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Q9JJ22 (ERAP1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Endoplasmic reticulum aminopeptidase 1

EC=3.4.11.-
Alternative name(s):
ARTS-1
Adipocyte-derived leucine aminopeptidase
Short name=A-LAP
Aminopeptidase PILS
Puromycin-insensitive leucyl-specific aminopeptidase
Short name=PILS-AP
Gene names
Name:Erap1
Synonyms:Appils, Arts1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length930 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Aminopeptidase that plays a central role in peptide trimming, a step required for the generation of most HLA class I-binding peptides. Peptide trimming is essential to customize longer precursor peptides to fit them to the correct length required for presentation on MHC class I molecules. Strongly prefers substrates 9-16 residues long. Rapidly degrades 13-mer to a 9-mer and then stops. Preferentially hydrolyzes the residue Leu and peptides with a hydrophobic C-terminus, while it has weak activity toward peptides with charged C-terminus. May play a role in the inactivation of peptide hormones. May be involved in the regulation of blood pressure through the inactivation of angiotensin II and/or the generation of bradykinin in the kidney By similarity.

Catalytic activity

Release of an N-terminal amino acid, Xaa-|-Xbb-, in which Xaa is preferably Leu, but may be other amino acids including Met, Cys and Phe.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subunit structure

Monomer. May also exist as a heterodimer; with ERAP2. Interacts with RBMX By similarity.

Subcellular location

Endoplasmic reticulum membrane; Single-pass type II membrane protein By similarity.

Tissue specificity

Ubiquitous. Ref.1

Post-translational modification

N-glycosylated By similarity.

Sequence similarities

Belongs to the peptidase M1 family.

Ontologies

Keywords
   Biological processAdaptive immunity
Immunity
   Cellular componentEndoplasmic reticulum
Membrane
   Coding sequence diversityAlternative splicing
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   LigandMetal-binding
Zinc
   Molecular functionAminopeptidase
Hydrolase
Metalloprotease
Protease
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processantigen processing and presentation

Traceable author statement PubMed 12436109. Source: RGD

membrane protein ectodomain proteolysis

Inferred from sequence or structural similarity. Source: UniProtKB

proteolysis

Inferred from mutant phenotype Ref.1. Source: RGD

   Cellular_componentendoplasmic reticulum lumen

Inferred from direct assay PubMed 12436109. Source: RGD

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular region

Inferred from sequence or structural similarity. Source: UniProtKB

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

intracellular membrane-bounded organelle

Inferred from direct assay PubMed 12436109. Source: RGD

   Molecular_functionaminopeptidase activity

Inferred from sequence or structural similarity. Source: UniProtKB

interleukin-6 receptor binding

Inferred from sequence or structural similarity. Source: UniProtKB

metalloexopeptidase activity

Inferred from sequence or structural similarity. Source: UniProtKB

tumor necrosis factor receptor binding

Inferred from physical interaction PubMed 20649583. Source: RGD

zinc ion binding

Inferred from mutant phenotype Ref.1. Source: RGD

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9JJ22-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9JJ22-2)

The sequence of this isoform differs from the canonical sequence as follows:
     883-884: FF → CM
     885-930: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 930930Endoplasmic reticulum aminopeptidase 1
PRO_0000026753

Regions

Topological domain1 – 22Cytoplasmic Potential
Transmembrane3 – 2321Helical; Signal-anchor for type II membrane protein; Potential
Topological domain24 – 930907Lumenal Potential
Region306 – 3105Substrate binding By similarity

Sites

Active site3431Proton acceptor By similarity
Metal binding3421Zinc; catalytic By similarity
Metal binding3461Zinc; catalytic By similarity
Metal binding3651Zinc; catalytic By similarity
Binding site1721Substrate By similarity
Site4271Transition state stabilizer By similarity

Amino acid modifications

Glycosylation591N-linked (GlcNAc...) Potential
Glycosylation1431N-linked (GlcNAc...) Potential
Glycosylation4031N-linked (GlcNAc...) Potential
Glycosylation6551N-linked (GlcNAc...) Potential
Glycosylation7491N-linked (GlcNAc...) Potential
Glycosylation8901N-linked (GlcNAc...) Potential
Disulfide bond393 ↔ 432 By similarity
Disulfide bond725 ↔ 732 By similarity

Natural variations

Alternative sequence883 – 8842FF → CM in isoform 2.
VSP_005451
Alternative sequence885 – 93046Missing in isoform 2.
VSP_005452

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 5, 2002. Version 2.
Checksum: 928E7143CBD0EE7F

FASTA930106,419
        10         20         30         40         50         60 
MPSLLSLVLT FLAVSSPSCC QNSDTASPKA SNGASFPWNN MRLPEYITPI HYDLMIHANL 

