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Q9JJ22

- ERAP1_RAT

UniProt

Q9JJ22 - ERAP1_RAT

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Protein
Endoplasmic reticulum aminopeptidase 1
Gene
Erap1, Appils, Arts1
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

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 activityi

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.

Cofactori

Binds 1 zinc ion per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei172 – 1721Substrate By similarity
Metal bindingi342 – 3421Zinc; catalytic By similarity
Active sitei343 – 3431Proton acceptor By similarity
Metal bindingi346 – 3461Zinc; catalytic By similarity
Metal bindingi365 – 3651Zinc; catalytic By similarity
Sitei427 – 4271Transition state stabilizer By similarity

GO - Molecular functioni

  1. aminopeptidase activity Source: UniProtKB
  2. interleukin-6 receptor binding Source: UniProtKB
  3. metalloexopeptidase activity Source: UniProtKB
  4. tumor necrosis factor receptor binding Source: RGD
  5. zinc ion binding Source: RGD

GO - Biological processi

  1. antigen processing and presentation Source: RGD
  2. membrane protein ectodomain proteolysis Source: UniProtKB
  3. proteolysis Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Adaptive immunity, Immunity

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM01.018.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Erap1
Synonyms:Appils, Arts1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi708542. Erap1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 22Cytoplasmic Reviewed prediction
Transmembranei3 – 2321Helical; Signal-anchor for type II membrane protein; Reviewed prediction
Add
BLAST
Topological domaini24 – 930907Lumenal Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum lumen Source: RGD
  2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  3. extracellular region Source: UniProtKB
  4. integral component of membrane Source: UniProtKB-KW
  5. intracellular membrane-bounded organelle Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 930930Endoplasmic reticulum aminopeptidase 1
PRO_0000026753Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi59 – 591N-linked (GlcNAc...) Reviewed prediction
Glycosylationi143 – 1431N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi393 ↔ 432 By similarity
Glycosylationi403 – 4031N-linked (GlcNAc...) Reviewed prediction
Glycosylationi655 – 6551N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi725 ↔ 732 By similarity
Glycosylationi749 – 7491N-linked (GlcNAc...) Reviewed prediction
Glycosylationi890 – 8901N-linked (GlcNAc...) Reviewed prediction

Post-translational modificationi

N-glycosylated By similarity.

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9JJ22.
PRIDEiQ9JJ22.

PTM databases

PhosphoSiteiQ9JJ22.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

GenevestigatoriQ9JJ22.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

MINTiMINT-4568526.
STRINGi10116.ENSRNOP00000013625.

Structurei

3D structure databases

ProteinModelPortaliQ9JJ22.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni306 – 3105Substrate binding By similarity

Sequence similaritiesi

Belongs to the peptidase M1 family.

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0308.
HOGENOMiHOG000106482.
HOVERGENiHBG108296.
InParanoidiQ9JJ22.
KOiK09604.
PhylomeDBiQ9JJ22.

