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P09006 (SPA3N_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 111. 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:
Serine protease inhibitor A3N

Short name=Serpin A3N
Alternative name(s):
CPI-26
Contrapsin-like protease inhibitor 6
SPI-2.2
Serine protease inhibitor 3
Short name=SPI-3
Gene names
Name:Serpina3n
Synonyms:Spin2c
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length418 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Subcellular location

Secreted By similarity.

Tissue specificity

Liver. Ref.2

Induction

By acute inflammation. Ref.1

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.

Post-translational modification

N-glycosylated. Ref.1

Miscellaneous

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

Sequence similarities

Belongs to the serpin family.

Caution

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

Sequence caution

The sequence AAH78796.2 differs from that shown. Reason: Erroneous initiation.

The sequence CAA34408.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence CAA34408.1 differs from that shown. Reason: Frameshift at position 7.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionProtease inhibitor
Serine protease inhibitor
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to cAMP

Inferred from expression pattern PubMed 11578771. Source: RGD

cellular response to glucocorticoid stimulus

Inferred from expression pattern PubMed 11578771. Source: RGD

cellular response to interferon-gamma

Inferred from expression pattern PubMed 7619083. Source: RGD

cellular response to interleukin-1

Inferred from expression pattern PubMed 10547273. Source: RGD

cellular response to interleukin-6

Inferred from expression pattern PubMed 8611141. Source: RGD

inflammatory response

Inferred from expression pattern Ref.1. Source: RGD

negative regulation of endopeptidase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

regulation of proteolysis

Inferred from Biological aspect of Ancestor. Source: RefGenome

response to lipopolysaccharide

Inferred from expression pattern PubMed 12127095. Source: RGD

response to peptide hormone

Inferred from electronic annotation. Source: Ensembl

response to vitamin B6

Inferred from expression pattern PubMed 21210427. Source: RGD

   Cellular_componentextracellular region

Inferred from Biological aspect of Ancestor. Source: RefGenome

extracellular space

Inferred from direct assay PubMed 2439511. Source: RGD

   Molecular_functionserine-type endopeptidase inhibitor activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929 By similarity
Chain30 – 418389Serine protease inhibitor A3N
PRO_0000032423

Regions

Region367 – 39428RCL

Sites

Site381 – 3822Reactive bond Potential

Amino acid modifications

Glycosylation1041N-linked (GlcNAc...) Potential
Glycosylation2581N-linked (GlcNAc...) Potential
Glycosylation2691N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict121A → D in CAA34408. Ref.3
Sequence conflict201C → S in CAA34408. Ref.3
Sequence conflict681D → H in CAA34408. Ref.3
Sequence conflict921N → S in CAA34408. Ref.3
Sequence conflict2361P → S in CAA34408. Ref.3
Sequence conflict3231E → EE in CAA31548. Ref.4
Sequence conflict3341V → A in CAA31548. Ref.4
Sequence conflict3531S → F in CAA34408. Ref.3
Sequence conflict3541Q → E in CAA31548. Ref.4
Sequence conflict3811M → V in CAA31548. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P09006 [UniParc].

Last modified November 1, 1997. Version 3.
Checksum: AADEFF087190B44F

FASTA41846,652
        10         20         30         40         50         60 
MTRLVTLELL MAGIGSALLC FPDCILGEDT LFHEDQDKGT QLDSLTLASI NTDFAFSLYK 

        70         80         90        100        110        120 
KLALRNPDKN VVFSPLSISA ALAVVSLGAK GNSMEEILEG LKFNLTETPE TEIHRGFGHL 

       130        140        150        160        170        180 
LQRLSQPRDE IQISTGNALF IEKRLQVLAE FQEKAKALYQ AEAFTADFQQ SREAKKLIND 

       190        200        210        220        230        240 
YVSKQTQGKI QGLITNLAKK TSMVLVNYIY FKGKWKVPFD PRDTFQSEFY SGKRRPVKVP 

       250        260        270        280        290        300 
MMKLEDLTTP YVRDEELNCT VVELKYTGNA SALFILPDQG KMQQVEASLQ PETLRRWKDS 

       310        320        330        340        350        360 
LRPSMIDELY LPKFSISADY NLEDVLPELG IKEVFSTQAD LSGITGDKDL MVSQVVHKAV 

       370        380        390        400        410 
LDVAETGTEA AAATGVKFVP MSAKLDPLII AFDRPFLMII SDTETAIAPF LAKIFNPK 

« Hide

References

« Hide 'large scale' references
[1]"Molecular characterization of three rat liver serine-protease inhibitors affected by inflammation and hypophysectomy. Protein and mRNA analysis and cDNA cloning."
Pages G., Rouayrenc J.F., le Cam G., Mariller M., le Cam A.
Eur. J. Biochem. 190:385-391(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, GLYCOSYLATION.
Tissue: Liver.
[2]"Molecular cloning and characterization of rat contrapsin-like protease inhibitor and related proteins."
Ohkubo K., Ogata S., Misumi Y., Takami N., Ikehara Y.
J. Biochem. 109:243-250(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Tissue: Liver.
[3]"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: Kidney.
[4]"Accelerated evolution in the reactive centre regions of serine protease inhibitors."
Hill R.E., Hastie N.D.
Nature 326:96-99(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 203-408.
[5]"Expression patterns of murine antichymotrypsin-like genes reflect evolutionary divergence at the Serpina3 locus."
Horvath A.J., Forsyth S.L., Coughlin P.B.
J. Mol. Evol. 59:488-497(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: REGION RCL.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X16359 mRNA. Translation: CAA34408.1. Sequence problems.
D00753 mRNA. Translation: BAA00650.1.
BC078796 mRNA. Translation: AAH78796.2. Different initiation.
X13150 mRNA. Translation: CAA31548.1.
PIRB26423.
RefSeqNP_113719.1. NM_031531.1.
UniGeneRn.202939.

3D structure databases

ProteinModelPortalP09006.
SMRP09006. Positions 47-418.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000014073.

Proteomic databases

PaxDbP09006.
PRIDEP09006.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000014073; ENSRNOP00000014073; ENSRNOG00000010527.
GeneID24795.
KEGGrno:24795.
UCSCRGD:3747. rat.

Organism-specific databases

CTD20716.
RGD3747. Serpina3n.

Phylogenomic databases

eggNOGCOG4826.
GeneTreeENSGT00740000115120.
HOGENOMHOG000238521.
HOVERGENHBG005957.
InParanoidP09006.
KOK04525.
OMAVKFVPMS.
OrthoDBEOG78M027.
PhylomeDBP09006.
TreeFamTF343201.

Gene expression databases

GenevestigatorP09006.

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

NextBio604438.
PROP09006.

Entry information

Entry nameSPA3N_RAT
AccessionPrimary (citable) accession number: P09006
Secondary accession number(s): Q03312
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1997
Last modified: April 16, 2014
This is version 111 of the entry and version 3 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