ERAP1
Endoplasmic reticulum aminopeptidase 1
Also known as: A-LAP, ARTS-1, ERAAP1, ERAP1_HUMAN, KIAA0525, PILS-AP
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- Q9NZ08
- Gene
- ERAP1
- Ensembl
- ENSG00000164307
- Chromosome
- 5
- Canonical length
- 941 aa
- Protein class
- Enzymes, Plasma proteins, Predicted intracellular proteins, Predicted secreted proteins
- Subcellular location
- Nucleoplasm,Plasma membrane,Cytosol
- Secretome location
- Secreted to blood
OverviewNCBI Gene
The protein encoded by this gene is an aminopeptidase involved in trimming HLA class I-binding precursors so that they can be presented on MHC class I molecules. The encoded protein acts as a monomer or as a heterodimer with ERAP2. This protein may also be involved in blood pressure regulation by inactivation of angiotensin II. Three transcript variants encoding two different isoforms have been found for this gene.[provided by RefSeq, Oct 2010]
Canonical amino-acid sequenceUniProt
941 residues, UniProt reviewed canonical sequence.
>Q9NZ08|ERAP1
1 MVFLPLKWSL ATMSFLLSSL LALLTVSTPS WCQSTEASPK RSDGTPFPWN KIRLPEYVIP
61 VHYDLLIHAN LTTLTFWGTT KVEITASQPT STIILHSHHL QISRATLRKG AGERLSEEPL
121 QVLEHPRQEQ IALLAPEPLL VGLPYTVVIH YAGNLSETFH GFYKSTYRTK EGELRILAST
181 QFEPTAARMA FPCFDEPAFK ASFSIKIRRE PRHLAISNMP LVKSVTVAEG LIEDHFDVTV
241 KMSTYLVAFI ISDFESVSKI TKSGVKVSVY AVPDKINQAD YALDAAVTLL EFYEDYFSIP
301 YPLPKQDLAA IPDFQSGAME NWGLTTYRES ALLFDAEKSS ASSKLGITMT VAHELAHQWF
361 GNLVTMEWWN DLWLNEGFAK FMEFVSVSVT HPELKVGDYF FGKCFDAMEV DALNSSHPVS
421 TPVENPAQIR EMFDDVSYDK GACILNMLRE YLSADAFKSG IVQYLQKHSY KNTKNEDLWD
481 SMASICPTDG VKGMDGFCSR SQHSSSSSHW HQEGVDVKTM MNTWTLQKGF PLITITVRGR
541 NVHMKQEHYM KGSDGAPDTG YLWHVPLTFI TSKSDMVHRF LLKTKTDVLI LPEEVEWIKF
601 NVGMNGYYIV HYEDDGWDSL TGLLKGTHTA VSSNDRASLI NNAFQLVSIG KLSIEKALDL
661 SLYLKHETEI MPVFQGLNEL IPMYKLMEKR DMNEVETQFK AFLIRLLRDL IDKQTWTDEG
721 SVSERMLRSQ LLLLACVHNY QPCVQRAEGY FRKWKESNGN LSLPVDVTLA VFAVGAQSTE
781 GWDFLYSKYQ FSLSSTEKSQ IEFALCRTQN KEKLQWLLDE SFKGDKIKTQ EFPQILTLIG
841 RNPVGYPLAW QFLRKNWNKL VQKFELGSSS IAHMVMGTTN QFSTRTRLEE VKGFFSSLKE
901 NGSQLRCVQQ TIETIEENIG WMDKNFDKIR VWLQSEKLER MLocalizationUniProt · AlphaFold · HPA
Whether an antibody against ERAP1 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.
- Antibody reachability
- Other membrane
- Secreted
- No
- Transmembrane segments
- 1
- Mean surface accessibility (rSASA)
- 0.23
- Highest tissue expression
- 60 nTPM
Expression across tissuesHPA
Tissue
- duodenum: 60 nTPM
- thymus: 59 nTPM
- small intestine: 52 nTPM
- adipose tissue: 48 nTPM
- placenta: 44 nTPM
- rectum: 41 nTPM
Single-cell type
- epicardial cells: 1,558 nCPM
- cardiomyocytes: 644 nCPM
- adipocytes: 217 nCPM
- endometrial glandular cells: 203 nCPM
- fibro-adipogenic progenitors: 150 nCPM
- myonuclei: 135 nCPM
Immune cell
- basophil: 29 nTPM
- NK-cell: 23 nTPM
- gdT-cell: 23 nTPM
- naive CD4 T-cell: 22 nTPM
- non-classical monocyte: 21 nTPM
- MAIT T-cell: 20 nTPM
Brain region
- cerebral cortex: 36 nTPM
- medulla oblongata: 35 nTPM
- thalamus: 32 nTPM
- white matter: 31 nTPM
- midbrain: 29 nTPM
- hypothalamus: 28 nTPM
Genetic constraint and essentialitygnomAD · DepMap
Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.
- gnomAD LOEUF (loss-of-function intolerance)
- 1.13
- gnomAD pLI
- 0
- gnomAD missense Z
- 0.53
- DepMap mean gene effect
- -0.03
- DepMap dependency class
- none
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 5% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- adaptive immune response
- angiogenesis
- antigen processing and presentation of endogenous peptide antigen via MHC class I
- antigen processing and presentation of peptide antigen via MHC class I
- fat cell differentiation
- membrane protein ectodomain proteolysis
- peptide catabolic process
- positive regulation of angiogenesis
- proteolysis
- regulation of blood pressure
- regulation of innate immune response
- response to bacterium
Molecular functions
- aminopeptidase activity
- endopeptidase activity
- interleukin-1, type II receptor binding
- interleukin-6 receptor binding
- metalloaminopeptidase activity
- metalloexopeptidase activity
- zinc ion binding
Cellular components
Protein domainsUniProt · Pfam · InterPro
- Peptidase M1, alanine aminopeptidase/leukotriene A4 hydrolase
- Peptidase M1, membrane alanine aminopeptidase
- ERAP1-like C-terminal domain
- Peptidase M4/M1, CTD superfamily
- Aminopeptidase N-type
- Aminopeptidase N-like , N-terminal domain superfamliy
- Aminopeptidase N-like , N-terminal domain
- Peptidase M1 family aminopeptidases
- Peptidase family M1 domain
- ERAP1-like C-terminal domain
- Peptidase M1 N-terminal domain
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of ERAP1 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads ERAP1 as an antibody target. Whether an autoantibody or antibody against ERAP1 could matter depends on whether native ERAP1 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
ERAP1 is annotated as predominantly intracellular. Intracellular proteins are common autoantibody markers, becoming visible to the immune system after cell injury or altered processing, but are usually markers of disease rather than direct drivers.
Annotation status
The present source text does not explicitly label ERAP1 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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