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Q9EQH2 (ERAP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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
VEGF-induced aminopeptidase
Gene names
Name:Erap1
Synonyms:Appils, Arts1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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.

Post-translational modification

N-glycosylated By similarity.

Sequence similarities

Belongs to the peptidase M1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 930930Endoplasmic reticulum aminopeptidase 1
PRO_0000026752

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 site3431 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

Experimental info

Sequence conflict540 – 5412KG → NA in AAG44260. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9EQH2 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: B5F542EBB30D16EB

FASTA930106,599
        10         20         30         40         50         60 
MPSLLPLVLT FLSVSSPSWC QNSDIESLKA SNGDSFPWNN MRLPEYMTPI HYDLMIHANL 

        70         80         90        100        110        120 
STLTFWGKTE VEIIASRPTS TIIMHSHHLQ ISKATLRRGA GEMLSEEPLK VLEYPAHEQV 

       130        140        150        160        170        180 
ALLAAQPLLA GSLYTVIIDY AANLSESFHG FYKSTYRTQE GEMRILAATQ FEPTAARMAF 

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

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

       310        320        330        340        350        360 
PDFQSGAMEN WGLTTYRESS LLYDKEKSSA SSKLGITMIV SHELAHQWFG NLVTMEWWND 

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

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

       490        500        510        520        530        540 
QTMDGFCSRS QHSSSTSHWR QEVVDVKTMM NTWTLQKGFP LITITVSGRN VHMKQEHYMK 

       550        560        570        580        590        600 
GSERFPETGY LWHVPLTFIT SKSDSVQRFL LKTKTDVLIL PEAVQWIKFN VGMNGYYIVH 

       610        620        630        640        650        660 
YADDGWASLS GLLKEAHTTI SSNDRASLIN NAFQLVSIEK LSIEKALDLT LYLKNETEIM 

       670        680        690        700        710        720 
PIFQALNELI PMYKLMEKRD MIEVETQFKD FLLKLLKDLI DKQTWTDEGS VSERMLRSQL 

       730        740        750        760        770        780 
LLLACVRNYQ PCVQRAERYF REWKSSNGNM SIPIDVTLAV FAVGAQNTEG WDFLYSKYQS 

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

       850        860        870        880        890        900 
FLRENWNKLV QKFELGSSSI AHMVMGTTDQ FSTRARLEEV KGFFSSLKEN GSQLRCVQQT 

       910        920        930 
IETIEENIRW MDKNFDKIRL WLQKEKPELL 

« Hide

References

« Hide 'large scale' references
[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 (JAN-2000) 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(2002) [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. expand/collapse author list , 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(2005) [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 (JUL-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(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Colon.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_109636.1. NM_030711.4.
XP_006517539.1. XM_006517476.1.
UniGeneMm.83526.

3D structure databases

ProteinModelPortalQ9EQH2.
SMRQ9EQH2. Positions 36-928.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9EQH2. 1 interaction.
MINTMINT-1863916.

Protein family/group databases

MEROPSM01.018.

PTM databases

PhosphoSiteQ9EQH2.

Proteomic databases

PaxDbQ9EQH2.
PRIDEQ9EQH2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000169114; ENSMUSP00000133166; ENSMUSG00000021583.
GeneID80898.
KEGGmmu:80898.
UCSCuc007rfi.1. mouse.

Organism-specific databases

CTD51752.
MGIMGI:1933403. Erap1.

Phylogenomic databases

eggNOGCOG0308.
GeneTreeENSGT00740000115181.
HOGENOMHOG000106482.
HOVERGENHBG108296.
InParanoidQ6GTP5.
KOK09604.
OMALIHANLT.
OrthoDBEOG754HNR.
TreeFamTF300395.

Gene expression databases

ArrayExpressQ9EQH2.
BgeeQ9EQH2.
CleanExMM_ERAP1.
GenevestigatorQ9EQH2.

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

NextBio350235.
PROQ9EQH2.
SOURCESearch...

Entry information

Entry nameERAP1_MOUSE
AccessionPrimary (citable) accession number: Q9EQH2
Secondary accession number(s): Q6GTP5, Q9ET63
Entry history
Integrated into UniProtKB/Swiss-Prot: March 5, 2002
Last sequence update: July 27, 2011
Last modified: March 19, 2014
This is version 112 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot