ID B0JZU8_XENTR Unreviewed; 1284 AA.
AC B0JZU8;
DT 18-MAR-2008, integrated into UniProtKB/TrEMBL.
DT 18-MAR-2008, sequence version 1.
DT 24-JAN-2024, entry version 82.
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|EMBL:AAI59327.1,
GN ECO:0000313|RefSeq:NP_001116882.1,
GN ECO:0000313|Xenbase:XB-GENE-479789};
GN Synonyms=ace1 {ECO:0000313|RefSeq:NP_001116882.1}, cd143
GN {ECO:0000313|RefSeq:NP_001116882.1}, dcp
GN {ECO:0000313|RefSeq:NP_001116882.1}, dcp1
GN {ECO:0000313|RefSeq:NP_001116882.1}, xace
GN {ECO:0000313|RefSeq:NP_001116882.1};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364 {ECO:0000313|EMBL:AAI59327.1};
RN [1] {ECO:0000313|RefSeq:NP_001116882.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12454917; DOI=10.1002/dvdy.10174;
RA Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA Richardson P.;
RT "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT initiative.";
RL Dev. Dyn. 225:384-391(2002).
RN [2] {ECO:0000313|EMBL:AAI59327.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=TGA IC {ECO:0000313|EMBL:AAI59327.1};
RC TISSUE=Testes {ECO:0000313|EMBL:AAI59327.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|RefSeq:NP_001116882.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (SEP-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 EMBL; BC159326; AAI59327.1; -; mRNA.
DR RefSeq; NP_001116882.1; NM_001123410.1.
DR MEROPS; M02.001; -.
DR GeneID; 100144634; -.
DR KEGG; xtr:100144634; -.
DR CTD; 1636; -.
DR Xenbase; XB-GENE-479789; ace.
DR OMA; DYSDFQD; -.
DR OrthoDB; 2898149at2759; -.
DR Proteomes; UP000008143; Chromosome 10.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; IEA:UniProtKB-KW.
DR GO; GO:0008241; F:peptidyl-dipeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06461; M2_ACE; 2.
DR Gene3D; 1.10.1370.30; -; 3.
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 2: Evidence at transcript level;
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:UP000008143};
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..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..1284
FT /note="Angiotensin-converting enzyme"
FT /evidence="ECO:0000256|SAM:SignalP,
FT ECO:0000313|RefSeq:NP_001116882.1"
FT /id="PRO_5033207444"
FT TRANSMEM 1247..1267
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 1284 AA; 148040 MW; 81BE5E5F44FDF291 CRC64;
MRVLLLGLLL LVGTNSALDS SFLPGTYPKD EAGARDFADA YNSTAEVILF KSVEASWAYN
TNLTDYNSKQ QILASMEEQE FNEAWGMKAK ELFNDVWENF TDPLLKKIIS SIRTLGASNL
NLTAREEYNT ILSEMDSIYS TAKVCPPNAT AKCWSLEPEI TEIMATSRSY KKLLYAWEGW
HNSAGIPLKE KYLRFVQLSN EAYRMDGYKD TGAYWRSWYA SPTFEEDLDG LYQQLEPLYL
NLHAFVRRKL YERYGAKYIN LKGPIPAHLF GNMWSQQWNN IYDMMIPFPD KTNIDVTNTM
REKGWNATHM FRVSEEFFTS LGLLEMPPEF WEKSMLEKPA DGREVVCHAS AWDFYNRKDF
RIKQCTTVTM EQLFTVHHEM GHVEYYLQYK DQPVTYRRGA NPGFHEAIGD VLSLSVSTPG
HLKTIGLLET VTNDKESDIN YLLKMALEKI AFLPFGFLID QWRWNVFSGR TPPTRYNYDW
WNLRTKYQGI CPPISRDDNQ FDAGAKYHIP GNTPYIRYFV SFVLQFQFHK ALCTAAKHTG
PLHTCDIYRS QEAGKILGDV LRSGSSKSWQ EVLKDMTGSE KMDVGPLLEY FTPVTQWLIE
QNTKNNEILG WPDFSWTPPM PDGYPGDIEK IANEKEADTF LSDYTKSAEV VWNDYTEASW
AYNTNITEAN KQVMLDKNLA MSGHTLQYGL QARNYDYSDF QDPETQRILR KLSEIDKAAL
SEEEQKEYNQ ITSDMETIYS VAKVCKDGNT NCHPLDPDLT EILAKSRDYD ELLFAWKGWR
DASGKQIREK YKRYVQLANK AAQLNGYNDN GAYWRSWYET PTLESDVEKL YDELQPLYLN
LHAYVRRALY KKYGDKRINL KGPIPAHLLG NMWAQSWSNI YELLVPYPNA AQVDATPAMI
AKNWTPKRMF EESDNFFKSL GLLPMPQEFW DKSMIEKPKD REVVCHASAW DFYNRKDFRI
KQCTVVNMDD LITVHHEMGH VQYFLQYKDQ PILFREGANP GFHEAIGDVL ALSVSTPKHL
QSIGLLDKVE DNPESDINYL MSIALDKIAF LPFGFLMDQW RWKVFDGRTP DSEYNQQWWN
LRLKYQGLVP PVLRTENDFD PGAKFHIPAS VPYIRYFISF VIQFQFHEAL CKAANQEGPL
HKCDIYQSTQ AGKLLGDAMK LGNSKPWPEA MQTITGQRNM SAHALLKYFQ PLTDWLIKEN
TKNGETLGWP EYNWSPVQSV PLPPSGDSNS DFLGLAVSNS QAAAGQWILL ALGIVLIITT
IVFGVLYSKM KSRAKMSSSQ MELK
//