Serine protease inhibitor A3N precursor

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P09006 (SPA3N_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 103. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:	Serpina3n
Synonyms:	Spin2c

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	418 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Secreted
Domain	Signal
Molecular function	Protease inhibitor Serine protease inhibitor
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular 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 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 stimulus Inferred from electronic annotation. Source: Compara response to vitamin B6 Inferred from expression pattern PubMed 21210427. Source: RGD
Cellular_component	extracellular space Inferred from direct assay PubMed 2439511. Source: RGD
Molecular_function	serine-type endopeptidase inhibitor activity Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 29

By similarity

Chain

30 – 418

389

Serine protease inhibitor A3N

PRO_0000032423

Regions

Region

367 – 394

RCL

Sites

Site

381 – 382

Reactive bond Potential

Amino acid modifications

Glycosylation

104

N-linked (GlcNAc...) Potential

Glycosylation

258

N-linked (GlcNAc...) Potential

Glycosylation

269

N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict

A → D in CAA34408. Ref.3

Sequence conflict

C → S in CAA34408. Ref.3

Sequence conflict

D → H in CAA34408. Ref.3

Sequence conflict

N → S in CAA34408. Ref.3

Sequence conflict

236

P → S in CAA34408. Ref.3

Sequence conflict

323

E → EE in CAA31548. Ref.4

Sequence conflict

334

V → A in CAA31548. Ref.4

Sequence conflict

353

S → F in CAA34408. Ref.3

Sequence conflict

354

Q → E in CAA31548. Ref.4

Sequence conflict

381

M → V in CAA31548. Ref.4

Sequences

Sequence

Length

Mass (Da)

Tools

P09006 [UniParc].

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

FASTA

418

46,652

        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' referencesShow '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.
IPI	IPI00211075.
PIR	B26423.
RefSeq	NP_113719.1. NM_031531.1.
UniGene	Rn.202939.
3D structure databases
ProteinModelPortal	P09006.
SMR	P09006. Positions 47-418.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000014073.
Protein family/group databases
MEROPS	I04.078.
Proteomic databases
PaxDb	P09006.
PRIDE	P09006.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000014073; ENSRNOP00000014073; ENSRNOG00000010527.
GeneID	24795.
KEGG	rno:24795.
UCSC	RGD:3747. rat.
Organism-specific databases
CTD	20716.
RGD	3747. Serpina3n.
Phylogenomic databases
eggNOG	COG4826.
GeneTree	ENSGT00700000104184.
HOGENOM	HOG000238521.
HOVERGEN	HBG005957.
InParanoid	P09006.
KO	K04525.
OMA	FQHLLLT.
OrthoDB	EOG4FFD1T.
Gene expression databases
Genevestigator	P09006.
GermOnline	ENSRNOG00000010527. Rattus norvegicus.
Family and domain databases
InterPro	IPR023795. Protease_inhib_I4_serpin_CS. IPR023796. Serpin_dom. IPR000215. Serpin_fam. [Graphical view]
PANTHER	PTHR11461. PTHR11461. 1 hit.
Pfam	PF00079. Serpin. 1 hit. [Graphical view]
SMART	SM00093. SERPIN. 1 hit. [Graphical view]
SUPFAM	SSF56574. Prot_inh_serpin. 1 hit.
PROSITE	PS00284. SERPIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	604438.

Entry information

Entry name

SPA3N_RAT

Accession

Primary (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 3, 2013
This is version 103 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents