P12822 · ACE_RABIT
- ProteinAngiotensin-converting enzyme
- GeneACE
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1310 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Dipeptidyl carboxypeptidase that removes dipeptides from the C-terminus of a variety of circulating hormones, such as angiotensin I, bradykinin or enkephalins, thereby playing a key role in the regulation of blood pressure, electrolyte homeostasis or synaptic plasticity (PubMed:7902354, PubMed:8171037).
Composed of two similar catalytic domains, each possessing a functional active site, with different selectivity for substrates (By similarity).
Plays a major role in the angiotensin-renin system that regulates blood pressure and sodium retention by the kidney by converting angiotensin I to angiotensin II, resulting in an increase of the vasoconstrictor activity of angiotensin (PubMed:7902354).
Also able to inactivate bradykinin, a potent vasodilator, and therefore enhance the blood pressure response (By similarity).
Acts as a regulator of synaptic transmission by mediating cleavage of neuropeptide hormones, such as substance P, neurotensin or enkephalins (By similarity).
Catalyzes degradation of different enkephalin neuropeptides (Met-enkephalin, Leu-enkephalin, Met-enkephalin-Arg-Phe and possibly Met-enkephalin-Arg-Gly-Leu) (By similarity).
Acts as a regulator of synaptic plasticity in the nucleus accumbens of the brain by mediating cleavage of Met-enkephalin-Arg-Phe, a strong ligand of Mu-type opioid receptor OPRM1, into Met-enkephalin (By similarity).
Met-enkephalin-Arg-Phe cleavage by ACE decreases activation of OPRM1, leading to long-term synaptic potentiation of glutamate release (By similarity).
Also acts as a regulator of hematopoietic stem cell differentiation by mediating degradation of hemoregulatory peptide N-acetyl-SDKP (AcSDKP) (By similarity).
Acts as a regulator of cannabinoid signaling pathway by mediating degradation of hemopressin, an antagonist peptide of the cannabinoid receptor CNR1 (By similarity).
Involved in amyloid-beta metabolism by catalyzing degradation of Amyloid-beta protein 40 and Amyloid-beta protein 42 peptides, thereby preventing plaque formation (By similarity).
Catalyzes cleavage of cholecystokinin (maturation of Cholecystokinin-8 and Cholecystokinin-5) and Gonadoliberin-1 (both maturation and degradation) hormones (PubMed:2554881).
Degradation of hemoregulatory peptide N-acetyl-SDKP (AcSDKP) and amyloid-beta proteins is mediated by the N-terminal catalytic domain, while angiotensin I and cholecystokinin cleavage is mediated by the C-terminal catalytic region (By similarity).
Composed of two similar catalytic domains, each possessing a functional active site, with different selectivity for substrates (By similarity).
Plays a major role in the angiotensin-renin system that regulates blood pressure and sodium retention by the kidney by converting angiotensin I to angiotensin II, resulting in an increase of the vasoconstrictor activity of angiotensin (PubMed:7902354).
Also able to inactivate bradykinin, a potent vasodilator, and therefore enhance the blood pressure response (By similarity).
Acts as a regulator of synaptic transmission by mediating cleavage of neuropeptide hormones, such as substance P, neurotensin or enkephalins (By similarity).
Catalyzes degradation of different enkephalin neuropeptides (Met-enkephalin, Leu-enkephalin, Met-enkephalin-Arg-Phe and possibly Met-enkephalin-Arg-Gly-Leu) (By similarity).
Acts as a regulator of synaptic plasticity in the nucleus accumbens of the brain by mediating cleavage of Met-enkephalin-Arg-Phe, a strong ligand of Mu-type opioid receptor OPRM1, into Met-enkephalin (By similarity).
Met-enkephalin-Arg-Phe cleavage by ACE decreases activation of OPRM1, leading to long-term synaptic potentiation of glutamate release (By similarity).
Also acts as a regulator of hematopoietic stem cell differentiation by mediating degradation of hemoregulatory peptide N-acetyl-SDKP (AcSDKP) (By similarity).
