Q5RFP3
Gene name |
ERAP2 |
Protein name |
Endoplasmic reticulum aminopeptidase 2 |
Names |
|
Species |
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) |
KEGG Pathway |
pon:100171433 |
EC number |
|
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q5RFP3
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q5RFP3-F1 | Predicted | AlphaFoldDB |
No variants for Q5RFP3
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q5RFP3 | |||||
No associated diseases with Q5RFP3
5 regional properties for Q5RFP3
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | RNA recognition motif domain | 39 - 117 | IPR000504-1 |
| domain | RNA recognition motif domain | 125 - 205 | IPR000504-2 |
| domain | RNA recognition motif domain | 277 - 355 | IPR000504-3 |
| domain | HuB, RNA recognition motif 3 | 274 - 359 | IPR034914 |
| domain | HuB, RNA recognition motif 2 | 120 - 203 | IPR034999 |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| endoplasmic reticulum membrane | The lipid bilayer surrounding the endoplasmic reticulum. |
| integral component of membrane | The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| metalloaminopeptidase activity | Catalysis of the hydrolysis of a single N-terminal amino acid residue from a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions. |
| zinc ion binding | Binding to a zinc ion (Zn). |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| adaptive immune response | An immune response mediated by cells expressing specific receptors for antigen produced through a somatic diversification process, and allowing for an enhanced secondary response to subsequent exposures to the same antigen (immunological memory). |
| antigen processing and presentation of endogenous peptide antigen via MHC class I | The process in which an antigen-presenting cell expresses a peptide antigen of endogenous origin on its cell surface in association with an MHC class I protein complex. The peptide antigen is typically, but not always, processed from a whole protein. Class I here refers to classical class I molecules. |
| proteolysis | The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MLHSSAMVNS | HRKSMFNIHK | GFYCLAAILP | QICICSQFSV | PSSYHFSEDP | GAFPVATNGE |
| 70 | 80 | 90 | 100 | 110 | 120 |
| RFPWQELRLP | SVVIPLHYDL | FVHPNLTSLD | FVASEKIEVL | VSNATQFIIL | HSKDLEITNA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| TLQSEEDSRY | MKPGKELKVL | SYPAHQQIAL | LVPEKLMPHL | KYYVAIDFQA | KLGDGFEGFY |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KSTYRTLGGE | TRILAVTDFE | PTQARMAFPC | FDEPLFKANF | SIKIRRESGH | IALSNMPKVR |
| 250 | 260 | 270 | 280 | 290 | 300 |
| TIELEGGLLE | DHFETTVKMS | TYLVAYIVCD | FHSVSGITSS | GVKVSIYASP | DKQNQTHYAL |
| 310 | 320 | 330 | 340 | 350 | 360 |
| QASLKLLDFY | EKYFDIYYPL | SKLDLIAIPD | FASGAMENWG | LITYRETSLL | FDPKTSSASD |
| 370 | 380 | 390 | 400 | 410 | 420 |
| KLWVTRVIAH | ELAHQWFGNL | VTMEWWNDIW | LKEGFAKYME | LIAVNATYPE | LQFDDYFLNV |
| 430 | 440 | 450 | 460 | 470 | 480 |
| CFEVITKDSL | NSSRPISKPA | ETPTQIQEMF | DEVSYNKGAC | ILNMLKDFLG | EEKFQKGIIQ |
| 490 | 500 | 510 | 520 | 530 | 540 |
| YLKKFSYRNA | KNDDLWSSLS | NSCLESDFTS | GGVCHSDPKM | TSNMLTFLGE | NAEVKEMMTT |
| 550 | 560 | 570 | 580 | 590 | 600 |
| WTLQKGIPLL | VVKQDGCSLR | LQQERFLQGV | FQEDPEWRAL | QERYLWHIPL | TYSTSSSNVI |
| 610 | 620 | 630 | 640 | 650 | 660 |
| HRHILKSKTD | TLDLPEKTSW | VKFNVDSNGY | YIVHYEGHGW | DQLITQLNQN | HTLLRPKDRV |
| 670 | 680 | 690 | 700 | 710 | 720 |
| GLIHDVFQLV | GAGRLTLDKA | LDMTHYLQHE | TSSPALLEGL | SYLELFYHMM | DRRNISDISE |
| 730 | 740 | 750 | 760 | 770 | 780 |
| NLKRYLLQYF | KPVIDRQSWS | DEGSVWDRML | RSALLKLACD | LNHAPCIQKA | TELFSQWMES |
| 790 | 800 | 810 | 820 | 830 | 840 |
| SGKLNIPTDV | LKIVYSVGAQ | TAAGWNYLLE | QYELSMSSAE | QNKILYALST | SKHQEKLLKL |
| 850 | 860 | 870 | 880 | 890 | 900 |
| IELGMEGKVI | KTQNLAALLH | VIARRPKGQQ | LAWDFVRENW | THLLKKFDLG | SFDIRMIISG |
| 910 | 920 | 930 | 940 | 950 | |
| TTARFSSKDK | LQEVKLFFES | LEAQGSHLDI | FQIVLETITK | NIKWLEKNLP | TLRTWLLVNT |