ID A0A212EUB5_DANPL Unreviewed; 299 AA.
AC A0A212EUB5;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Angiotensin-converting enzyme {ECO:0000256|RuleBase:RU361144};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361144};
DE Flags: Fragment;
GN ORFNames=KGM_212896A {ECO:0000313|EMBL:OWR45090.1};
OS Danaus plexippus plexippus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Nymphalidae; Danainae; Danaini; Danaina; Danaus; Danaus.
OX NCBI_TaxID=278856 {ECO:0000313|EMBL:OWR45090.1, ECO:0000313|Proteomes:UP000007151};
RN [1] {ECO:0000313|EMBL:OWR45090.1, ECO:0000313|Proteomes:UP000007151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F-2 {ECO:0000313|EMBL:OWR45090.1};
RX PubMed=22118469; DOI=10.1016/j.cell.2011.09.052;
RA Zhan S., Merlin C., Boore J.L., Reppert S.M.;
RT "The monarch butterfly genome yields insights into long-distance
RT migration.";
RL Cell 147:1171-1185(2011).
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 -!- SIMILARITY: Belongs to the peptidase M2 family.
CC {ECO:0000256|ARBA:ARBA00008139, ECO:0000256|RuleBase:RU361144}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OWR45090.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AGBW02012415; OWR45090.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A212EUB5; -.
DR STRING; 278856.A0A212EUB5; -.
DR KEGG; dpl:KGM_212896A; -.
DR eggNOG; KOG3690; Eukaryota.
DR InParanoid; A0A212EUB5; -.
DR Proteomes; UP000007151; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
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:SF45; ANGIOTENSIN-CONVERTING ENZYME; 1.
DR Pfam; PF01401; Peptidase_M2; 2.
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 Metal-binding {ECO:0000256|RuleBase:RU361144};
KW Metalloprotease {ECO:0000256|RuleBase:RU361144};
KW Protease {ECO:0000256|RuleBase:RU361144};
KW Reference proteome {ECO:0000313|Proteomes:UP000007151};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Zinc {ECO:0000256|RuleBase:RU361144}.
FT NON_TER 299
FT /evidence="ECO:0000313|EMBL:OWR45090.1"
SQ SEQUENCE 299 AA; 35109 MW; 7338FBD2B94E65F3 CRC64;
MSQWKFVTNI TEYNRRRMLE ELALSSKFEK LSWRKAAAYD GSRLSDPQNR RQLSRIIQNS
RAALSDDKFS EIQQLITEMK ELYNSAKICP YGQKPYDPHI PKVLPTSTET PDSTKDHQTY
QLTNQPYQHY QPYQENTDYP NYCDMQLDPE ITRILAHSRI ENELLYVWKS FRDQTGPKLK
NRFMRYVQLA NEAAVKTGFK DAGDQMRAAY EDPSFRASVE EIYNQIIPLY KQLFTYVRRK
LLLRYGDKSV RPDGPIPAHL LGNMWAQNWK SIMDLVMPFP QAPNVDVTSE MLRQGFTPL
//