        70         80         90        100        110        120 
STLTFWGKTE VEITVSQPTS TIIMHSHQLQ ISKATLRRGA EEMLPEEPLK LMEYSAHEQV 

       130        140        150        160        170        180 
ALLTAQPLLA GSVYTVIITY AANLSENFHG FYKSTYRTQE GERRILAATQ FEPTAARMAF 

       190        200        210        220        230        240 
PCFDEPALKA SFSIKIKRDP RHLAISNMPL VKSVTVAEGL IEDHFDITVK MSTYLVAFII 

       250        260        270        280        290        300 
SDFKSVSKMT KSGVKVSVYA VPDKINQADY ALDAAVTLLE FYEDYFSIPY PLPKQDLAAI 

       310        320        330        340        350        360 
PDFQSGAMEN WGLTTYRESA LLYDKEKSSA SSKLGITMTV SHELAHQWFG NLVTMEWWND 

       370        380        390        400        410        420 
LWLNEGFAKF MEFVSVTVTH PELKVEEYFF GKCFNAMEVD ALNSSHPVST PVENPAQIRE 

       430        440        450        460        470        480 
MFDEVSYEKG ACILNMLRDY LSADTFKRGI VQYLQKYSYK NTKNEDLWNS MMHICPTDGT 

       490        500        510        520        530        540 
QTMDGFCSRN QHSSSTSHWR QEVIDIKSMM NTWTLQKGFP LITITVRGRN VHLKQEHYMK 

       550        560        570        580        590        600 
GSECFPETGS LWHVPLTFIT SKSDSVQRFL LKTKTDVIIL PEAVEWIKFN VGMNGYYIVH 

       610        620        630        640        650        660 
YGDDGWASLN GLLKEAHTTI SSNDRASLIN NAFQLVSIGK LSIEKALDLI LYLKNETEIM 

       670        680        690        700        710        720 
PIFQGLNELI PMYKLMEKRD MVEVETQFKD FLLRLLKDLI NKQTWTDEGS VSERMLRSQL 

       730        740        750        760        770        780 
LLLACVHRYQ LCVQRAERYF REWKASNGNM SLPIDVTLAV FAVGAQNTEG WDFLYSKYQS 

       790        800        810        820        830        840 
SLSSTEKSQI EFSLCISQDP EKLQWLLDQS FKGEIIKTQE FPHILTLIGR NPVGYPLAWK 

       850        860        870        880        890        900 
FLKENWNKIV QKFELGSSSI AHMVMGTTNQ FSTRARLEEV KGFFSSLKKN GSQLRCVQQT 

       910        920        930 
IETIEENIRW MDKNFDKIRL WLQKERQELL 

« Hide

Isoform 2 [UniParc].

Checksum: CD2F195A7B72FAB0
Show »

FASTA884100,730

References

[1]"Molecular characterization of a puromycin-insensitive leucyl-specific aminopeptidase, PILS-AP."
Schomburg L., Kollmus H., Friedrichsen S., Bauer K.
Eur. J. Biochem. 267:3198-3207(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY.
Strain: Sprague-Dawley.
Tissue: Pineal gland.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF148323 mRNA. Translation: AAF73106.1.
AF148324 mRNA. Translation: AAF73107.1.
RefSeqNP_110463.1. NM_030836.1.
UniGeneRn.22516.

3D structure databases

ProteinModelPortalQ9JJ22.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-4568526.
STRING10116.ENSRNOP00000013625.

Protein family/group databases

MEROPSM01.018.

PTM databases

PhosphoSiteQ9JJ22.

Proteomic databases

PaxDbQ9JJ22.
PRIDEQ9JJ22.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID80897.
KEGGrno:80897.
UCSCRGD:708542. rat. [Q9JJ22-1]

Organism-specific databases

CTD51752.
RGD708542. Erap1.

Phylogenomic databases

eggNOGCOG0308.
HOGENOMHOG000106482.
HOVERGENHBG108296.
InParanoidQ9JJ22.
KOK09604.
PhylomeDBQ9JJ22.

Gene expression databases

GenevestigatorQ9JJ22.

Family and domain databases

InterProIPR024571. ERAP1-like_C_dom.
IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
[Graphical view]
PANTHERPTHR11533. PTHR11533. 1 hit.
PfamPF11838. ERAP1_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSPR00756. ALADIPTASE.
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio614912.
PROQ9JJ22.

Entry information

Entry nameERAP1_RAT
AccessionPrimary (citable) accession number: Q9JJ22
Secondary accession number(s): Q9JJ23
Entry history
Integrated into UniProtKB/Swiss-Prot: March 5, 2002
Last sequence update: March 5, 2002
Last modified: April 16, 2014
This is version 105 of the entry and version 2 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

Peptidase families

Classification of peptidase families and list of entries