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Protein

Endoplasmic reticulum aminopeptidase 1

Gene

Erap1

Organism
Mus musculus (Mouse)
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 – 3431PROSITE-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. peptidase activity Source: MGI
  5. zinc ion binding Source: InterPro

GO - Biological processi

  1. immune system process Source: UniProtKB-KW
  2. membrane protein ectodomain proteolysis Source: UniProtKB
  3. positive regulation of angiogenesis Source: MGI
  4. proteolysis Source: MGI
  5. response to bacterium Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Adaptive immunity, Immunity

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_339401. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.

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
VEGF-induced aminopeptidase
Gene namesi
Name:Erap1
Synonyms:Appils, Arts1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:1933403. 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. cytoplasm Source: MGI
  2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  3. extracellular region Source: UniProtKB
  4. extracellular space Source: MGI
  5. extracellular vesicular exosome Source: MGI
  6. integral component of membrane Source: UniProtKB-KW
  7. membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 930930Endoplasmic reticulum aminopeptidase 1PRO_0000026752Add
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

MaxQBiQ9EQH2.
PaxDbiQ9EQH2.
PRIDEiQ9EQH2.

PTM databases

PhosphoSiteiQ9EQH2.

Expressioni

Gene expression databases

BgeeiQ9EQH2.
CleanExiMM_ERAP1.
ExpressionAtlasiQ9EQH2. baseline and differential.
GenevestigatoriQ9EQH2.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiQ9EQH2. 1 interaction.
MINTiMINT-1863916.

Structurei

3D structure databases

ProteinModelPortaliQ9EQH2.
SMRiQ9EQH2. Positions 36-928.
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.
GeneTreeiENSGT00760000119082.
HOGENOMiHOG000106482.
HOVERGENiHBG108296.
InParanoidiQ9EQH2.
KOiK09604.
OMAiDGFCSRS.
OrthoDBiEOG754HNR.
TreeFamiTF300395.

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]

Sequencei

Sequence statusi: Complete.

Q9EQH2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPSLLPLVLT FLSVSSPSWC QNSDIESLKA SNGDSFPWNN MRLPEYMTPI
60 70 80 90 100
HYDLMIHANL STLTFWGKTE VEIIASRPTS TIIMHSHHLQ ISKATLRRGA
110 120 130 140 150
GEMLSEEPLK VLEYPAHEQV ALLAAQPLLA GSLYTVIIDY AANLSESFHG
160 170 180 190 200
FYKSTYRTQE GEMRILAATQ FEPTAARMAF PCFDEPALKA SFSIKIKRDP
210 220 230 240 250
RHLAISNMPL VKSVNVAEGL IEDHFDITVK MSTYLVAFII SDFKSVSKMT
260 270 280 290 300
KSGVKVSVYA VPDKINQADY ALDAAVTLLE FYEDYFNIPY PLPKQDLAAI
310 320 330 340 350
PDFQSGAMEN WGLTTYRESS LLYDKEKSSA SSKLGITMIV SHELAHQWFG
360 370 380 390 400
NLVTMEWWND LWLNEGFAKF MEFVSVTVTH PELKVEDYFF GKCFNAMEVD
410 420 430 440 450
ALNSSHPVST PVENPAQIRE MFDDVSYEKG ACILNMLRDY LSADTFKRGI
460 470 480 490 500
VQYLQKYSYK NTKNEDLWNS MMHICPTDGT QTMDGFCSRS QHSSSTSHWR
510 520 530 540 550
QEVVDVKTMM NTWTLQKGFP LITITVSGRN VHMKQEHYMK GSERFPETGY
560 570 580 590 600
LWHVPLTFIT SKSDSVQRFL LKTKTDVLIL PEAVQWIKFN VGMNGYYIVH
610 620 630 640 650
YADDGWASLS GLLKEAHTTI SSNDRASLIN NAFQLVSIEK LSIEKALDLT
660 670 680 690 700
LYLKNETEIM PIFQALNELI PMYKLMEKRD MIEVETQFKD FLLKLLKDLI
710 720 730 740 750
DKQTWTDEGS VSERMLRSQL LLLACVRNYQ PCVQRAERYF REWKSSNGNM
760 770 780 790 800
SIPIDVTLAV FAVGAQNTEG WDFLYSKYQS SLSSTEKSQI EFSLCTSKDP
810 820 830 840 850
EKLQWLLDQS FKGEIIKTQE FPHILTLIGR NPVGYPLAWK FLRENWNKLV
860 870 880 890 900
QKFELGSSSI AHMVMGTTDQ FSTRARLEEV KGFFSSLKEN GSQLRCVQQT
910 920 930
IETIEENIRW MDKNFDKIRL WLQKEKPELL
Length:930
Mass (Da):106,599
Last modified:July 27, 2011 - v2
Checksum:iB5F542EBB30D16EB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti540 – 5412KG → NA in AAG44260 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF227511 mRNA. Translation: AAG44260.1.
AB047552 mRNA. Translation: BAB11982.1.
AK030329 mRNA. Translation: BAC26904.1.
CH466563 Genomic DNA. Translation: EDL37102.1.
BC046610 mRNA. Translation: AAH46610.1.
CCDSiCCDS26647.1.
RefSeqiNP_109636.1. NM_030711.4.
XP_006517539.1. XM_006517476.2.
UniGeneiMm.83526.

