ID C7ECU2_MOUSE Unreviewed; 787 AA.
AC C7ECU2;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Angiotensin-converting enzyme {ECO:0000256|RuleBase:RU361144};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361144};
DE Flags: Fragment;
GN Name=Ace2 {ECO:0000313|MGI:MGI:1917258};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000313|EMBL:ACT66269.1};
RN [1] {ECO:0000313|EMBL:ACT66269.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BALB/c {ECO:0000313|EMBL:ACT66269.1};
RA Li K.K.B., Yip C.W., Hon C.C., Lam C.Y., Leung F.C.C.;
RT "Comparative susceptibility to SARS-CoV mediated by ACE2 protein of 15
RT different species.";
RL Submitted (JUN-2009) 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; GQ262785; ACT66269.1; -; mRNA.
DR AlphaFoldDB; C7ECU2; -.
DR SMR; C7ECU2; -.
DR MEROPS; M02.006; -.
DR PeptideAtlas; C7ECU2; -.
DR AGR; MGI:1917258; -.
DR MGI; MGI:1917258; Ace2.
DR ChiTaRS; Ace2; mouse.
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 2: Evidence at transcript level;
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 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..787
FT /note="Angiotensin-converting enzyme"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002976909"
FT TRANSMEM 741..765
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 617..770
FT /note="Collectrin"
FT /evidence="ECO:0000259|Pfam:PF16959"
FT NON_TER 787
FT /evidence="ECO:0000313|EMBL:ACT66269.1"
SQ SEQUENCE 787 AA; 90354 MW; BABEE8A359E310D8 CRC64;
MSSSSWLLLS LVTVTTAQSL TGENAKTFLN NFNQEAEDLS YQSSLASWNY NTNITEENAQ
KMSGAAAKWS AFYEEQSKTA QSFSLQEIQT PIIKRQLQAL QQSGSSALSA DKNKQLNTIL
NTMSTIYSTG KVCNPKNPQE CLLLESGLDE IMATSTDYNS RLWAWEGWRA EVGKQLRPLY
EEYVVLKNEM ARANNYNDYG DYWRGGYEAE GADGYNYNRN QLIEDVERTF AEIKPLYEHL
HAYVRRKLMD TYPSYISPTG CLPAHLLGDM WGRFWTNLYP LTVPFAQKPN IDVTDAMMNQ
GWDAERIFQE AEKFFVSVGL PHMTQGFWAN SMLTEPADGR KVVCHPTAWD LGHGDFRIKM
CTKVTMDNFL TAHHEMGHIQ YDMAYARQPF LLRNGANEGF HEAVGEIMSL SAATPKHLKS
IGLLPSDFQE DSETEINFLL KQALTIVGTL PFIYMLEKWR WMVFRGEIPK EQWMKKWWEM
KREIVGVVEP LRCDETYCDP ASLFHVSNDY SFIRYYTRTI YQFQFQEALC QAAKYNGSLH
KCDISNSTEA GQKLLKMLSL GNSEPWTKAL ENVVGARNMD VKPLLNYFQP LFDWLKEQNR
NSFVGWNTEW SPYADQSIKV RISLKSALGA NAYEWTNNEM FLFRSSVAYA MRKYFSIIKN
QTVPFLEEDV RVSDLKPRVS FYFFVTSPQN VSDVIPRSEV EDAIRMSRGR INDVFGLNDN
SLEFLGIHLT LEPPYQPPVT IWLIIFGVVM ALVVVGIIIL IVTGIKGRKK KNETKREENP
YDSMDIG
//
