Q58DD0
Gene name |
ACE2 |
Protein name |
Angiotensin-converting enzyme 2 |
Names |
ACE-related carboxypeptidase |
Species |
Bos taurus (Bovine) |
KEGG Pathway |
|
EC number |
3.4.17.23: Metallocarboxypeptidases |
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 Q58DD0
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q58DD0-F1 | Predicted | AlphaFoldDB |
No variants for Q58DD0
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q58DD0 | |||||
No associated diseases with Q58DD0
1 regional properties for Q58DD0
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Collectrin domain | 616 - 769 | IPR031588 |
Functions
| Description | ||
|---|---|---|
| EC Number | 3.4.17.23 | Metallocarboxypeptidases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
7 GO annotations of cellular component
| Name | Definition |
|---|---|
| apical plasma membrane | The region of the plasma membrane located at the apical end of the cell. |
| cell surface | The external part of the cell wall and/or plasma membrane. |
| cilium | A specialized eukaryotic organelle that consists of a filiform extrusion of the cell surface and of some cytoplasmic parts. Each cilium is largely bounded by an extrusion of the cytoplasmic (plasma) membrane, and contains a regular longitudinal array of microtubules, anchored to a basal body. |
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| 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. |
5 GO annotations of molecular function
| Name | Definition |
|---|---|
| carboxypeptidase activity | Catalysis of the hydrolysis of a single C-terminal amino acid residue from a polypeptide chain. |
| metal ion binding | Binding to a metal ion. |
| metallopeptidase activity | Catalysis of the hydrolysis of peptide bonds 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. |
| peptidyl-dipeptidase activity | Catalysis of the release of C-terminal dipeptides from a polypeptide chain. |
| virus receptor activity | Combining with a virus component and mediating entry of the virus into the cell. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| 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 |
| MTGSFWLLLS | LVAVTAAQST | TEEQAKTFLE | KFNHEAEDLS | YQSSLASWNY | NTNITDENVQ |
| 70 | 80 | 90 | 100 | 110 | 120 |
| KMNEARAKWS | AFYEEQSRMA | KTYSLEEIQN | LTLKRQLKAL | QHSGTSALSA | EKSKRLNTIL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| NKMSTIYSTG | KVLDPNTQEC | LALEPGLDDI | MENSRDYNRR | LWAWEGWRAE | VGKQLRPLYE |
| 190 | 200 | 210 | 220 | 230 | 240 |
| EYVVLENEMA | RANNYEDYGD | YWRGDYEVTG | AGDYDYSRDQ | LMKDVERTFA | EIKPLYEQLH |
| 250 | 260 | 270 | 280 | 290 | 300 |
| AYVRAKLMHT | YPSYISPTGC | LPAHLLGDMW | GRFWTNLYSL | TVPFEHKPSI | DVTEKMENQS |
| 310 | 320 | 330 | 340 | 350 | 360 |
| WDAERIFKEA | EKFFVSISLP | YMTQGFWDNS | MLTEPGDGRK | VVCHPTAWDL | GKGDFRIKMC |
| 370 | 380 | 390 | 400 | 410 | 420 |
| TKVTMDDFLT | AHHEMGHIQY | DMAYAAQPYL | LRNGANEGFH | EAVGEIMSLS | AATPHYLKAL |
| 430 | 440 | 450 | 460 | 470 | 480 |
| GLLAPDFHED | NETEINFLLK | QALTIVGTLP | FTYMLEKWRW | MVFKGEIPKQ | QWMEKWWEMK |
| 490 | 500 | 510 | 520 | 530 | 540 |
| REIVGVVEPL | PHDETYCDPA | CLFHVAEDYS | FIRYYTRTIY | QFQFHEALCK | TAKHEGALFK |
| 550 | 560 | 570 | 580 | 590 | 600 |
| CDISNSTEAG | QRLLQMLRLG | KSEPWTLALE | NIVGIKTMDV | KPLLNYFEPL | FTWLKEQNRN |
| 610 | 620 | 630 | 640 | 650 | 660 |
| SFVGWSTEWT | PYSDQSIKVR | ISLKSALGEN | AYEWNDNEMY | LFQSSVAYAM | RKYFSEARNE |
| 670 | 680 | 690 | 700 | 710 | 720 |
| TVLFGEDNVW | VSDKKPRISF | KFFVTSPNNV | SDIIPRTEVE | NAIRLSRDRI | NDVFQLDDNS |
| 730 | 740 | 750 | 760 | 770 | 780 |
| LEFLGIQPTL | GPPYEPPVTI | WLIIFGVVMG | VVVIGIVVLI | FTGIRNRRKK | NQASSEENPY |
| 790 | 800 | ||||
| GSVDLNKGEN | NSGFQNIDDV | QTSL |