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Protein

Endoplasmic reticulum aminopeptidase 2

Gene

ERAP2

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 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. Preferentially hydrolyzes the basic residues Arg and Lys (By similarity).By similarity

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei194 – 1941SubstrateBy similarity
Metal bindingi364 – 3641Zinc; catalyticPROSITE-ProRule annotation
Active sitei365 – 3651Proton acceptorPROSITE-ProRule annotation
Metal bindingi368 – 3681Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi387 – 3871Zinc; catalyticPROSITE-ProRule annotation
Sitei449 – 4491Transition state stabilizerBy similarity

GO - Molecular functioni

GO - Biological processi

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

ReactomeiR-BTA-983170. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.

Protein family/group databases

MEROPSiM01.024.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoplasmic reticulum aminopeptidase 2 (EC:3.4.11.-)
Gene namesi
Name:ERAP2
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 7

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 77CytoplasmicSequence analysis
Transmembranei8 – 2821Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini29 – 954926LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 954954Endoplasmic reticulum aminopeptidase 2PRO_0000315718Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi79 – 791N-linked (GlcNAc...)Sequence analysis
Glycosylationi113 – 1131N-linked (GlcNAc...)Sequence analysis
Glycosylationi399 – 3991N-linked (GlcNAc...)Sequence analysis
Disulfide bondi415 ↔ 454By similarity
Glycosylationi644 – 6441N-linked (GlcNAc...)Sequence analysis
Disulfide bondi753 ↔ 760By similarity

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiA6QPT7.
PRIDEiA6QPT7.

Interactioni

Subunit structurei

Heterodimer with ERAP1.By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000001164.

Structurei

3D structure databases

ProteinModelPortaliA6QPT7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni328 – 3325Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the peptidase M1 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1046. Eukaryota.
COG0308. LUCA.
GeneTreeiENSGT00760000119082.
HOGENOMiHOG000106482.
HOVERGENiHBG108296.
InParanoidiA6QPT7.
KOiK13723.
OMAiHYEGHGW.
OrthoDBiEOG754HNR.
TreeFamiTF300395.

Family and domain databases

InterProiIPR024571. ERAP1-like_C_dom.
IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
[Graphical view]
PANTHERiPTHR11533. PTHR11533. 2 hits.
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.

A6QPT7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANSCRKLIF NIYVVFYCSA VIMPQICICS QFTSSPIDQF NKDPKAFPVA
60 70 80 90 100
TNGEIFPWHE LRLPTVVIPL HYDLLIHPNL TSLDFVASEK IEVLVRDATQ
110 120 130 140 150
FIILHSKDLE ILNASLQSEE DVRYKKPGEN LTVLSYPAHQ QIALLVPEKL
160 170 180 190 200
RAHLRYSVAI DFQAKLADGF EGFYKSTYRT LGGETRTIAV TDFEPTEARM
210 220 230 240 250
AFPCFDEPLF KANFSIKIRR ESRHIALSNM PKVKTIELEG GLLEDHFETT
260 270 280 290 300
VRMSTYLVAY IVCDFTSVSG TASSGVKVSI YASPDKWSQT HYALEASVKL
310 320 330 340 350
LDFYENYFDI HYPLPKLDLV AIPDFASGAM ENWGLITYRE TSLLFDPKTS
360 370 380 390 400
STSDKLWVTK VIAHELAHQW FGNLVTMEWW NDIWLNEGFA RYMELISLNI
410 420 430 440 450
TYPELQFDDS FSNTCFEVIK RDSLNSSHPI SNEAKTATQI KEMFDAVSYN
460 470 480 490 500
KGACILNMLK DFLSEETFRK GIIHYLKKFT YRNAKNDDLW HSLSNNCLEG
510 520 530 540 550
DSTSGGFCYS DSRKTSNTLA FLRENVELKE MMATWTLQKG IPLVVVKREG
560 570 580 590 600
RSLRLQQERF LSGVFKEDPE WGTLQERYLW HIPVTYSTSS SQAIHRHILK
610 620 630 640 650
LKTDTVDLSE KTDWVKFNVD SSGYYIVHYE GQGWDELITL LNQNHTLLRP
660 670 680 690 700
KDRLGLIHDA FQLVSAGRLT LDKALDLTRY LQHETSIPAL LKGLEYLELF
710 720 730 740 750
YRMVERRNIS DVTENLKHYL LQYFKPVIDT QSWLDEGSVW DRMLRSTVLK
760 770 780 790 800
LACYLNHAPC IQKATELFSQ WMESSGKLNI PADVLTIVYS VGAQTTAGWN
810 820 830 840 850
YLLEQYELSL SGAEKNKILY ALSTSKHQEK LMKLIELGME GKVIKTQDLA
860 870 880 890 900
TLLFTTARNP KGQQLAWNFV KENWTHLLKK FELGSFPIRM IISGTTSHFS
910 920 930 940 950
SKDELQEVKL FFESLKAQGS HLDIFQIILE TISKNIKWLE KNLPTLRKWL

LTSI
Length:954
Mass (Da):109,719
Last modified:August 21, 2007 - v1
Checksum:iCC9F28CB1EBFBE2F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC149475 mRNA. Translation: AAI49476.1.
RefSeqiNP_001069096.2. NM_001075628.2.
XP_005209817.1. XM_005209760.3.
UniGeneiBt.59451.

Genome annotation databases

EnsembliENSBTAT00000001164; ENSBTAP00000001164; ENSBTAG00000039275.
GeneIDi513572.
KEGGibta:513572.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC149475 mRNA. Translation: AAI49476.1.
RefSeqiNP_001069096.2. NM_001075628.2.
XP_005209817.1. XM_005209760.3.
UniGeneiBt.59451.

3D structure databases

ProteinModelPortaliA6QPT7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000001164.

Protein family/group databases

MEROPSiM01.024.

Proteomic databases

PaxDbiA6QPT7.
PRIDEiA6QPT7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000001164; ENSBTAP00000001164; ENSBTAG00000039275.
GeneIDi513572.
KEGGibta:513572.

Organism-specific databases

CTDi64167.

Phylogenomic databases

eggNOGiKOG1046. Eukaryota.
COG0308. LUCA.
GeneTreeiENSGT00760000119082.
HOGENOMiHOG000106482.
HOVERGENiHBG108296.
InParanoidiA6QPT7.
KOiK13723.
OMAiHYEGHGW.
OrthoDBiEOG754HNR.
TreeFamiTF300395.

Enzyme and pathway databases

ReactomeiR-BTA-983170. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.

Miscellaneous databases

NextBioi20870919.

Family and domain databases

InterProiIPR024571. ERAP1-like_C_dom.
IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
[Graphical view]
PANTHERiPTHR11533. PTHR11533. 2 hits.
PfamiPF11838. ERAP1_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSiPR00756. ALADIPTASE.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. NIH - Mammalian Gene Collection (MGC) project
    Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Thymus.

Entry informationi

Entry nameiERAP2_BOVIN
AccessioniPrimary (citable) accession number: A6QPT7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 21, 2007
Last modified: April 13, 2016
This is version 72 of the entry and version 1 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

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 one 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.