Genome annotation databases

EnsembliENSMUST00000169114; ENSMUSP00000133166; ENSMUSG00000021583.
GeneIDi80898.
KEGGimmu:80898.
UCSCiuc007rfi.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF227511 mRNA. Translation: AAG44260.1.
AB047552 mRNA. Translation: BAB11982.1.
AK030329 mRNA. Translation: BAC26904.1.
CH466563 Genomic DNA. Translation: EDL37102.1.
BC046610 mRNA. Translation: AAH46610.1.
CCDSiCCDS26647.1.
RefSeqiNP_109636.1. NM_030711.4.
XP_006517539.1. XM_006517476.2.
UniGeneiMm.83526.

3D structure databases

ProteinModelPortaliQ9EQH2.
SMRiQ9EQH2. Positions 36-928.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9EQH2. 1 interaction.
MINTiMINT-1863916.

Protein family/group databases

MEROPSiM01.018.

PTM databases

PhosphoSiteiQ9EQH2.

Proteomic databases

MaxQBiQ9EQH2.
PaxDbiQ9EQH2.
PRIDEiQ9EQH2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000169114; ENSMUSP00000133166; ENSMUSG00000021583.
GeneIDi80898.
KEGGimmu:80898.
UCSCiuc007rfi.1. mouse.

Organism-specific databases

CTDi51752.
MGIiMGI:1933403. Erap1.

Phylogenomic databases

eggNOGiCOG0308.
GeneTreeiENSGT00760000119082.
HOGENOMiHOG000106482.
HOVERGENiHBG108296.
InParanoidiQ9EQH2.
KOiK09604.
OMAiDGFCSRS.
OrthoDBiEOG754HNR.
TreeFamiTF300395.

Enzyme and pathway databases

ReactomeiREACT_339401. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.

Miscellaneous databases

NextBioi350235.
PROiQ9EQH2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9EQH2.
CleanExiMM_ERAP1.
ExpressionAtlasiQ9EQH2. baseline and differential.
GenevestigatoriQ9EQH2.

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

« Hide 'large scale' publications
  1. "Molecular cloning of murine adipocyte-derived leucine aminopeptidase and its expression in adipocyte cell line, 3T3-L1 cells."
    Hattori A., Kitatani K., Matsumoto H., Mizutani S., Tsujimoto M.
    Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "A mouse orthologue of puromycin-insensitive leucyl-specific aminopeptidase is expressed in endothelial cells and plays an important role in angiogenesis."
    Miyashita H., Yamazaki T., Akada T., Niizeki O., Ogawa M., Nishikawa S., Sato Y.
    Blood 99:3241-3249(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Colon.

Entry informationi

Entry nameiERAP1_MOUSE
AccessioniPrimary (citable) accession number: Q9EQH2
Secondary accession number(s): Q6GTP5, Q9ET63
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 5, 2002
Last sequence update: July 27, 2011
Last modified: April 1, 2015
This is version 120 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. 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.