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Angiotensin-converting enzyme 2 (EC 3.4.17.23) (ACE-related carboxypeptidase) [Cleaved into: Processed angiotensin-converting enzyme 2]

 ACE2_FELCA              Reviewed;         805 AA.
Q56H28; Q2PGE2;
19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
10-MAY-2005, sequence version 1.
28-FEB-2018, entry version 87.
RecName: Full=Angiotensin-converting enzyme 2;
EC=3.4.17.23;
AltName: Full=ACE-related carboxypeptidase;
Contains:
RecName: Full=Processed angiotensin-converting enzyme 2;
Flags: Precursor;
Name=ACE2;
Felis catus (Cat) (Felis silvestris catus).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae;
Felinae; Felis.
NCBI_TaxID=9685;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Wang C., Guo A.Z., Chen H.C.;
"Identification of cat ACE2 gene and its potential function as a SARS-
CoV receptor.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Kidney;
Zamoto A., Tagichi F., Fukushi S., Morikawa S., Yamada Y.K.;
"Identification of cat and racoon ACE2 and the its receptor function
for SARS-CoV.";
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Carboxypeptidase which converts angiotensin I to
angiotensin 1-9, a peptide of unknown function, and angiotensin II
to angiotensin 1-7, a vasodilator. Also able to hydrolyze apelin-
13 and dynorphin-13 with high efficiency. May be an important
regulator of heart function (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: Angiotensin II + H(2)O = angiotensin-(1-7) +
L-phenylalanine.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- COFACTOR:
Name=chloride; Xref=ChEBI:CHEBI:17996; Evidence={ECO:0000250};
Note=Binds 1 Cl(-) ion per subunit. {ECO:0000250};
-!- SUBUNIT: Interacts with ITGB1 and the catalytically active form of
TMPRSS2. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Processed angiotensin-converting enzyme 2:
Secreted {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass
type I membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}.
Note=Detected in both cell membrane and cytoplasm in neurons.
{ECO:0000250}.
-!- PTM: Proteolytic cleavage by ADAM17 generates a secreted form.
Also cleaved by serine proteases: TMPRSS2, TMPRSS11D and
HPN/TMPRSS1 (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase M2 family. {ECO:0000305}.
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EMBL; AY957464; AAX59005.1; -; mRNA.
EMBL; AB211997; BAE72461.1; -; mRNA.
RefSeq; NP_001034545.1; NM_001039456.1.
RefSeq; XP_006943638.1; XM_006943576.2.
RefSeq; XP_019678890.1; XM_019823331.1.
ProteinModelPortal; Q56H28; -.
SMR; Q56H28; -.
STRING; 9685.ENSFCAP00000008647; -.
MEROPS; M02.006; -.
Ensembl; ENSFCAT00000009326; ENSFCAP00000008647; ENSFCAG00000009320.
GeneID; 554349; -.
KEGG; fca:554349; -.
CTD; 59272; -.
eggNOG; KOG3690; Eukaryota.
eggNOG; ENOG410XPJ3; LUCA.
GeneTree; ENSGT00520000055576; -.
HOVERGEN; HBG000265; -.
InParanoid; Q56H28; -.
KO; K09708; -.
OMA; DFLTAHH; -.
OrthoDB; EOG091G033S; -.
Proteomes; UP000011712; Chromosome X.
Bgee; ENSFCAG00000009320; -.
GO; GO:0009986; C:cell surface; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005615; C:extracellular space; IEA:Ensembl.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
GO; GO:0004175; F:endopeptidase activity; IEA:Ensembl.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
GO; GO:0008241; F:peptidyl-dipeptidase activity; IEA:InterPro.
GO; GO:0001618; F:virus receptor activity; ISS:UniProtKB.
GO; GO:0003051; P:angiotensin-mediated drinking behavior; IEA:Ensembl.