Family and domain databases

InterProiIPR024571. ERAP1-like_C_dom.
IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
[Graphical view]
PANTHERiPTHR11533. PTHR11533. 1 hit.
PfamiPF11838. ERAP1_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSiPR00756. ALADIPTASE.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9JJ22-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MPSLLSLVLT FLAVSSPSCC QNSDTASPKA SNGASFPWNN MRLPEYITPI    50
HYDLMIHANL STLTFWGKTE VEITVSQPTS TIIMHSHQLQ ISKATLRRGA 100
EEMLPEEPLK LMEYSAHEQV ALLTAQPLLA GSVYTVIITY AANLSENFHG 150
FYKSTYRTQE GERRILAATQ FEPTAARMAF PCFDEPALKA SFSIKIKRDP 200
RHLAISNMPL VKSVTVAEGL IEDHFDITVK MSTYLVAFII SDFKSVSKMT 250
KSGVKVSVYA VPDKINQADY ALDAAVTLLE FYEDYFSIPY PLPKQDLAAI 300
PDFQSGAMEN WGLTTYRESA LLYDKEKSSA SSKLGITMTV SHELAHQWFG 350
NLVTMEWWND LWLNEGFAKF MEFVSVTVTH PELKVEEYFF GKCFNAMEVD 400
ALNSSHPVST PVENPAQIRE MFDEVSYEKG ACILNMLRDY LSADTFKRGI 450
VQYLQKYSYK NTKNEDLWNS MMHICPTDGT QTMDGFCSRN QHSSSTSHWR 500
QEVIDIKSMM NTWTLQKGFP LITITVRGRN VHLKQEHYMK GSECFPETGS 550
LWHVPLTFIT SKSDSVQRFL LKTKTDVIIL PEAVEWIKFN VGMNGYYIVH 600
YGDDGWASLN GLLKEAHTTI SSNDRASLIN NAFQLVSIGK LSIEKALDLI 650
LYLKNETEIM PIFQGLNELI PMYKLMEKRD MVEVETQFKD FLLRLLKDLI 700
NKQTWTDEGS VSERMLRSQL LLLACVHRYQ LCVQRAERYF REWKASNGNM 750
SLPIDVTLAV FAVGAQNTEG WDFLYSKYQS SLSSTEKSQI EFSLCISQDP 800
EKLQWLLDQS FKGEIIKTQE FPHILTLIGR NPVGYPLAWK FLKENWNKIV 850
QKFELGSSSI AHMVMGTTNQ FSTRARLEEV KGFFSSLKKN GSQLRCVQQT 900
IETIEENIRW MDKNFDKIRL WLQKERQELL 930
Length:930
Mass (Da):106,419
Last modified:March 5, 2002 - v2
Checksum:i928E7143CBD0EE7F
GO
Isoform 2 (identifier: Q9JJ22-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:884
Mass (Da):100,730
Checksum:iCD2F195A7B72FAB0
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei883 – 8842FF → CM in isoform 2.
VSP_005451
Alternative sequencei885 – 93046Missing in isoform 2.
VSP_005452Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF148323 mRNA. Translation: AAF73106.1.
AF148324 mRNA. Translation: AAF73107.1.
RefSeqiNP_110463.1. NM_030836.1. [Q9JJ22-2]
UniGeneiRn.22516.

Genome annotation databases

GeneIDi80897.
KEGGirno:80897.
UCSCiRGD:708542. rat. [Q9JJ22-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF148323 mRNA. Translation: AAF73106.1 .
AF148324 mRNA. Translation: AAF73107.1 .
RefSeqi NP_110463.1. NM_030836.1. [Q9JJ22-2 ]
UniGenei Rn.22516.

3D structure databases

ProteinModelPortali Q9JJ22.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-4568526.
STRINGi 10116.ENSRNOP00000013625.

Protein family/group databases

MEROPSi M01.018.

PTM databases

PhosphoSitei Q9JJ22.

Proteomic databases

PaxDbi Q9JJ22.
PRIDEi Q9JJ22.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 80897.
KEGGi rno:80897.
UCSCi RGD:708542. rat. [Q9JJ22-1 ]

Organism-specific databases

CTDi 51752.
RGDi 708542. Erap1.

Phylogenomic databases

eggNOGi COG0308.
HOGENOMi HOG000106482.
HOVERGENi HBG108296.
InParanoidi Q9JJ22.
KOi K09604.
PhylomeDBi Q9JJ22.

Miscellaneous databases

NextBioi 614912.
PROi Q9JJ22.

Gene expression databases

Genevestigatori Q9JJ22.

Family and domain databases

InterProi IPR024571. ERAP1-like_C_dom.
IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
[Graphical view ]
PANTHERi PTHR11533. PTHR11533. 1 hit.
Pfami PF11838. ERAP1_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view ]
PRINTSi PR00756. ALADIPTASE.
PROSITEi PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiERAP1_RAT
AccessioniPrimary (citable) accession number: Q9JJ22
Secondary accession number(s): Q9JJ23
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 5, 2002
Last sequence update: March 5, 2002
Last modified: May 14, 2014
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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