Acts as a regulator of cannabinoid signaling pathway by mediating degradation of hemopressin, an antagonist peptide of the cannabinoid receptor CNR1 (By similarity).
Involved in amyloid-beta metabolism by catalyzing degradation of Amyloid-beta protein 40 and Amyloid-beta protein 42 peptides, thereby preventing plaque formation (By similarity).
Catalyzes cleavage of cholecystokinin (maturation of Cholecystokinin-8 and Cholecystokinin-5) and Gonadoliberin-1 (both maturation and degradation) hormones (PubMed:2554881).
Degradation of hemoregulatory peptide N-acetyl-SDKP (AcSDKP) and amyloid-beta proteins is mediated by the N-terminal catalytic domain, while angiotensin I and cholecystokinin cleavage is mediated by the C-terminal catalytic region (By similarity).
Angiotensin-converting enzyme, soluble form
Soluble form that is released in blood plasma and other body fluids following proteolytic cleavage in the juxtamembrane stalk region.
Isoform Testis-specific
Isoform produced by alternative promoter usage that is specifically expressed in spermatocytes and adult testis, and which is required for male fertility (By similarity).
In contrast to somatic isoforms, only contains one catalytic domain (By similarity).
Acts as a dipeptidyl carboxypeptidase that removes dipeptides from the C-terminus of substrates (PubMed:7902354).
The identity of substrates that are needed for male fertility is unknown (By similarity).
May also have a glycosidase activity which releases GPI-anchored proteins from the membrane by cleaving the mannose linkage in the GPI moiety (By similarity).
The GPIase activity was reported to be essential for the egg-binding ability of the sperm (By similarity).
This activity is however unclear and has been challenged by other groups, suggesting that it may be indirect (PubMed:16270062).
In contrast to somatic isoforms, only contains one catalytic domain (By similarity).
Acts as a dipeptidyl carboxypeptidase that removes dipeptides from the C-terminus of substrates (PubMed:7902354).
The identity of substrates that are needed for male fertility is unknown (By similarity).
May also have a glycosidase activity which releases GPI-anchored proteins from the membrane by cleaving the mannose linkage in the GPI moiety (By similarity).
The GPIase activity was reported to be essential for the egg-binding ability of the sperm (By similarity).
This activity is however unclear and has been challenged by other groups, suggesting that it may be indirect (PubMed:16270062).
Catalytic activity
- angiotensin I + H2O = angiotensin II + L-histidyl-L-leucineThis reaction proceeds in the forward direction.
- bradykinin + H2O = bradykinin(1-7) + L-Phe-L-ArgThis reaction proceeds in the forward direction.
- H2O + substance P = L-Leu-L-Met-NH2 + substance P(1-9)This reaction proceeds in the forward direction.
- H2O + substance P = Gly-L-Leu-L-Met-NH2 + substance P(1-8)This reaction proceeds in the forward direction.
- H2O + substance P = L-Phe-L-Phe-Gly-L-Leu-L-Met-NH2 + substance P(1-6)This reaction proceeds in the forward direction.
- H2O + neurotensin = L-isoleucyl-L-leucine + neurotensin(1-11)This reaction proceeds in the forward direction.
- goralatide + H2O = L-lysyl-L-proline + N-acetyl-L-seryl-L-aspartateThis reaction proceeds in the forward direction.
- H2O + Met-enkephalin = L-phenylalanyl-L-methionine + L-tyrosylglycylglycineThis reaction proceeds in the forward direction.
- H2O + Leu-enkephalin = L-phenylalanyl-L-leucine + L-tyrosylglycylglycineThis reaction proceeds in the forward direction.
- H2O + Met-enkephalin-Arg-Phe = L-arginyl-L-phenylalanine + Met-enkephalinThis reaction proceeds in the forward direction.
Isoform Testis-specific
Release of a C-terminal dipeptide, oligopeptide-|-Xaa-Yaa, when Xaa is not Pro, and Yaa is neither Asp nor Glu. Thus, conversion of angiotensin I to angiotensin II, with increase in vasoconstrictor activity, but no action on angiotensin II.
