ID G1KNF0_ANOCA Unreviewed; 1305 AA.
AC G1KNF0;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 2.
DT 24-JAN-2024, entry version 68.
DE RecName: Full=Angiotensin-converting enzyme {ECO:0000256|ARBA:ARBA00039858, ECO:0000256|RuleBase:RU361144};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361144};
GN Name=ace {ECO:0000313|Ensembl:ENSACAP00000012980.3};
OS Anolis carolinensis (Green anole) (American chameleon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Dactyloidae; Anolis.
OX NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000012980.3, ECO:0000313|Proteomes:UP000001646};
RN [1] {ECO:0000313|Ensembl:ENSACAP00000012980.3, ECO:0000313|Proteomes:UP000001646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000012980.3,
RC ECO:0000313|Proteomes:UP000001646};
RG The Genome Sequencing Platform;
RA Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACAP00000012980.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + Leu-enkephalin = L-phenylalanyl-L-leucine + L-
CC tyrosylglycylglycine; Xref=Rhea:RHEA:71487, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:190689, ChEBI:CHEBI:190708, ChEBI:CHEBI:190710;
CC Evidence={ECO:0000256|ARBA:ARBA00037024};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71488;
CC Evidence={ECO:0000256|ARBA:ARBA00037024};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + Met-enkephalin = L-phenylalanyl-L-methionine + L-
CC tyrosylglycylglycine; Xref=Rhea:RHEA:71483, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:189868, ChEBI:CHEBI:190708, ChEBI:CHEBI:190709;
CC Evidence={ECO:0000256|ARBA:ARBA00036262};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71484;
CC Evidence={ECO:0000256|ARBA:ARBA00036262};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + Met-enkephalin-Arg-Phe = L-arginyl-L-phenylalanine +
CC Met-enkephalin; Xref=Rhea:RHEA:70675, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:189868, ChEBI:CHEBI:189869, ChEBI:CHEBI:189870;
CC Evidence={ECO:0000256|ARBA:ARBA00036091};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70676;
CC Evidence={ECO:0000256|ARBA:ARBA00036091};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + neurotensin = L-isoleucyl-L-leucine + neurotensin(1-11);
CC Xref=Rhea:RHEA:71475, ChEBI:CHEBI:15377, ChEBI:CHEBI:147362,
CC ChEBI:CHEBI:190704, ChEBI:CHEBI:190706;
CC Evidence={ECO:0000256|ARBA:ARBA00034019};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71476;
CC Evidence={ECO:0000256|ARBA:ARBA00034019};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + substance P = Gly-L-Leu-L-Met-NH2 + substance P(1-8);
CC Xref=Rhea:RHEA:71463, ChEBI:CHEBI:15377, ChEBI:CHEBI:190692,
CC ChEBI:CHEBI:190694, ChEBI:CHEBI:190699;
CC Evidence={ECO:0000256|ARBA:ARBA00035850};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71464;
CC Evidence={ECO:0000256|ARBA:ARBA00035850};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + substance P = L-Leu-L-Met-NH2 + substance P(1-9);
CC Xref=Rhea:RHEA:71459, ChEBI:CHEBI:15377, ChEBI:CHEBI:190692,
CC ChEBI:CHEBI:190693, ChEBI:CHEBI:190700;
CC Evidence={ECO:0000256|ARBA:ARBA00034071};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71460;
CC Evidence={ECO:0000256|ARBA:ARBA00034071};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + substance P = L-Phe-L-Phe-Gly-L-Leu-L-Met-NH2 +
CC substance P(1-6); Xref=Rhea:RHEA:71471, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:190692, ChEBI:CHEBI:190696, ChEBI:CHEBI:190697;
CC Evidence={ECO:0000256|ARBA:ARBA00036862};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71472;
CC Evidence={ECO:0000256|ARBA:ARBA00036862};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of a C-terminal dipeptide, oligopeptide-|-Xaa-Yaa,
CC when Xaa is not Pro, and Yaa is neither Asp nor Glu. Thus, conversion
CC of angiotensin I to angiotensin II, with increase in vasoconstrictor
CC activity, but no action on angiotensin II.; EC=3.4.15.1;
CC Evidence={ECO:0000256|ARBA:ARBA00036868};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=angiotensin I + H2O = angiotensin II + L-histidyl-L-leucine;
CC Xref=Rhea:RHEA:63560, ChEBI:CHEBI:15377, ChEBI:CHEBI:58506,
CC ChEBI:CHEBI:147350, ChEBI:CHEBI:147392; EC=3.4.15.1;
CC Evidence={ECO:0000256|ARBA:ARBA00036030};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63561;
CC Evidence={ECO:0000256|ARBA:ARBA00036030};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=bradykinin + H2O = bradykinin(1-7) + L-Phe-L-Arg;
CC Xref=Rhea:RHEA:71451, ChEBI:CHEBI:15377, ChEBI:CHEBI:132988,
CC ChEBI:CHEBI:133147, ChEBI:CHEBI:147352;
CC Evidence={ECO:0000256|ARBA:ARBA00035977};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71452;
CC Evidence={ECO:0000256|ARBA:ARBA00035977};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=goralatide + H2O = L-lysyl-L-proline + N-acetyl-L-seryl-L-
CC aspartate; Xref=Rhea:RHEA:71455, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:190701, ChEBI:CHEBI:190702, ChEBI:CHEBI:190703;
CC Evidence={ECO:0000256|ARBA:ARBA00036673};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71456;
CC Evidence={ECO:0000256|ARBA:ARBA00036673};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU361144};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|RuleBase:RU361144};
CC -!- COFACTOR:
CC Name=chloride; Xref=ChEBI:CHEBI:17996;
CC Evidence={ECO:0000256|ARBA:ARBA00001923};
CC -!- SIMILARITY: Belongs to the peptidase M2 family.
