Protein: Angiotensin-converting enzyme (ACE) (EC 3.4.15.1) (Dipeptidyl carboxypeptidase I) (Kininase II) (Q10751)
Organism: Gallus gallus (Chicken)
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 (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 (By similarity). 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). Also acts as a regulator of hematopoietic stem cell differentiation by mediating degradation of hemoregulatory peptide N-acetyl-SDKP (AcSDKP) (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P12821}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:P09470}. Note=Detected in both cell membrane and cytoplasm in neurons. {ECO:0000250|UniProtKB:P09470}.
Interaction partners:
- Angiotensinogen
- Renin
- Type-1 angiotensin II receptor
- Collectrin, amino acid transport regulator
- Aminopeptidase Ey
- chymotrypsin
- Angiotensin II receptor type 2
- Transmembrane protease serine 2
- Collagen alpha-1
- Albumin
Sequence:
MPAALGLLLPWLSLVGALQPGLEPPQSDPTEAGAVFFASEYNSTAEIVLFRSVSASWEYNTNLTTANAALQVEASLEEQNFTELWGKKAKELYGNIWSNFSDPQLKKIIGSIQTLGPSNLPLDKRQQYNTILSDMDKIYSTAKVCLDNGTCWDLEPDISDIMATSRSYKKLLYAWEGWHNAAGNPLRAKYQEFVTLSNEAYQMDGFEDTGSYWRSWYDSTTFEDDLEHLYNQLEPLYLNLHAFVRRKLYDRYGPKYINLKGPIPAHLLGNMWAQQWNNIYDLMVPYPDKPNLDVTNTMVNQGWNATHMFRVSEEFFTSLGLLEMPPEFWEKSMLEKPADGREVVCHASAWDFYNRKDFRIKQCTTVTMEQLFTVHHEMGHVQYYLQYKDQPVSFRGGANPGFHEAIGDVLSLSVSTPSHLQKIGLLSSAVEDEESNINYLLKMALEKIAFLPFGYLIDQWRWNVFSGRTPPSRYNYDWWYLRTKYQGICAPVSRNESNFDPGAKYHIPGNTPYIRYFVSFILQFQFHKALCQAANHTGPLHTCDIYMSKEAGAKLREVLKAGSSKSWQEILFNLTGTDKMDAGALLEYFSPVTTWLQEQNNKTNEVLGWPEFDWRPPIPEGYPEGIDKIVDEAQAKEFLSEYNSTAEVVWNAYTEASWEYNTNITDHNKEVMLEKNLAMSKHTIEYGMRARQFDPSDFQDETVTRILNKLSVLERAALPEDELKEYNTLLSDMETTYSVAKVCRENNTCHPLDPDLTDILATSRDYNELLFAWKGWRDASGAKIKDKYKRYVELSNKAAVLNGYTDNGAYWRSLYETPTFEEDLERLYLQLQPLYLNLHAYVRRALYNKYGAEHISLKGPIPAHLLGNMWAQSWSNIFDLVMPFPDATKVDATPAMKQQGWTPKMMFEESDRFFTSLGLIPMPQEFWDKSMIEKPADGREVVCHASAWDFYNRKDFRIKQCTVVNMDDLITVHHEMGHVQYFLQYMDQPISFRDGANPGFHEAIGDVMALSVSTPKHLHSINLLDQVTENEESDINYLMSIALDKIAFLPFGYLMDQWRWKVFDGRIKEDEYNQQWWNLRLKYQGLCPPVPRSEDDFDPGAKFHIPANVPYIRYFVSFVIQFQFHQALCKAAGHTGPLHTCDIYQSKEAGKLLGDAMKLGFSKPWPEAMQLITGQPNMSAEALMSYFEPLMTWLVKKNTENGEVLGWPEYSWTPYAVTEFHAATDTADFLGMSVGTKQATAGAWVLLALALVFLITSIFLGVKLFSSRRKAFKSSSEMELK