Cofactor
Protein has several cofactor binding sites:
Note: Binds 2 Zn2+ ions per subunit.
Isoform Testis-specific
Zn2+ (UniProtKB | Rhea| CHEBI:29105 )Note: Isoform Testis-specific only binds 1 Zn2+ ion per subunit.
Note: Binds 3 chloride ions per subunit.
Isoform Testis-specific
chloride (UniProtKB | Rhea| CHEBI:17996 )Activity regulation
The dipeptidyl carboxypeptidase activity is strongly activated by chloride (By similarity).
Specifically inhibited by lisinopril (PubMed:7902354).
Inhibited by mixanpril, an orally-active drug used for the treatment of hypertension (PubMed:8171037).
Specifically inhibited by lisinopril (PubMed:7902354).
Inhibited by mixanpril, an orally-active drug used for the treatment of hypertension (PubMed:8171037).
Isoform Testis-specific
Strongly inhibited by lisinopril and captopril.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.6 mM | Hip-His-Leu | |||||
0.09 mM | angiotensin I |
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 236 | chloride 1 (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 395 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Active site | 396 | Proton acceptor 1 | ||||
Sequence: E | ||||||
Binding site | 399 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 422 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Active site | 524 | Proton donor 1 | ||||
Sequence: H | ||||||
Binding site | 533 | chloride 1 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 795 | chloride 2 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 833 | chloride 3 (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 992 | Zn2+ 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Active site | 993 | Proton acceptor 2 | ||||
Sequence: E | ||||||
Binding site | 996 | Zn2+ 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 1020 | Zn2+ 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Binding site | 1094 | chloride 2 (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 1098 | chloride 2 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Active site | 1122 | Proton donor 2 | ||||
Sequence: H | ||||||
Binding site | 1131 | chloride 3 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Site | 1236-1237 | Cleavage | ||||
Sequence: RS |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | extracellular region | |
Cellular Component | extracellular space | |
Cellular Component | plasma membrane | |
Molecular Function | calmodulin binding | |
Molecular Function | carboxypeptidase activity | |
Molecular Function | chloride ion binding | |
Molecular Function | metal ion binding | |
Molecular Function | metallodipeptidase activity | |
Molecular Function | metalloendopeptidase activity | |
Molecular Function | peptidase activity | |
Molecular Function | peptidyl-dipeptidase activity | |
Biological Process | angiotensin maturation | |
Biological Process | bradykinin catabolic process | |
Biological Process | hormone catabolic process | |
Biological Process | hormone metabolic process | |
Biological Process | kidney development | |
Biological Process | positive regulation of systemic arterial blood pressure | |
Biological Process | regulation of blood pressure | |
Biological Process | regulation of synaptic plasticity | |
Biological Process | substance P catabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameAngiotensin-converting enzyme
- EC number
- Short namesACE
- Alternative names
- Cleaved into 1 chains
- CD Antigen Name
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Lagomorpha > Leporidae > Oryctolagus
Accessions
- Primary accessionP12822
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass type I membrane protein
Note: Detected in both cell membrane and cytoplasm in neurons.
