Alpha-1-antiproteinase precursor - Rattus norvegicus (Rat)

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P17475 (A1AT_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 107. 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:
Alpha-1-antiproteinase

Alternative name(s):
Alpha-1-antitrypsin
Alpha-1-proteinase inhibitor
Serpin A1

Gene names

Name:

Serpina1

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	411 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)

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 process	Acute phase
Cellular component	Secreted
Domain	Signal
Molecular function	Protease inhibitor Serine protease inhibitor
PTM	Glycoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	acute-phase response Inferred from electronic annotation. Source: UniProtKB-KW inflammatory response Inferred from expression pattern PubMed 20118217. 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 stimulus Inferred from expression pattern PubMed 9533938. Source: RGD response to estradiol stimulus Inferred from expression pattern PubMed 1466268. Source: RGD response to hypoxia Inferred from expression pattern PubMed 12121987. 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 triglyceride Inferred from expression pattern PubMed 10362649. Source: RGD
Cellular_component	extracellular space Inferred from direct assay PubMed 17634200. 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 – 24

Ref.3

Chain

25 – 411

387

Alpha-1-antiproteinase

PRO_0000032398

Regions

Region

367 – 386

RCL

Sites

Site

376 – 377

Reactive bond

Amino acid modifications

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

101

N-linked (GlcNAc...) Potential

Glycosylation

265

N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict

A → G in BAA00579. Ref.1

Sequence conflict

A → G in AAH78824. Ref.2

Sequence conflict

L → V in BAA00579. Ref.1

Sequence conflict

247

M → I in CAA34349. Ref.5

Sequence conflict

248

H → Y in BAA00579. Ref.1

Sequence conflict

318

K → N in BAA00579. Ref.1

Sequence conflict

322

S → D in CAA34349. Ref.5

Sequences

Sequence

Length

Mass (Da)

Tools

P17475 [UniParc].

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

FASTA

411

46,136

        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' referencesShow '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, 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.
IPI	IPI00324019.
PIR	ITRT. A33892.
RefSeq	NP_071964.2. NM_022519.2.
UniGene	Rn.1419.
3D structure databases
ProteinModelPortal	P17475.
SMR	P17475. Positions 39-411.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000012577.
Protein family/group databases
MEROPS	I04.001.
PTM databases
PhosphoSite	P17475.
Proteomic databases
PaxDb	P17475.
PRIDE	P17475.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000012577; ENSRNOP00000012577; ENSRNOG00000032669.
GeneID	24648.
KEGG	rno:24648.
UCSC	RGD:3326. rat.
Organism-specific databases
CTD	5265.
RGD	3326. Serpina1.
Phylogenomic databases
eggNOG	COG4826.
GeneTree	ENSGT00700000104184.
HOGENOM	HOG000238521.
HOVERGEN	HBG005957.
InParanoid	P17475.
KO	K03984.
OrthoDB	EOG4FR0S4.
Gene expression databases
Genevestigator	P17475.
GermOnline	ENSRNOG00000032669. 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	603964.

Entry information

Entry name

A1AT_RAT

Accession

Primary (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:	April 3, 2013
This is version 107 of the entry and version 2 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

PTM 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