ID A0A093R6P5_PHACA Unreviewed; 803 AA.
AC A0A093R6P5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Angiotensin-converting enzyme {ECO:0000256|RuleBase:RU361144};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361144};
GN ORFNames=N336_07656 {ECO:0000313|EMBL:KFW94280.1};
OS Phalacrocorax carbo (Great cormorant) (Pelecanus carbo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Suliformes; Phalacrocoracidae;
OC Phalacrocorax.
OX NCBI_TaxID=9209 {ECO:0000313|EMBL:KFW94280.1, ECO:0000313|Proteomes:UP000053238};
RN [1] {ECO:0000313|EMBL:KFW94280.1, ECO:0000313|Proteomes:UP000053238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N336 {ECO:0000313|EMBL:KFW94280.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=angiotensin I + H2O = angiotensin-(1-9) + L-leucine;
CC Xref=Rhea:RHEA:63532, ChEBI:CHEBI:15377, ChEBI:CHEBI:57427,
CC ChEBI:CHEBI:147350, ChEBI:CHEBI:147351;
CC Evidence={ECO:0000256|ARBA:ARBA00000796};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63533;
CC Evidence={ECO:0000256|ARBA:ARBA00000796};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=angiotensin II + H2O = angiotensin-(1-7) + L-phenylalanine;
CC Xref=Rhea:RHEA:26554, ChEBI:CHEBI:15377, ChEBI:CHEBI:58095,
CC ChEBI:CHEBI:58506, ChEBI:CHEBI:58922; EC=3.4.17.23;
CC Evidence={ECO:0000256|ARBA:ARBA00001502};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26555;
CC Evidence={ECO:0000256|ARBA:ARBA00001502};
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 -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000256|ARBA:ARBA00004221}. Cell membrane
CC {ECO:0000256|ARBA:ARBA00004236}. Cell projection, cilium
CC {ECO:0000256|ARBA:ARBA00004138}. Cytoplasm
CC {ECO:0000256|ARBA:ARBA00004496}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479}. Secreted
CC {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the peptidase M2 family.
CC {ECO:0000256|ARBA:ARBA00008139, ECO:0000256|RuleBase:RU361144}.
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DR EMBL; KL441318; KFW94280.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093R6P5; -.
DR MEROPS; M02.006; -.
DR Proteomes; UP000053238; Unassembled WGS sequence.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; 1.
DR Gene3D; 1.10.1370.30; -; 1.
DR InterPro; IPR031588; Collectrin_dom.
DR InterPro; IPR001548; Peptidase_M2.
DR PANTHER; PTHR10514; ANGIOTENSIN-CONVERTING ENZYME; 1.
DR PANTHER; PTHR10514:SF24; ANGIOTENSIN-CONVERTING ENZYME 2; 1.
DR Pfam; PF16959; Collectrin; 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|ARBA:ARBA00022645,
KW ECO:0000256|RuleBase:RU361144};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Chloride {ECO:0000256|ARBA:ARBA00023214};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180,
KW ECO:0000256|RuleBase:RU361144};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361144};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|RuleBase:RU361144};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU361144};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU361144};
KW Reference proteome {ECO:0000313|Proteomes:UP000053238};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|RuleBase:RU361144}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..803
FT /note="Angiotensin-converting enzyme"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001887569"
FT TRANSMEM 733..757
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 611..764
FT /note="Collectrin"
FT /evidence="ECO:0000259|Pfam:PF16959"
FT REGION 764..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..785
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 803 AA; 92474 MW; 18A78A3AE63BC3FE CRC64;
MLVHLCLLCG LSAVVTPQDV TQQAQTFLEE FNRRAENISY ESSLASWNYN TNITEETARK
MNEADAKWSA FYSEASRNSS RFPLSSIQDA LTRLQIQSLQ DRGSSVLSQD KYDRLNTVLN
TMSTIYSTGT VCKITEPSEC LVLEPGLDTI MANSTDYHER LWAWEGWRAD VGRMMRPLYE
EYVELKNEVA KLNGYSDYGD YWRANYEADY PENYKYSRDQ LVKDVEKTFE QIKPLYQQLH
AYVRHRLEQV YGPELISSTG CLPAHLLGDM WGRFWTNLYA LTVPYPAKPN IDVTSAMVEK
KWDAVKIFKA AEAFFFSIGL EKMTEGFWNN SMLTEPTDNR KVVCHPTAWD LGKKDYRIKM
CTKVTMDDFL TAHHEMGHIE YDMAYSEQPF LLRGGANEGF HEAVGEIMSL SAATPQHLKS
LDLLEPTFQE DKETEINFLL KQALTIVGTM PFTYMLEKWR WMVFREILCF SFIPRREIVG
VVEPVPHDET YCDPAMLFHV ANDYSFIRYY TRTIYQFQFQ EALCKAANHT GPLHTCDITN
SKAAGQKLRQ LLELGRSKPW TQALESVTGE KYMNAMPLLH YFEPLYKWLQ RNNSGRYIGW
KTDWAPYSDN AIKVRISLKS ALGSQAYGWD ESELFLFKSS VAYAMRKYFA EVKQQDVKFQ
ITDIHVGRQT QRISFYLTVS MPGNISDVVP KADVENAIRM SRGRINEAFR LDDNTLEFVG
ILPTLATPYE PPVTIWLIIF GVVISLVVIG VIVLIITGQR DRKKRAREYG SEARSNCEEE
NPYDEGGKSN MGFESPEETQ TSF
//
