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Protein

Endoplasmic reticulum aminopeptidase 1

Gene

Erap1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -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).By similarity

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei172SubstrateBy similarity1
Metal bindingi342Zinc; catalyticPROSITE-ProRule annotation1
Active sitei343Proton acceptorPROSITE-ProRule annotation1
Metal bindingi346Zinc; catalyticPROSITE-ProRule annotation1
Metal bindingi365Zinc; catalyticPROSITE-ProRule annotation1
Sitei427Transition state stabilizerBy similarity1

GO - Molecular functioni

  • aminopeptidase activity Source: RGD
  • interleukin-6 receptor binding Source: UniProtKB
  • metalloaminopeptidase activity Source: GO_Central
  • metalloexopeptidase activity Source: UniProtKB
  • peptide binding Source: GO_Central
  • tumor necrosis factor receptor binding Source: RGD
  • zinc ion binding Source: RGD

GO - Biological processi

Keywordsi

Molecular functionAminopeptidase, Hydrolase, Metalloprotease, Protease
Biological processAdaptive immunity, Immunity
LigandMetal-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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi708542 Erap1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 2CytoplasmicSequence analysis2
Transmembranei3 – 23Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini24 – 930LumenalSequence analysisAdd BLAST907

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000267531 – 930Endoplasmic reticulum aminopeptidase 1Add BLAST930

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi59N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi143N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi393 ↔ 432By similarity
Glycosylationi403N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi655N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi725 ↔ 732By similarity
Glycosylationi749N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi890N-linked (GlcNAc...) asparagineSequence analysis1

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9JJ22
PeptideAtlasiQ9JJ22
PRIDEiQ9JJ22

PTM databases

iPTMnetiQ9JJ22
PhosphoSitePlusiQ9JJ22

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Interactioni

Subunit structurei

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

GO - Molecular functioni

  • interleukin-6 receptor binding Source: UniProtKB
  • tumor necrosis factor receptor binding Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000013625

Structurei

3D structure databases

ProteinModelPortaliQ9JJ22
SMRiQ9JJ22
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni306 – 310Substrate bindingBy similarity5

Sequence similaritiesi

Belongs to the peptidase M1 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1046 Eukaryota
COG0308 LUCA
HOGENOMiHOG000106482
HOVERGENiHBG108296
InParanoidiQ9JJ22
KOiK09604
PhylomeDBiQ9JJ22

Family and domain databases

CDDicd09601 M1_APN_2, 1 hit
InterProiView protein in InterPro
IPR033520 ERAP1
IPR024571 ERAP1-like_C_dom
IPR034016 M1_APN-typ
IPR001930 Peptidase_M1
IPR014782 Peptidase_M1_N
PANTHERiPTHR11533 PTHR11533, 1 hit
PTHR11533:SF156 PTHR11533:SF156, 1 hit
PfamiView protein in Pfam
PF11838 ERAP1_C, 1 hit
PF01433 Peptidase_M1, 1 hit
PRINTSiPR00756 ALADIPTASE
PROSITEiView protein in PROSITE
PS00142 ZINC_PROTEASE, 1 hit

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

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

        10         20         30         40         50
MPSLLSLVLT FLAVSSPSCC QNSDTASPKA SNGASFPWNN MRLPEYITPI
60 70 80 90 100
HYDLMIHANL STLTFWGKTE VEITVSQPTS TIIMHSHQLQ ISKATLRRGA
110 120 130 140 150
EEMLPEEPLK LMEYSAHEQV ALLTAQPLLA GSVYTVIITY AANLSENFHG
160 170 180 190 200
FYKSTYRTQE GERRILAATQ FEPTAARMAF PCFDEPALKA SFSIKIKRDP
210 220 230 240 250
RHLAISNMPL VKSVTVAEGL IEDHFDITVK MSTYLVAFII SDFKSVSKMT
260 270 280 290 300
KSGVKVSVYA VPDKINQADY ALDAAVTLLE FYEDYFSIPY PLPKQDLAAI
310 320 330 340 350
PDFQSGAMEN WGLTTYRESA LLYDKEKSSA SSKLGITMTV SHELAHQWFG
360 370 380 390 400
NLVTMEWWND LWLNEGFAKF MEFVSVTVTH PELKVEEYFF GKCFNAMEVD
410 420 430 440 450
ALNSSHPVST PVENPAQIRE MFDEVSYEKG ACILNMLRDY LSADTFKRGI
460 470 480 490 500
VQYLQKYSYK NTKNEDLWNS MMHICPTDGT QTMDGFCSRN QHSSSTSHWR
510 520 530 540 550
QEVIDIKSMM NTWTLQKGFP LITITVRGRN VHLKQEHYMK GSECFPETGS
560 570 580 590 600
LWHVPLTFIT SKSDSVQRFL LKTKTDVIIL PEAVEWIKFN VGMNGYYIVH
610 620 630 640 650
YGDDGWASLN GLLKEAHTTI SSNDRASLIN NAFQLVSIGK LSIEKALDLI
660 670 680 690 700
LYLKNETEIM PIFQGLNELI PMYKLMEKRD MVEVETQFKD FLLRLLKDLI
710 720 730 740 750
NKQTWTDEGS VSERMLRSQL LLLACVHRYQ LCVQRAERYF REWKASNGNM
760 770 780 790 800
SLPIDVTLAV FAVGAQNTEG WDFLYSKYQS SLSSTEKSQI EFSLCISQDP
810 820 830 840 850
EKLQWLLDQS FKGEIIKTQE FPHILTLIGR NPVGYPLAWK FLKENWNKIV
860 870 880 890 900
QKFELGSSSI AHMVMGTTNQ FSTRARLEEV KGFFSSLKKN GSQLRCVQQT
910 920 930
IETIEENIRW MDKNFDKIRL WLQKERQELL
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)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_005451883 – 884FF → CM in isoform 2. 1 Publication2
Alternative sequenceiVSP_005452885 – 930Missing in isoform 2. 1 PublicationAdd BLAST46

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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

Similar proteinsi

Entry informationi

Entry nameiERAP1_RAT
AccessioniPrimary (citable) accession number: Q9JJ22
Secondary accession number(s): Q9JJ23
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 5, 2002
Last sequence update: March 5, 2002
Last modified: June 20, 2018
This is version 129 of the entry and version 2 of the sequence. See 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

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