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Protein

Endoplasmic reticulum aminopeptidase 1

Gene

Erap1

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

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei172 – 1721SubstrateBy similarity
Metal bindingi342 – 3421Zinc; catalyticPROSITE-ProRule annotation
Active sitei343 – 3431Proton acceptorPROSITE-ProRule annotation
Metal bindingi346 – 3461Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi365 – 3651Zinc; catalyticPROSITE-ProRule annotation
Sitei427 – 4271Transition state stabilizerBy 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 Componenti: Unplaced

Organism-specific databases

RGDi708542. Erap1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 22CytoplasmicSequence Analysis
Transmembranei3 – 2321Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini24 – 930907LumenalSequence AnalysisAdd
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 1PRO_0000026753Add
BLAST

Amino acid modifications

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

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).By similarity

Protein-protein interaction databases

MINTiMINT-4568526.
STRINGi10116.ENSRNOP00000013625.

Structurei

3D structure databases

ProteinModelPortaliQ9JJ22.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

Sequence similaritiesi

Belongs to the peptidase M1 family.Curated

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. 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)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei883 – 8842FF → CM in isoform 2. 1 PublicationVSP_005451
Alternative sequencei885 – 93046Missing in isoform 2. 1 PublicationVSP_005452Add
BLAST

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

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliQ9JJ22.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4568526.
STRINGi10116.ENSRNOP00000013625.

Protein family/group databases

MEROPSiM01.018.

PTM databases

PhosphoSiteiQ9JJ22.

Proteomic databases

PaxDbiQ9JJ22.
PRIDEiQ9JJ22.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi51752.
RGDi708542. Erap1.

Phylogenomic databases

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

Miscellaneous databases

NextBioi614912.
PROiQ9JJ22.

Gene expression databases

GenevestigatoriQ9JJ22.

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]
ProtoNetiSearch...

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: January 7, 2015
This is version 110 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.