071964.2. NM_022519.2.
XP_006240518.1. XM_006240456.1.
XP_006240519.1. XM_006240457.1.
UniGeneRn.1419.

3D structure databases

ProteinModelPortalP17475.
SMRP17475. Positions 39-411.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000012577.

Protein family/group databases

MEROPSI04.001.

PTM databases

PhosphoSiteP17475.

Proteomic databases

PaxDbP17475.
PRIDEP17475.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000012577; ENSRNOP00000012577; ENSRNOG00000032669.
GeneID24648.
KEGGrno:24648.
UCSCRGD:3326. rat.

Organism-specific databases

CTD5265.
RGD3326. Serpina1.

Phylogenomic databases

eggNOGCOG4826.
GeneTreeENSGT00750000117448.
HOGENOMHOG000238521.
HOVERGENHBG005957.
InParanoidP17475.
KOK03984.
OrthoDBEOG7QC7W9.
PhylomeDBP17475.
TreeFamTF343201.

Gene expression databases

GenevestigatorP17475.

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

NextBio603964.

Entry information

Entry nameA1AT_RAT
AccessionPrimary (citable) accession number: P17475
Secondary accession number(s): Q6AYZ5
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: February 1, 1991
Last modified: June 11, 2014
This is version 117 of the entry and version 2 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