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Protein

Serine protease inhibitor A3N

Gene

Serpina3n

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei381 – 3822Reactive bondSequence Analysis

GO - Molecular functioni

  1. serine-type endopeptidase inhibitor activity Source: GO_Central

GO - Biological processi

  1. cellular response to cAMP Source: RGD
  2. cellular response to glucocorticoid stimulus Source: RGD
  3. cellular response to interferon-gamma Source: RGD
  4. cellular response to interleukin-1 Source: RGD
  5. cellular response to interleukin-6 Source: RGD
  6. inflammatory response Source: RGD
  7. negative regulation of endopeptidase activity Source: GO_Central
  8. response to lipopolysaccharide Source: RGD
  9. response to vitamin B6 Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Serine protease inhibitor

Protein family/group databases

MEROPSiI04.029.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Serpina3n
Synonyms:Spin2c
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 6

Organism-specific databases

RGDi3747. Serpina3n.

Subcellular locationi

  1. Secreted By similarity

GO - Cellular componenti

  1. extracellular space Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2929By similarityAdd
BLAST
Chaini30 – 418389Serine protease inhibitor A3NPRO_0000032423Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi104 – 1041N-linked (GlcNAc...)Sequence Analysis
Glycosylationi258 – 2581N-linked (GlcNAc...)Sequence Analysis
Glycosylationi269 – 2691N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiP09006.
PRIDEiP09006.

Expressioni

Tissue specificityi

Liver.1 Publication

Inductioni

By acute inflammation.1 Publication

Gene expression databases

GenevestigatoriP09006.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000014073.

Structurei

3D structure databases

ProteinModelPortaliP09006.
SMRiP09006. Positions 47-418.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni367 – 39428RCLAdd
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 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.By similarity

Sequence similaritiesi

Belongs to the serpin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG4826.
GeneTreeiENSGT00760000118839.
HOGENOMiHOG000238521.
HOVERGENiHBG005957.
InParanoidiP09006.
KOiK04525.
OMAiLQPRHID.
OrthoDBiEOG78M027.
PhylomeDBiP09006.
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.

P09006-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTRLVTLELL MAGIGSALLC FPDCILGEDT LFHEDQDKGT QLDSLTLASI
60 70 80 90 100
NTDFAFSLYK KLALRNPDKN VVFSPLSISA ALAVVSLGAK GNSMEEILEG
110 120 130 140 150
LKFNLTETPE TEIHRGFGHL LQRLSQPRDE IQISTGNALF IEKRLQVLAE
160 170 180 190 200
FQEKAKALYQ AEAFTADFQQ SREAKKLIND YVSKQTQGKI QGLITNLAKK
210 220 230 240 250
TSMVLVNYIY FKGKWKVPFD PRDTFQSEFY SGKRRPVKVP MMKLEDLTTP
260 270 280 290 300
YVRDEELNCT VVELKYTGNA SALFILPDQG KMQQVEASLQ PETLRRWKDS
310 320 330 340 350
LRPSMIDELY LPKFSISADY NLEDVLPELG IKEVFSTQAD LSGITGDKDL
360 370 380 390 400
MVSQVVHKAV LDVAETGTEA AAATGVKFVP MSAKLDPLII AFDRPFLMII
410
SDTETAIAPF LAKIFNPK
Length:418
Mass (Da):46,652
Last modified:November 1, 1997 - v3
Checksum:iAADEFF087190B44F
GO

Sequence cautioni

The sequence AAH78796.2 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAA34408.1 differs from that shown. Reason: Frameshift at position 7. Curated
The sequence CAA34408.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121A → D in CAA34408 (PubMed:15489334).Curated
Sequence conflicti20 – 201C → S in CAA34408 (PubMed:15489334).Curated
Sequence conflicti68 – 681D → H in CAA34408 (PubMed:15489334).Curated
Sequence conflicti92 – 921N → S in CAA34408 (PubMed:15489334).Curated
Sequence conflicti236 – 2361P → S in CAA34408 (PubMed:15489334).Curated
Sequence conflicti323 – 3231E → EE in CAA31548 (PubMed:3493437).Curated
Sequence conflicti334 – 3341V → A in CAA31548 (PubMed:3493437).Curated
Sequence conflicti353 – 3531S → F in CAA34408 (PubMed:15489334).Curated
Sequence conflicti354 – 3541Q → E in CAA31548 (PubMed:3493437).Curated
Sequence conflicti381 – 3811M → V in CAA31548 (PubMed:3493437).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16359 mRNA. Translation: CAA34408.1. Sequence problems.
D00753 mRNA. Translation: BAA00650.1.
BC078796 mRNA. Translation: AAH78796.2. Different initiation.
X13150 mRNA. Translation: CAA31548.1.
PIRiB26423.
RefSeqiNP_113719.1. NM_031531.1.
UniGeneiRn.202939.

Genome annotation databases

EnsembliENSRNOT00000014073; ENSRNOP00000014073; ENSRNOG00000010527.
GeneIDi24795.
KEGGirno:24795.
UCSCiRGD:3747. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16359 mRNA. Translation: CAA34408.1. Sequence problems.
D00753 mRNA. Translation: BAA00650.1.
BC078796 mRNA. Translation: AAH78796.2. Different initiation.
X13150 mRNA. Translation: CAA31548.1.
PIRiB26423.
RefSeqiNP_113719.1. NM_031531.1.
UniGeneiRn.202939.

3D structure databases

ProteinModelPortaliP09006.
SMRiP09006. Positions 47-418.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000014073.

Protein family/group databases

MEROPSiI04.029.

Proteomic databases

PaxDbiP09006.
PRIDEiP09006.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000014073; ENSRNOP00000014073; ENSRNOG00000010527.
GeneIDi24795.
KEGGirno:24795.
UCSCiRGD:3747. rat.

Organism-specific databases

CTDi20716.
RGDi3747. Serpina3n.

Phylogenomic databases

eggNOGiCOG4826.
GeneTreeiENSGT00760000118839.
HOGENOMiHOG000238521.
HOVERGENiHBG005957.
InParanoidiP09006.
KOiK04525.
OMAiLQPRHID.
OrthoDBiEOG78M027.
PhylomeDBiP09006.
TreeFamiTF343201.

Miscellaneous databases

NextBioi604438.
PROiP09006.

Gene expression databases

GenevestigatoriP09006.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiSPA3N_RAT
AccessioniPrimary (citable) accession number: P09006
Secondary accession number(s): Q03312
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1997
Last modified: March 4, 2015
This is version 116 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.