P97449
PR
Gene name |
Anpep (Lap-1, Lap1) |
Protein name |
Aminopeptidase N |
Names |
|
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:16790 |
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 P97449
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P97449-F1 | Predicted | AlphaFoldDB |
78 variants for P97449
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3398311637 | 19 | G>A | No | EVA | |
| rs3388921025 | 19 | G>C | No | EVA | |
| rs254615395 | 47 | A>T | No | EVA | |
| rs3388879674 | 55 | S>L | No | EVA | |
| rs3388899909 | 58 | T>I | No | EVA | |
| rs3388916416 | 86 | R>W | No | EVA | |
| rs3388916407 | 90 | R>G | No | EVA | |
| rs235793617 | 97 | N>S | No | EVA | |
| rs222660145 | 147 | A>V | No | EVA | |
| rs3398193752 | 167 | Q>* | No | EVA | |
| rs259981690 | 168 | G>E | No | EVA | |
| rs3388924014 | 175 | Q>K | No | EVA | |
| rs3398210767 | 179 | D>V | No | EVA | |
| rs240556356 | 181 | Q>E | No | EVA | |
| rs3388893368 | 185 | E>K | No | EVA | |
| rs224013850 | 202 | D>G | No | EVA | |
| rs3388902863 | 214 | A>T | No | EVA | |
| rs3388899919 | 223 | C>W | No | EVA | |
| rs244681598 | 241 | N>S | No | EVA | |
| rs3388921048 | 243 | L>F | No | EVA | |
| rs3388902873 | 249 | M>V | No | EVA | |
| rs3388879700 | 256 | P>S | No | EVA | |
| rs3388918110 | 265 | M>I | No | EVA | |
| rs3388902916 | 272 | P>T | No | EVA | |
| rs3397996198 | 280 | A>S | No | EVA | |
| rs3388923993 | 290 | S>I | No | EVA | |
| rs3388893360 | 294 | A>T | No | EVA | |
| rs3388899889 | 305 | P>H | No | EVA | |
| rs3388917736 | 317 | L>V | No | EVA | |
| rs3388899921 | 355 | N>S | No | EVA | |
| rs3388893378 | 359 | V>A | No | EVA | |
| rs3388924056 | 384 | V>L | No | EVA | |
| rs3388917783 | 402 | W>* | No | EVA | |
| rs3388908855 | 411 | G>S | No | EVA | |
| rs3388893339 | 509 | S>L | No | EVA | |
| rs3412945627 | 530 | V>A | No | EVA | |
| rs220446951 | 530 | V>I | No | EVA | |
| rs581926568 | 531 | Q>* | No | EVA | |
| rs8279795 | 531 | Q>H | No | EVA | |
| rs8279794 | 532 | P>L | No | EVA | |
| rs8279793 | 557 | N>S | No | EVA | |
| rs213430640 | 583 | I>T | No | EVA | |
| rs3388916413 | 593 | S>N | No | EVA | |
| rs244107981 | 602 | D>N | No | EVA | |
| rs8279788 | 603 | V>A | No | EVA | |
| rs3398114361 | 624 | N>K | No | EVA | |
| rs3398131888 | 625 | V>L | No | EVA | |
| rs3397905959 | 627 | G>S | No | EVA | |
| rs3398131828 | 628 | Y>* | No | EVA | |
| rs3398193737 | 629 | Y>* | No | EVA | |
| rs3398193808 | 630 | L>P | No | EVA | |
| rs3388924885 | 632 | N>K | No | EVA | |
| rs3388917738 | 639 | K>R | No | EVA | |
| rs3388899904 | 657 | R>L | No | EVA | |
| rs3388921482 | 662 | H>Y | No | EVA | |
| rs13474937 | 689 | A>T | No | EVA | |
| rs3388908892 | 690 | E>D | No | EVA | |
| rs3398161076 | 698 | L>Q | No | EVA | |
| rs3398193791 | 699 | S>G | No | EVA | |
| rs3388921056 | 711 | S>W | No | EVA | |
| rs13474938 | 726 | T>M | No | EVA | |
| rs3398311598 | 745 | T>K | No | EVA | |
| rs3388916350 | 760 | C>F | No | EVA | |
| rs3388906719 | 775 | Y>C | No | EVA | |
| rs235438144 | 781 | N>T | No | EVA | |
| rs227203719 | 817 | N>T | No | EVA | |
| rs3388913522 | 824 | A>G | No | EVA | |
| rs3388917747 | 838 | W>C | No | EVA | |
| rs3388917716 | 847 | T>I | No | EVA | |
| rs3388906700 | 879 | V>I | No | EVA | |
| rs3388893344 | 921 | K>N | No | EVA | |
| rs3388921050 | 929 | F>S | No | EVA | |
| rs3388906729 | 954 | K>* | No | EVA | |
| rs226901879 | 956 | A>V | No | EVA | |
| rs3398137980 | 957 | V>G | No | EVA | |
| rs1132564607 | 966 | S>C | No | EVA | |
| rs1132564607 | 966 | S>G | No | EVA | |
| rs3398114455 | 967 | S>C | No | EVA |
No associated diseases with P97449
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 | |
8 GO annotations of cellular component
| Name | Definition |
|---|---|
| brush border membrane | The portion of the plasma membrane surrounding the brush border. |
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| endoplasmic reticulum-Golgi intermediate compartment | A complex system of membrane-bounded compartments located between endoplasmic reticulum (ER) and the Golgi complex, with a distinctive membrane protein composition; involved in ER-to-Golgi and Golgi-to-ER transport. |