Angiotensin-converting enzyme, soluble form
Isoform Testis-specific
Cell membrane ; Single-pass type I membrane protein
Note: The testis-specific isoform can be cleaved before the transmembrane region, releasing a soluble form.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 34-1260 | Extracellular | ||||
Sequence: TLDPGLLPGDFAADEAGARLFASSYNSSAEQVLFRSTAASWAHDTNITAENARRQEEEALLSQEFAEAWGKKAKELYDPVWQNFTDPELRRIIGAVRTLGPANLPLAKRQQYNSLLSNMSQIYSTGKVCFPNKTASCWSLDPDLNNILASSRSYAMLLFAWEGWHNAVGIPLKPLYQEFTALSNEAYRQDGFSDTGAYWRSWYDSPTFEEDLERIYHQLEPLYLNLHAYVRRVLHRRYGDRYINLRGPIPAHLLGNMWAQSWESIYDMVVPFPDKPNLDVTSTMVQKGWNATHMFRVAEEFFTSLGLLPMPPEFWAESMLEKPEDGREVVCHASAWDFYNRKDFRIKQCTQVTMDQLSTVHHEMGHVQYYLQYKDQPVSLRRANPGFHEAIGDVLALSVSTPAHLHKIGLLDHVTNDTESDINYLLKMALEKIAFLPFGYLVDQWRWGVFSGRTPSSRYNFDWWYLRTKYQGICPPVVRNETHFDAGAKFHIPSVTPYIRYFVSFVLQFQFHQALCMEAGHQGPLHQCDIYQSTRAGAKLRAVLQAGCSRPWQEVLKDMVASDALDAQPLLDYFQPVTQWLQEQNERNGEVLGWPEYQWRPPLPNNYPEGIDLVTDEAEASRFVEEYDRSFQAVWNEYAEANWNYNTNITTEASKILLQKNMQIANHTLTYGNWARRFDVSNFQNATSKRIIKKVQDLQRAVLPVKELEEYNQILLDMETIYSVANVCRVDGSCLQLEPDLTNLMATSRKYDELLWVWTSWRDKVGRAILPYFPKYVEFTNKAARLNGYVDAGDSWRSMYETPTLEQDLERLFQELQPLYLNLHAYVGRALHRHYGAQHINLEGPIPAHLLGNMWAQTWSNIYDLVAPFPSASTMDATEAMIKQGWTPRRMFEEADKFFISLGLLPVPPEFWNKSMLEKPTDGREVVCHASAWDFYNGKDFRIKQCTTVNMEDLVVVHHEMGHIQYFMQYKDLPVALREGANPGFHEAIGDVLALSVSTPKHLHSINLLSSEGGGYEHDINFLMKMALDKIAFIPFSYLVDEWRWRVFDGSITKENYNQEWWSLRLKYQGLCPPAPRSQGDFDPGAKFHIPSSVPYIRYFVSFIIQFQFHEALCKAAGHTGPLHTCDIYQSKEAGKRLADAMKLGYSKPWPEAMKVITGQPNMSASAMMNYFKPLMDWLLTENGRHGEKLGWPQYTWTPNSARSEGSLPDSGRVNFLGMNLDAQQAR | ||||||
Transmembrane | 1261-1281 | Helical | ||||
Sequence: VGQWVLLFLGVALLLASLGLT | ||||||
Topological domain | 1282-1310 | Cytoplasmic | ||||
Sequence: QRLFSIRYQSLRQPHHGPQFGSEVELRHS |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 727 | No effect on activity. 20-fold reduction in catalytic efficiency; when associated with F-809. | ||||
Sequence: K → E | ||||||
Mutagenesis | 809 | No effect on activity. 20-fold reduction in catalytic efficiency; when associated with E-727. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 1303 | Abolished phosphorylation without affecting calmodulin-binding. | ||||
Sequence: S → A | ||||||
Mutagenesis | 1303 | Mimics phosphorylation; does not affect calmodulin-binding. | ||||
Sequence: S → D |
Chemistry
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-33 | |||||
Sequence: MGAAPGRRGPRLLRPPPPLLLLLLLLRPPPAAL | ||||||
Chain | PRO_0000028552 | 34-1236 | Angiotensin-converting enzyme, soluble form | |||
