P09006 · SPA3N_RAT

  • Protein
    Serine protease inhibitor A3N
  • Gene
    Serpina3n
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

Miscellaneous

The single human alpha1-antichymotrypsin gene (SERPINA3) is represented by a cluster of 6 individual rat paralogs.

Caution

It is uncertain whether Met-1 or Met-11 is the initiator.

Features

Showing features for site.

141850100150200250300350400
TypeIDPosition(s)Description
Site381-382Reactive bond

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentextracellular region
Cellular Componentextracellular space
Molecular Functionserine-type endopeptidase inhibitor activity
Biological Processcellular response to cAMP
Biological Processcellular response to glucocorticoid stimulus
Biological Processcellular response to interleukin-1
Biological Processcellular response to interleukin-6
Biological Processcellular response to type II interferon
Biological Processresponse to bacterium
Biological Processresponse to cytokine
Biological Processresponse to lipopolysaccharide
Biological Processresponse to peptide hormone
Biological Processresponse to vitamin B6

Keywords

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Serine protease inhibitor A3N
  • Short names
    Serpin A3N
  • Alternative names
    • CPI-26
    • Contrapsin-like protease inhibitor 6
    • SPI-2.2
    • Serine protease inhibitor 3 (SPI-3)

Gene names

    • Name
      Serpina3n
    • Synonyms
      Spin2c

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus

Accessions

  • Primary accession
    P09006
  • Secondary accessions
    • Q03312

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, chain, modified residue, glycosylation.

TypeIDPosition(s)Description
Signal1-29
ChainPRO_000003242330-418Serine protease inhibitor A3N
Modified residue93Phosphoserine
Glycosylation104N-linked (GlcNAc...) asparagine
Glycosylation258N-linked (GlcNAc...) asparagine
Glycosylation269N-linked (GlcNAc...) asparagine

Post-translational modification

N-glycosylated.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Liver.

Induction

By acute inflammation.

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region367-394RCL

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 serpin reactive site and the protease. The resulting inactive serpin-protease complex is highly stable (By similarity).
Variability within the reactive center loop (RCL) sequences of Serpina3 paralogs may determine target protease specificity

Sequence similarities

Belongs to the serpin family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    418
  • Mass (Da)
    46,652
  • Last updated
    1997-11-01 v3
  • Checksum
    AADEFF087190B44F
MTRLVTLELLMAGIGSALLCFPDCILGEDTLFHEDQDKGTQLDSLTLASINTDFAFSLYKKLALRNPDKNVVFSPLSISAALAVVSLGAKGNSMEEILEGLKFNLTETPETEIHRGFGHLLQRLSQPRDEIQISTGNALFIEKRLQVLAEFQEKAKALYQAEAFTADFQQSREAKKLINDYVSKQTQGKIQGLITNLAKKTSMVLVNYIYFKGKWKVPFDPRDTFQSEFYSGKRRPVKVPMMKLEDLTTPYVRDEELNCTVVELKYTGNASALFILPDQGKMQQVEASLQPETLRRWKDSLRPSMIDELYLPKFSISADYNLEDVLPELGIKEVFSTQADLSGITGDKDLMVSQVVHKAVLDVAETGTEAAAATGVKFVPMSAKLDPLIIAFDRPFLMIISDTETAIAPFLAKIFNPK

Sequence caution

The sequence AAH78796.2 differs from that shown. Reason: Erroneous initiation
The sequence CAA34408.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.
The sequence CAA34408.1 differs from that shown. Reason: Frameshift

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict12in Ref. 3; CAA34408
Sequence conflict20in Ref. 3; CAA34408
Sequence conflict68in Ref. 3; CAA34408
Sequence conflict92in Ref. 3; CAA34408
Sequence conflict236in Ref. 3; CAA34408
Sequence conflict323in Ref. 4; CAA31548
Sequence conflict334in Ref. 4; CAA31548
Sequence conflict353in Ref. 3; CAA34408
Sequence conflict354in Ref. 4; CAA31548
Sequence conflict381in Ref. 4; CAA31548

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X16359
EMBL· GenBank· DDBJ
CAA34408.1
EMBL· GenBank· DDBJ
mRNA Sequence problems.
D00753
EMBL· GenBank· DDBJ
BAA00650.1
EMBL· GenBank· DDBJ
mRNA
BC078796
EMBL· GenBank· DDBJ
AAH78796.2
EMBL· GenBank· DDBJ
mRNA Different initiation
X13150
EMBL· GenBank· DDBJ
CAA31548.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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