| external side of plasma membrane | The leaflet of the plasma membrane that faces away from the cytoplasm and any proteins embedded or anchored in it or attached to its surface. |
| extracellular exosome | A vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane. Extracellular exosomes, also simply called exosomes, have a diameter of about 40-100 nm. |
| extracellular space | That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid. |
| 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. |
4 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. |
| zinc ion binding | Binding to a zinc ion (Zn). |
8 GO annotations of biological process
| Name | Definition |
|---|---|
| angiogenesis | Blood vessel formation when new vessels emerge from the proliferation of pre-existing blood vessels. |
| cell differentiation | The process in which relatively unspecialized cells, e.g. embryonic or regenerative cells, acquire specialized structural and/or functional features that characterize the cells, tissues, or organs of the mature organism or some other relatively stable phase of the organism's life history. Differentiation includes the processes involved in commitment of a cell to a specific fate and its subsequent development to the mature state. |
| negative regulation of renal sodium excretion | Any process that decreases the amount of sodium excreted in urine over a unit of time. |
| 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. |
| protein processing | Any protein maturation process achieved by the cleavage of a peptide bond or bonds within a protein. Protein maturation is the process leading to the attainment of the full functional capacity of a protein. |
| 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 |
| Q9UKU6 | TRHDE | Thyrotropin-releasing hormone-degrading ectoenzyme | Homo sapiens (Human) | PR |
| Q9NZ08 | ERAP1 | Endoplasmic reticulum aminopeptidase 1 | Homo sapiens (Human) | PR |
| P55786 | NPEPPS | Puromycin-sensitive aminopeptidase | Homo sapiens (Human) | PR |
| P15144 | ANPEP | Aminopeptidase N | Homo sapiens (Human) | 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 |
| Q10836 | Trhde | Thyrotropin-releasing hormone-degrading ectoenzyme | Rattus norvegicus (Rat) | PR |
| Q9JJ22 | Erap1 | Endoplasmic reticulum aminopeptidase 1 | Rattus norvegicus (Rat) | PR |
| P97629 | Lnpep | Leucyl-cystinyl aminopeptidase | Rattus norvegicus (Rat) | PR |
| P15684 | Anpep | Aminopeptidase N | 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 |
| MAKGFYISKT | LGILGILLGV | AAVCTIIALS | VVYAQEKNRN | AENSATAPTL | PGSTSATTAT |
| 70 | 80 | 90 | 100 | 110 | 120 |
| TTPAVDESKP | WNQYRLPKTL | IPDSYRVILR | PYLTPNNQGL | YIFQGNSTVR | FTCNQTTDVI |
| 130 | 140 | 150 | 160 | 170 | 180 |
| IIHSKKLNYT | LKGNHRVVLR | TLDGTPAPNI | DKTELVERTE | YLVVHLQGSL | VEGRQYEMDS |
| 190 | 200 | 210 | 220 | 230 | 240 |
| QFQGELADDL | AGFYRSEYME | GDVKKVVATT | QMQAADARKS | FPCFDEPAMK | AMFNITLIYP |
| 250 | 260 | 270 | 280 | 290 | 300 |
| NNLIALSNML | PKESKPYPED | PSCTMTEFHS | TPKMSTYLLA | YIVSEFKNIS | SVSANGVQIG |
| 310 | 320 | 330 | 340 | 350 | 360 |
| IWARPSAIDE | GQGDYALNVT | GPILNFFAQH | YNTSYPLPKS | DQIALPDFNA | GAMENWGLVT |
| 370 | 380 | 390 | 400 | 410 | 420 |
| YRESSLVFDS | QSSSISNKER | VVTVIAHELA | HQWFGNLVTV | AWWNDLWLNE | GFASYVEYLG |
| 430 | 440 | 450 | 460 | 470 | 480 |
| ADYAEPTWNL | KDLMVLNDVY | RVMAVDALAS | SHPLSSPADE | IKTPDQIMEL | FDSITYSKGA |
| 490 | 500 | 510 | 520 | 530 | 540 |
| SVIRMLSSFL | TEDLFKKGLS | SYLHTYQYSN | TVYLDLWEHL | QKAVNQQTAV | QPPATVRTIM |
| 550 | 560 | 570 | 580 | 590 | 600 |
| DRWILQMGFP | VITVNTNTGE | ISQKHFLLDS | KSNVTRPSEF | NYIWIAPIPF | LKSGQEDHYW |
| 610 | 620 | 630 | 640 | 650 | 660 |
| LDVEKNQSAK | FQTSSNEWIL | LNINVTGYYL | VNYDENNWKK | LQNQLQTDLS | VIPVINRAQI |
| 670 | 680 | 690 | 700 | 710 | 720 |
| IHDSFNLASA | KMIPITLALD | NTLFLVKEAE | YMPWQAALSS | LNYFTLMFDR | SEVYGPMKRY |
| 730 | 740 | 750 | 760 | 770 | 780 |
| LKKQVTPLFF | YFQNRTNNWV | NRPPTLMEQY | NEINAISTAC | SSGLKECRDL | VVELYSQWMK |
| 790 | 800 | 810 | 820 | 830 | 840 |
| NPNNNTIHPN | LRSTVYCNAI | AFGGEEEWNF | AWEQFRNATL | VNEADKLRSA | LACSKDVWIL |
| 850 | 860 | 870 | 880 | 890 | 900 |
| NRYLSYTLNP | DYIRKQDTTS | TIISIASNVA | GHPLVWDFVR | SNWKKLFENY | GGGSFSFANL |
| 910 | 920 | 930 | 940 | 950 | 960 |
| IQGVTRRFSS | EFELQQLEQF | KADNSATGFG | TGTRALEQAL | EKTRANIDWV | KENKDAVFKW |
| FTENSS |