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Database: UniProt
Entry: E4YK34_OIKDI
LinkDB: E4YK34_OIKDI
Original site: E4YK34_OIKDI 
ID   E4YK34_OIKDI            Unreviewed;       225 AA.
AC   E4YK34;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Angiotensin-converting enzyme {ECO:0000256|ARBA:ARBA00039858, ECO:0000256|RuleBase:RU361144};
DE            EC=3.4.-.- {ECO:0000256|RuleBase:RU361144};
GN   ORFNames=GSOID_T00028315001 {ECO:0000313|EMBL:CBY35845.1};
OS   Oikopleura dioica (Tunicate).
OC   Eukaryota; Metazoa; Chordata; Tunicata; Appendicularia; Copelata;
OC   Oikopleuridae; Oikopleura.
OX   NCBI_TaxID=34765 {ECO:0000313|EMBL:CBY35845.1};
RN   [1] {ECO:0000313|EMBL:CBY35845.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21097902; DOI=10.1126/science.1194167;
RA   Denoeud F., Henriet S., Mungpakdee S., Aury J.M., Da Silva C.,
RA   Brinkmann H., Mikhaleva J., Olsen L.C., Jubin C., Canestro C.,
RA   Bouquet J.M., Danks G., Poulain J., Campsteijn C., Adamski M., Cross I.,
RA   Yadetie F., Muffato M., Louis A., Butcher S., Tsagkogeorga G., Konrad A.,
RA   Singh S., Jensen M.F., Cong E.H., Eikeseth-Otteraa H., Noel B.,
RA   Anthouard V., Porcel B.M., Kachouri-Lafond R., Nishino A., Ugolini M.,
RA   Chourrout P., Nishida H., Aasland R., Huzurbazar S., Westhof E., Delsuc F.,
RA   Lehrach H., Reinhardt R., Weissenbach J., Roy S.W., Artiguenave F.,
RA   Postlethwait J.H., Manak J.R., Thompson E.M., Jaillon O., Du Pasquier L.,
RA   Boudinot P., Liberles D.A., Volff J.N., Philippe H., Lenhard B.,
RA   Roest Crollius H., Wincker P., Chourrout D.;
RT   "Plasticity of animal genome architecture unmasked by rapid evolution of a
RT   pelagic tunicate.";
RL   Science 330:1381-1385(2010).
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 1 zinc ion 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; FN654685; CBY35845.1; -; Genomic_DNA.
DR   AlphaFoldDB; E4YK34; -.
DR   Proteomes; UP000011014; Unassembled WGS sequence.
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   InterPro; IPR001548; Peptidase_M2.
DR   PANTHER; PTHR10514; ANGIOTENSIN-CONVERTING ENZYME; 1.
DR   PANTHER; PTHR10514:SF27; ANGIOTENSIN-CONVERTING ENZYME; 1.
DR   Pfam; PF01401; Peptidase_M2; 1.
DR   PRINTS; PR00791; PEPDIPTASEA.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
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   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|RuleBase:RU361144}.
FT   TRANSMEM        201..224
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   225 AA;  25922 MW;  69A57C5BE373C2C3 CRC64;
     MYASLHDKHA QLFNMTTTTE INFLMYMALK ELPFLAFAKS LEEWRWKVFS GMYPESQFQK
     MWEDIVFENM GLLQPLERDV SDMDPLSKIH ILLNLDYAKY FLSTPSLYEI LASLCPPDTN
     GKCDLRKDAK RPGTILLSAM SKGNTMPWEN VYQTLTGSTS ISGQALRNYF KPLEDYLDKT
     IELHRLKVGW KRTKPARKKD ILPCSAGSTS FNLQVFALLL LTLML
//
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