Sequence: TLDPGLLPGDFAADEAGARLFASSYNSSAEQVLFRSTAASWAHDTNITAENARRQEEEALLSQEFAEAWGKKAKELYDPVWQNFTDPELRRIIGAVRTLGPANLPLAKRQQYNSLLSNMSQIYSTGKVCFPNKTASCWSLDPDLNNILASSRSYAMLLFAWEGWHNAVGIPLKPLYQEFTALSNEAYRQDGFSDTGAYWRSWYDSPTFEEDLERIYHQLEPLYLNLHAYVRRVLHRRYGDRYINLRGPIPAHLLGNMWAQSWESIYDMVVPFPDKPNLDVTSTMVQKGWNATHMFRVAEEFFTSLGLLPMPPEFWAESMLEKPEDGREVVCHASAWDFYNRKDFRIKQCTQVTMDQLSTVHHEMGHVQYYLQYKDQPVSLRRANPGFHEAIGDVLALSVSTPAHLHKIGLLDHVTNDTESDINYLLKMALEKIAFLPFGYLVDQWRWGVFSGRTPSSRYNFDWWYLRTKYQGICPPVVRNETHFDAGAKFHIPSVTPYIRYFVSFVLQFQFHQALCMEAGHQGPLHQCDIYQSTRAGAKLRAVLQAGCSRPWQEVLKDMVASDALDAQPLLDYFQPVTQWLQEQNERNGEVLGWPEYQWRPPLPNNYPEGIDLVTDEAEASRFVEEYDRSFQAVWNEYAEANWNYNTNITTEASKILLQKNMQIANHTLTYGNWARRFDVSNFQNATSKRIIKKVQDLQRAVLPVKELEEYNQILLDMETIYSVANVCRVDGSCLQLEPDLTNLMATSRKYDELLWVWTSWRDKVGRAILPYFPKYVEFTNKAARLNGYVDAGDSWRSMYETPTLEQDLERLFQELQPLYLNLHAYVGRALHRHYGAQHINLEGPIPAHLLGNMWAQTWSNIYDLVAPFPSASTMDATEAMIKQGWTPRRMFEEADKFFISLGLLPVPPEFWNKSMLEKPTDGREVVCHASAWDFYNGKDFRIKQCTTVNMEDLVVVHHEMGHIQYFMQYKDLPVALREGANPGFHEAIGDVLALSVSTPKHLHSINLLSSEGGGYEHDINFLMKMALDKIAFIPFSYLVDEWRWRVFDGSITKENYNQEWWSLRLKYQGLCPPAPRSQGDFDPGAKFHIPSSVPYIRYFVSFIIQFQFHEALCKAAGHTGPLHTCDIYQSKEAGKRLADAMKLGYSKPWPEAMKVITGQPNMSASAMMNYFKPLMDWLLTENGRHGEKLGWPQYTWTPNSAR | ||||||
Chain | PRO_0000028551 | 34-1310 | Angiotensin-converting enzyme | |||
Sequence: TLDPGLLPGDFAADEAGARLFASSYNSSAEQVLFRSTAASWAHDTNITAENARRQEEEALLSQEFAEAWGKKAKELYDPVWQNFTDPELRRIIGAVRTLGPANLPLAKRQQYNSLLSNMSQIYSTGKVCFPNKTASCWSLDPDLNNILASSRSYAMLLFAWEGWHNAVGIPLKPLYQEFTALSNEAYRQDGFSDTGAYWRSWYDSPTFEEDLERIYHQLEPLYLNLHAYVRRVLHRRYGDRYINLRGPIPAHLLGNMWAQSWESIYDMVVPFPDKPNLDVTSTMVQKGWNATHMFRVAEEFFTSLGLLPMPPEFWAESMLEKPEDGREVVCHASAWDFYNRKDFRIKQCTQVTMDQLSTVHHEMGHVQYYLQYKDQPVSLRRANPGFHEAIGDVLALSVSTPAHLHKIGLLDHVTNDTESDINYLLKMALEKIAFLPFGYLVDQWRWGVFSGRTPSSRYNFDWWYLRTKYQGICPPVVRNETHFDAGAKFHIPSVTPYIRYFVSFVLQFQFHQALCMEAGHQGPLHQCDIYQSTRAGAKLRAVLQAGCSRPWQEVLKDMVASDALDAQPLLDYFQPVTQWLQEQNERNGEVLGWPEYQWRPPLPNNYPEGIDLVTDEAEASRFVEEYDRSFQAVWNEYAEANWNYNTNITTEASKILLQKNMQIANHTLTYGNWARRFDVSNFQNATSKRIIKKVQDLQRAVLPVKELEEYNQILLDMETIYSVANVCRVDGSCLQLEPDLTNLMATSRKYDELLWVWTSWRDKVGRAILPYFPKYVEFTNKAARLNGYVDAGDSWRSMYETPTLEQDLERLFQELQPLYLNLHAYVGRALHRHYGAQHINLEGPIPAHLLGNMWAQTWSNIYDLVAPFPSASTMDATEAMIKQGWTPRRMFEEADKFFISLGLLPVPPEFWNKSMLEKPTDGREVVCHASAWDFYNGKDFRIKQCTTVNMEDLVVVHHEMGHIQYFMQYKDLPVALREGANPGFHEAIGDVLALSVSTPKHLHSINLLSSEGGGYEHDINFLMKMALDKIAFIPFSYLVDEWRWRVFDGSITKENYNQEWWSLRLKYQGLCPPAPRSQGDFDPGAKFHIPSSVPYIRYFVSFIIQFQFHEALCKAAGHTGPLHTCDIYQSKEAGKRLADAMKLGYSKPWPEAMKVITGQPNMSASAMMNYFKPLMDWLLTENGRHGEKLGWPQYTWTPNSARSEGSLPDSGRVNFLGMNLDAQQARVGQWVLLFLGVALLLASLGLTQRLFSIRYQSLRQPHHGPQFGSEVELRHS | ||||||