CC {ECO:0000256|ARBA:ARBA00008139, ECO:0000256|RuleBase:RU361144}.
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DR RefSeq; XP_008111340.1; XM_008113133.1.
DR STRING; 28377.ENSACAP00000012980; -.
DR MEROPS; M02.004; -.
DR Ensembl; ENSACAT00000013239.4; ENSACAP00000012980.3; ENSACAG00000013067.4.
DR GeneID; 100558092; -.
DR KEGG; acs:100558092; -.
DR CTD; 1636; -.
DR eggNOG; KOG3690; Eukaryota.
DR GeneTree; ENSGT00940000163600; -.
DR HOGENOM; CLU_006219_0_0_1; -.
DR InParanoid; G1KNF0; -.
DR OrthoDB; 2898149at2759; -.
DR TreeFam; TF312861; -.
DR Proteomes; UP000001646; Chromosome 6.
DR Bgee; ENSACAG00000013067; Expressed in lung and 12 other cell types or tissues.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IBA:GO_Central.
DR GO; GO:0008241; F:peptidyl-dipeptidase activity; IBA:GO_Central.
DR GO; GO:0003084; P:positive regulation of systemic arterial blood pressure; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0003081; P:regulation of systemic arterial blood pressure by renin-angiotensin; IBA:GO_Central.
DR CDD; cd06461; M2_ACE; 2.
DR Gene3D; 1.10.1370.30; -; 1.
DR InterPro; IPR001548; Peptidase_M2.
DR PANTHER; PTHR10514; ANGIOTENSIN-CONVERTING ENZYME; 1.
DR PANTHER; PTHR10514:SF27; ANGIOTENSIN-CONVERTING ENZYME; 1.
DR Pfam; PF01401; Peptidase_M2; 2.
DR PRINTS; PR00791; PEPDIPTASEA.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 2.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|RuleBase:RU361144};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180,
KW ECO:0000256|RuleBase:RU361144}; Hydrolase {ECO:0000256|RuleBase:RU361144};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|RuleBase:RU361144};
KW Metalloprotease {ECO:0000256|RuleBase:RU361144};
KW Protease {ECO:0000256|RuleBase:RU361144};
KW Reference proteome {ECO:0000313|Proteomes:UP000001646};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|RuleBase:RU361144}.
FT SIGNAL 1..40
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 41..1305
FT /note="Angiotensin-converting enzyme"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003413833"
FT TRANSMEM 1268..1288
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 1305 AA; 150413 MW; DCB8550F6DFEACDF CRC64;
MRSAPLYKPA PSLRPPFRTA KMPQLLALAL LLLCCGAALA LDASLLPPGS PAATEEGARL
FAQEYNATAE TVFFDNTLAS WVYNTNLTDF NAQLQVAASL MEQEFIEVWG KKTKEIYGNI
WQNFSDPELK KIISNIQTLG PSNLDLEKRQ RYNTIMSEMD NIYSTSKVCL PNQTSNCWAL
EPDITDIMAN SRSYSKLLYA WEGWHNSAGN PLRPKYEEFV SLSNEAYKMD GFKDTGAYWR
SSYDSPTFED DLEELYHQLE PLYLNLHAFV RRKLYDRYGS KYINLKGPIP AHLLGNMWAQ
QWNNIYDMMI PFPNKPNVDV TNTMQQQNWN VTRMFRVSEE FFTSLGMLGM PPEFWEKSML
EKPTDGREVV CHASAWDFYN RKDFRIKQCT TITMEQLFTV HHEMGHVEYY LQYKDQPVTF
REGANPGFHE AIGDVMSLSV STPAHLKKIG LLSEVTEDKE SDINYLLKMA LQKIAFIPFG
YLIDQWRWNV FSGRTTPSRY NYDWWYLRTK YQGICPPIAR NETNFDPGAK YHIPGNTPYI
RYFVSYIVQF QFHKALCQAA NHTGPLHTCD IYQSKEAGRL LSAALRPGSS QPWQDILQQI
TGTNKMDAAP LLEFFSPVIS WLEEQNKQTN ETLGWPDFEW RPPVPEGYPE GLDKITDEAE
AAKFLEEYNS TAEVVWNTYT EASWTYNVNI TEHNKNIMLE KNLELSNHTL HYGLRARTFD
PTDFKDPSIK RILKKLSDIE RAALSEQELK EYNQLLSDME TTYSVAKVCT GEKVCKSLDP
DLTKTMAQSR DYDELLEAWK GWRDVSGKKI RTPYKRYVQL SNKAARLNGH ADNGAFWRSL
YETPAFEEDL ERIWHQLQSL YFNLHAYVRR ALYKKYGADH INLKGPIPAH LLGNMWAQSW
ANIFDLVAPF PNAIKVDATP AMKSKGWTPK KMFEESDNFF KSLGLIPMPD EFWKSSMLEK
PKDGREVVCH ASAWDFYNRK DFRIKQCTVV NMDDLITTHH EMGHVQYFLQ YKDQPISFRD
GANPGFHEAI GDVMALSVST PKHLFSIKLL DQVEDNPESD INYLMSIALD KIAFLPFGYL
MDQWRWKVFD GRITEDEYNQ QWWNLRLKYQ GLCPPAPRSE DDFDPGAKFH IPANVPYVRY
FVSFVIQFQF HQALCKAAGH TGPLHKCDIY NSEAAGTILG NALKLGFSKP WPEVMQLITG
QPNMSADALL TYFQPLTDWL INQNLKNQET LGWPEYTWLP YAGQVQADNK VNFLGMLMTS
SEAAAGQWIL LVLGLLLLIA AIVLGAKWHQ ARRRATRSSM EMELK
//