Q10836
PR
Gene name |
Trhde |
Protein name |
Thyrotropin-releasing hormone-degrading ectoenzyme |
Names |
TRH-DE, TRH-degrading ectoenzyme, Pyroglutamyl-peptidase II, PAP-II, TRH-specific aminopeptidase, Thyroliberinase |
Species |
Rattus norvegicus (Rat) |
KEGG Pathway |
|
EC number |
3.4.19.6: Omega peptidases |
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 Q10836
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q10836-F1 | Predicted | AlphaFoldDB |
No variants for Q10836
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q10836 | |||||
No associated diseases with Q10836
Functions
| Description | ||
|---|---|---|
| EC Number | 3.4.19.6 | Omega peptidases |
| 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. |
| 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. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
5 GO annotations of molecular function
| Name | Definition |
|---|---|
| aminopeptidase activity | Catalysis of the hydrolysis of a single N-terminal amino acid residue from a polypeptide chain. |
| 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. |
| pyroglutamyl-peptidase activity | Catalysis of the release of the N-terminal pyroglutamyl group from a peptide or protein. |
| zinc ion binding | Binding to a zinc ion (Zn). |
4 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. |
| regulation of blood pressure | Any process that modulates the force with which blood travels through the circulatory system. The process is controlled by a balance of processes that increase pressure and decrease pressure. |
| signal transduction | The cellular process in which a signal is conveyed to trigger a change in the activity or state of a cell. Signal transduction begins with reception of a signal (e.g. a ligand binding to a receptor or receptor activation by a stimulus such as light), or for signal transduction in the absence of ligand, signal-withdrawal or the activity of a constitutively active receptor. Signal transduction ends with regulation of a downstream cellular process, e.g. regulation of transcription or regulation of a metabolic process. Signal transduction covers signaling from receptors located on the surface of the cell and signaling via molecules located within the cell. For signaling between cells, signal transduction is restricted to events at and within the receiving cell. |
22 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 |
| Q9UIQ6 | LNPEP | Leucyl-cystinyl aminopeptidase | Homo sapiens (Human) | PR |
| Q9NZ08 | ERAP1 | Endoplasmic reticulum aminopeptidase 1 | Homo sapiens (Human) | PR |
| P15144 | ANPEP | Aminopeptidase N | Homo sapiens (Human) | PR |
| P55786 | NPEPPS | Puromycin-sensitive aminopeptidase | Homo sapiens (Human) | PR |
| Q9UKU6 | TRHDE | Thyrotropin-releasing hormone-degrading ectoenzyme | Homo sapiens (Human) | PR |
| Q11011 | Npepps | Puromycin-sensitive aminopeptidase | Mus musculus (Mouse) | PR |
| Q8C129 | Lnpep | Leucyl-cystinyl aminopeptidase | Mus musculus (Mouse) | PR |
| P97449 | Anpep | Aminopeptidase N | Mus musculus (Mouse) | PR |
| Q9EQH2 | Erap1 | Endoplasmic reticulum aminopeptidase 1 | Mus musculus (Mouse) | PR |
| Q8K093 | Trhde | Thyrotropin-releasing hormone-degrading ectoenzyme | 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 |
| 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 |
| Q6K4E7 | Os09g0362800 | Aminopeptidase M1-D | 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 |
| MGEDDAALRA | SGRGLSDPWA | DSVGVRPRTT | ERHIAVHKRL | VLAFAVSIVA | LLAVTMLAVL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LSLRFDECGA | SAAMPGTDGG | LGGFPERGGN | SSYPGSARRN | HHAGEESSQR | EIGEVGTAGT |
| 130 | 140 | 150 | 160 | 170 | 180 |
| PSAHPPSEEE | QEQWQPWTQL | RLSGHLKPLH | YNLMLTAFME | NFTFSGEVNV | EIACQNATRY |
| 190 | 200 | 210 | 220 | 230 | 240 |
| VVLHASRVAV | EKVQVAEDRA | FGAVPVAGFF | LYPQTQVLVV | VLNRTLDAQR | HYNLKIIYNA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LIENELLGFF | RSSYVIHGER | RFLGVTQFSP | THARKAFPCF | DEPIYKATFK | ISIKHQATYL |
| 310 | 320 | 330 | 340 | 350 | 360 |
| SLSNMPVETS | VFEEDGWVTD | HFSQTPLMST | YYLAWAICNF | TYRETTTKSG | VVVRLYARPD |
| 370 | 380 | 390 | 400 | 410 | 420 |
| AIRRGSGDYA | LHITKRLIEF | YEDYFKVPYS | LPKLDLLAVP | KHPYAAMENW | GLSIFVEQRI |
| 430 | 440 | 450 | 460 | 470 | 480 |
| LLDPSVSSIS | YLLDVTMVIV | HEICHQWFGD | LVTPVWWEDV | WLKEGFAHYF | EFVGTDYLYP |
| 490 | 500 | 510 | 520 | 530 | 540 |
| SWNMEKQRFL | TDVLHEVMLL | DGLASSHPVS | QEVLRATDID | KVFDWIAYKK | GAALIRMLAN |
| 550 | 560 | 570 | 580 | 590 | 600 |
| FMGHSVFQRG | LQDYLTIHKY | GNAARNDLWN | TLSEALKRNG | KYVNIQEVMD | QWTLQMGYPV |
| 610 | 620 | 630 | 640 | 650 | 660 |
| ITILGNMTAE | NRILITQQHF | IYDIGAKTKA | LQLQNSSYLW | QIPLTIVVGN | RSHVSSEAII |
| 670 | 680 | 690 | 700 | 710 | 720 |
| WVSNKSEHHR | ITYLDKGSWI | LGNINQTGYF | RVNYDLRNWR | LLIDQLIRNH | EVLSVSNRAG |
| 730 | 740 | 750 | 760 | 770 | 780 |
| LIDDAFSLAR | AGYLPQNIPL | EIIRYLSEEK | DFLPWHAASR | ALYPLDKLLD | RMENYNIFNE |
| 790 | 800 | 810 | 820 | 830 | 840 |
| YILKQVATTY | SKLGWPKNNF | NGSVVQASYQ | HEELRREVIM | LACSFGNKHC | HQQASTLISD |
| 850 | 860 | 870 | 880 | 890 | 900 |
| WISSNRNRIP | LNVRDIVYCT | GVSLLDEDVW | EFIWMKFHST | TAVSEKKILL | EALTCSDDRN |
| 910 | 920 | 930 | 940 | 950 | 960 |
| LLSRLLNLSL | NSEVVLDQDA | IDVIIHVARN | PHGRDLAWKF | FRDKWKILNT | RYGEALFMNS |
| 970 | 980 | 990 | 1000 | 1010 | 1020 |
| KLISGVTEFL | NTEGELKELK | NFMKSYDGVA | SASFSRAVET | VEANVRWKRL | YQDELFQWLG |
| KAMRH |