Glycosylation | 59 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 79 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 151 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 162↔170 | |||||
Sequence: CFPNKTASC | ||||||
Glycosylation | 323 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 364↔382 | |||||
Sequence: CHASAWDFYNRKDFRIKQC | ||||||
Glycosylation | 449 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 513 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 549↔561 | |||||
Sequence: CMEAGHQGPLHQC | ||||||
Glycosylation | 681 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 699 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 718 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 761↔767 | |||||
Sequence: CRVDGSC | ||||||
Glycosylation | 946 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 961↔979 | |||||
Sequence: CHASAWDFYNGKDFRIKQC | ||||||
Disulfide bond | 1147↔1159 | |||||
Sequence: CKAAGHTGPLHTC | ||||||
Glycosylation | 1195 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 1303 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
N-glycosylated.
Phosphorylated by CK2 on Ser-1303; which allows membrane retention (By similarity).
Phosphorylated on tyrosine residues on its extracellular part, promoting cleavage by secretase enzymes and formation of the soluble form (Angiotensin-converting enzyme, soluble form) (PubMed:15252021).
Phosphorylated on tyrosine residues on its extracellular part, promoting cleavage by secretase enzymes and formation of the soluble form (Angiotensin-converting enzyme, soluble form) (PubMed:15252021).
Angiotensin-converting enzyme, soluble form
Produced following proteolytic cleavage by secretase enzymes that cleave the transmembrane form in the juxtamembrane stalk region upstream of the transmembrane region (PubMed:15252021, PubMed:16096279).
Cleavage can take place at different sites of the juxtamembrane stalk region (By similarity).
Cleavage can take place at different sites of the juxtamembrane stalk region (By similarity).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Isoform Testis-specific
Testis-specific isoform is expressed in spermatocytes, adult testis.
Interaction
Subunit
Monomer and homodimer; homodimerizes following binding to an inhibitor (By similarity).
Interacts with calmodulin (CALM1, CALM2 or CALM3); interaction takes place in the cytoplasmic region and regulates phosphorylation and proteolytic cleavage (PubMed:16096279).
Interacts with calmodulin (CALM1, CALM2 or CALM3); interaction takes place in the cytoplasmic region and regulates phosphorylation and proteolytic cleavage (PubMed:16096279).
