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Database: UniProt/TrEMBL
Entry: G1KNF0_ANOCA
LinkDB: G1KNF0_ANOCA
Original site: G1KNF0_ANOCA 
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
//
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