Q6K4E7
PR
Gene name |
Os09g0362800 (LOC_Os09g19800/LOC_Os09g19820, OJ1506_A04.11) |
Protein name |
Aminopeptidase M1-D |
Names |
Alpha-aminoacylpeptide hydrolase |
Species |
Oryza sativa subsp japonica (Rice) |
KEGG Pathway |
osa:4346856 |
EC number |
3.4.11.2: Aminopeptidases |
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 Q6K4E7
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q6K4E7-F1 | Predicted | AlphaFoldDB |
No variants for Q6K4E7
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q6K4E7 | |||||
No associated diseases with Q6K4E7
Functions
| Description | ||
|---|---|---|
| EC Number | 3.4.11.2 | Aminopeptidases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| endoplasmic reticulum | The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached). |
| membrane | A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it. |
3 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. |
| peptide binding | Binding to a peptide, an organic compound comprising two or more amino acids linked by peptide bonds. |
| zinc ion binding | Binding to a zinc ion (Zn). |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| peptide catabolic process | The chemical reactions and pathways resulting in the breakdown of peptides, compounds of 2 or more (but usually less than 100) amino acids where the alpha carboxyl group of one is bound to the alpha amino group of another. |
| proteolysis | The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. |
23 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| P40462 | TMA108 | Protein TMA108 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | PR |
| P32454 | APE2 | Aminopeptidase 2, mitochondrial | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | PR |
| P79171 | ANPEP | Aminopeptidase N | Felis catus (Cat) (Felis silvestris catus) | PR |
| P15144 | ANPEP | Aminopeptidase N | Homo sapiens (Human) | PR |
| Q9NZ08 | ERAP1 | Endoplasmic reticulum aminopeptidase 1 | Homo sapiens (Human) | PR |
| Q9UIQ6 | LNPEP | Leucyl-cystinyl aminopeptidase | Homo sapiens (Human) | PR |
| Q9UKU6 | TRHDE | Thyrotropin-releasing hormone-degrading ectoenzyme | Homo sapiens (Human) | PR |
| A6NEC2 | NPEPPSL1 | Puromycin-sensitive aminopeptidase-like protein | Homo sapiens (Human) | PR |
| P55786 | NPEPPS | Puromycin-sensitive aminopeptidase | Homo sapiens (Human) | PR |
| P97449 | Anpep | Aminopeptidase N | Mus musculus (Mouse) | PR |
| Q11011 | Npepps | Puromycin-sensitive aminopeptidase | Mus musculus (Mouse) | PR |
| Q8C129 | Lnpep | Leucyl-cystinyl aminopeptidase | Mus musculus (Mouse) | PR |
| Q8K093 | Trhde | Thyrotropin-releasing hormone-degrading ectoenzyme | Mus musculus (Mouse) | PR |
| Q9EQH2 | Erap1 | Endoplasmic reticulum aminopeptidase 1 | Mus musculus (Mouse) | PR |
| P15145 | ANPEP | Aminopeptidase N | Sus scrofa (Pig) | PR |
| P15684 | Anpep | Aminopeptidase N | Rattus norvegicus (Rat) | PR |
| P97629 | Lnpep | Leucyl-cystinyl aminopeptidase | Rattus norvegicus (Rat) | PR |
| Q10836 | Trhde | Thyrotropin-releasing hormone-degrading ectoenzyme | Rattus norvegicus (Rat) | PR |
| Q9JJ22 | Erap1 | Endoplasmic reticulum aminopeptidase 1 | Rattus norvegicus (Rat) | PR |
| Q0J5V5 | Os08g0398700 | Aminopeptidase M1-B | Oryza sativa subsp japonica (Rice) | PR |
| Q6Z6L4 | Os02g0218200 | Aminopeptidase M1-A | Oryza sativa subsp japonica (Rice) | PR |
| Q17405 | AC3.5 | Aminopeptidase-like protein AC3.5 | Caenorhabditis elegans | PR |
| Q8VZH2 | APM1 | Aminopeptidase M1 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAAAAAEFRG | QARLPRFAAP | RRYELRLRPD | LAACVFSGEA | SVAVDVSAPT | RFLVLNAADL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| AVDRASIRFQ | GLAPAEVSVF | EEDEILVLEF | AGELPLGEGV | LAMRFNGTLN | DQMRGFYRSK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| YEYKGETKNM | AVTQFESVDA | RRCFPCWDEP | SFKAKFKLTL | EVPSELVALS | NMPIVNEKIA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| GPIKTVEYEE | SPVMSTYLVA | IVVGLFDYIE | GVTSEGNKVR | VYTQVGKSNQ | GKFALDVGVK |
| 250 | 260 | 270 | 280 | 290 | 300 |
| SLNLYKEFFD | TPYPLPKLDM | VAIPDFTNGA | MENYGLVTYR | EIYLLFDEQS | SSASTKQNVA |
| 310 | 320 | 330 | 340 | 350 | 360 |
| ITVAHELAHQ | WFGNLVTMEW | WTHLWLNEGF | ATWMSYLAVD | SFFPEWNIWT | QFLDSTTSAL |
| 370 | 380 | 390 | 400 | 410 | 420 |
| KLDSLAESHP | IEVEIHHASE | IDSIFDSISY | DKGASVIRML | QSYLGAERFQ | KALASYIKKY |
| 430 | 440 | 450 | 460 | 470 | 480 |
| AYSNAKTEDL | WAVLEEVSGE | PVKNLMTTWT | KKQGYPVIGV | KLKGHDVELE | QDQFLLDGSS |
| 490 | 500 | 510 | 520 | 530 | 540 |
| DSGMWIVPIT | LGCNSHDMQK | RFLLKHKFSD | IKGINSQYDD | QDRQNSGNFW | IKLNIDETGF |
| 550 | 560 | 570 | 580 | 590 | 600 |
| YRVKYDDELT | TALRNALQMK | KLSLMDKIGI | VEDAHALSIA | GKQTLSSLLH | LLYACRDEDD |
| 610 | 620 | 630 | 640 | 650 | 660 |
| FSVLSHINSV | TSSVAKISID | ATPELAGEIK | QLFIKLLLPT | AEKLGWDPKN | SESHLDAMLR |
| 670 | 680 | 690 | 700 | 710 | 720 |
| PVLLVGLVQL | GHDKTISEGV | RRFQIFFDDR | NTSLPPDTRK | AAYLSVMHNV | SSTNRSGYDA |
| 730 | 740 | 750 | 760 | 770 | 780 |
| LLKIYRESTE | VEERLNVLGI | LSSCQDKDIV | LESLNFIFTD | EVRNQDAYLV | LRSVIIDARE |
| 790 | 800 | 810 | 820 | 830 | 840 |
| TAWSWLKENW | DRITKTFAAS | AILSDYVKSI | VTLFTSKEKE | AEISQFFATR | TKPGFKRALK |
| 850 | 860 | 870 | |||
| QSLENVRISA | RWVDGIRGEA | ELAQTVHDLL | IKL |