Protein-protein interaction databases
Chemistry
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 45-628 | Peptidase M2 1 | ||||
Sequence: AADEAGARLFASSYNSSAEQVLFRSTAASWAHDTNITAENARRQEEEALLSQEFAEAWGKKAKELYDPVWQNFTDPELRRIIGAVRTLGPANLPLAKRQQYNSLLSNMSQIYSTGKVCFPNKTASCWSLDPDLNNILASSRSYAMLLFAWEGWHNAVGIPLKPLYQEFTALSNEAYRQDGFSDTGAYWRSWYDSPTFEEDLERIYHQLEPLYLNLHAYVRRVLHRRYGDRYINLRGPIPAHLLGNMWAQSWESIYDMVVPFPDKPNLDVTSTMVQKGWNATHMFRVAEEFFTSLGLLPMPPEFWAESMLEKPEDGREVVCHASAWDFYNRKDFRIKQCTQVTMDQLSTVHHEMGHVQYYLQYKDQPVSLRRANPGFHEAIGDVLALSVSTPAHLHKIGLLDHVTNDTESDINYLLKMALEKIAFLPFGYLVDQWRWGVFSGRTPSSRYNFDWWYLRTKYQGICPPVVRNETHFDAGAKFHIPSVTPYIRYFVSFVLQFQFHQALCMEAGHQGPLHQCDIYQSTRAGAKLRAVLQAGCSRPWQEVLKDMVASDALDAQPLLDYFQPVTQWLQEQNERNGEVLGWP | ||||||
Domain | 647-1226 | Peptidase M2 2 | ||||
Sequence: VTDEAEASRFVEEYDRSFQAVWNEYAEANWNYNTNITTEASKILLQKNMQIANHTLTYGNWARRFDVSNFQNATSKRIIKKVQDLQRAVLPVKELEEYNQILLDMETIYSVANVCRVDGSCLQLEPDLTNLMATSRKYDELLWVWTSWRDKVGRAILPYFPKYVEFTNKAARLNGYVDAGDSWRSMYETPTLEQDLERLFQELQPLYLNLHAYVGRALHRHYGAQHINLEGPIPAHLLGNMWAQTWSNIYDLVAPFPSASTMDATEAMIKQGWTPRRMFEEADKFFISLGLLPVPPEFWNKSMLEKPTDGREVVCHASAWDFYNGKDFRIKQCTTVNMEDLVVVHHEMGHIQYFMQYKDLPVALREGANPGFHEAIGDVLALSVSTPKHLHSINLLSSEGGGYEHDINFLMKMALDKIAFIPFSYLVDEWRWRVFDGSITKENYNQEWWSLRLKYQGLCPPAPRSQGDFDPGAKFHIPSSVPYIRYFVSFIIQFQFHEALCKAAGHTGPLHTCDIYQSKEAGKRLADAMKLGYSKPWPEAMKVITGQPNMSASAMMNYFKPLMDWLLTENGRHGEKLGWP | ||||||
Region | 1219-1260 | Juxtamembrane stalk | ||||
Sequence: HGEKLGWPQYTWTPNSARSEGSLPDSGRVNFLGMNLDAQQAR |
Sequence similarities
Belongs to the peptidase M2 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative promoter usage.
P12822-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- NameSomatic
- Length1,310
- Mass (Da)150,406
- Last updated1997-11-01 v3
- Checksum04777FAB17981DEA
P12822-2
- NameTestis-specific
- SynonymsACE-T
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_037644 | 1-573 | in isoform Testis-specific | |||
Sequence: Missing | ||||||
Sequence conflict | 48 | in Ref. 6; AA sequence | ||||
Sequence: E → N | ||||||
Alternative sequence | VSP_037645 | 574-645 | in isoform Testis-specific | |||
Sequence: RAVLQAGCSRPWQEVLKDMVASDALDAQPLLDYFQPVTQWLQEQNERNGEVLGWPEYQWRPPLPNNYPEGID → MGQGWAAPGLPSLLLLLLCCGHSLLVPSRVAARRVTVNQGTTSQATTTSKATTSIRATTHQTTAHQTTQSPN |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X62551 EMBL· GenBank· DDBJ | CAA44428.1 EMBL· GenBank· DDBJ | mRNA | ||
J05041 EMBL· GenBank· DDBJ | AAA31153.1 EMBL· GenBank· DDBJ | mRNA | ||
M58579 EMBL· GenBank· DDBJ | AAA31151.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
M58580 EMBL· GenBank· DDBJ | AAA31152.1 EMBL· GenBank· DDBJ | Genomic DNA |