GO; GO:0060452; P:positive regulation of cardiac muscle contraction; IEA:Ensembl.
GO; GO:1903598; P:positive regulation of gap junction assembly; IEA:Ensembl.
GO; GO:0032800; P:receptor biosynthetic process; IEA:Ensembl.
GO; GO:0046813; P:receptor-mediated virion attachment to host cell; IEA:Ensembl.
GO; GO:1903779; P:regulation of cardiac conduction; IEA:Ensembl.
GO; GO:0015827; P:tryptophan transport; IEA:Ensembl.
CDD; cd06461; M2_ACE; 1.
InterPro; IPR031588; Collectrin_dom.
InterPro; IPR001548; Peptidase_M2.
PANTHER; PTHR10514; PTHR10514; 1.
Pfam; PF16959; Collectrin; 1.
Pfam; PF01401; Peptidase_M2; 1.
PRINTS; PR00791; PEPDIPTASEA.
PROSITE; PS00142; ZINC_PROTEASE; 1.
2: Evidence at transcript level;
Carboxypeptidase; Cell membrane; Chloride; Complete proteome;
Cytoplasm; Disulfide bond; Glycoprotein; Hydrolase; Membrane;
Metal-binding; Metalloprotease; Protease; Reference proteome;
Secreted; Signal; Transmembrane; Transmembrane helix; Zinc.
SIGNAL 1 17 {ECO:0000255}.
CHAIN 18 805 Angiotensin-converting enzyme 2.
/FTId=PRO_0000028569.
CHAIN 18 708 Processed angiotensin-converting enzyme
2.
/FTId=PRO_0000292267.
TOPO_DOM 18 740 Extracellular. {ECO:0000255}.
TRANSMEM 741 761 Helical. {ECO:0000255}.
TOPO_DOM 762 805 Cytoplasmic. {ECO:0000255}.
REGION 652 659 Essential for cleavage by ADAM17.
{ECO:0000250}.
REGION 697 716 Essential for cleavage by TMPRSS11D and
TMPRSS2. {ECO:0000250}.
ACT_SITE 375 375 {ECO:0000255|PROSITE-ProRule:PRU10095}.
ACT_SITE 505 505 {ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 374 374 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 378 378 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 402 402 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
BINDING 169 169 Chloride. {ECO:0000250}.
BINDING 273 273 Substrate. {ECO:0000250}.
BINDING 345 345 Substrate. {ECO:0000250}.
BINDING 346 346 Substrate; via carbonyl oxygen.
{ECO:0000250}.
BINDING 371 371 Substrate. {ECO:0000250}.
BINDING 477 477 Chloride. {ECO:0000250}.
BINDING 481 481 Chloride. {ECO:0000250}.
BINDING 515 515 Substrate. {ECO:0000250}.
CARBOHYD 53 53 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 90 90 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 216 216 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 299 299 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 322 322 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 546 546 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 660 660 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 690 690 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 133 141 {ECO:0000250}.
DISULFID 344 361 {ECO:0000250}.
DISULFID 530 542 {ECO:0000250}.
SEQUENCE 805 AA; 92708 MW; 9F41A2EF300BE19E CRC64;
MSGSFWLLLS FAALTAAQST TEELAKTFLE KFNHEAEELS YQSSLASWNY NTNITDENVQ
KMNEAGAKWS AFYEEQSKLA KTYPLAEIHN TTVKRQLQAL QQSGSSVLSA DKSQRLNTIL
NAMSTIYSTG KACNPNNPQE CLLLEPGLDD IMENSKDYNE RLWAWEGWRA EVGKQLRPLY
EEYVALKNEM ARANNYEDYG DYWRGDYEEE WTDGYNYSRS QLIKDVEHTF TQIKPLYQHL
HAYVRAKLMD TYPSRISPTG CLPAHLLGDM WGRFWTNLYP LTVPFGQKPN IDVTDAMVNQ
SWDARRIFKE AEKFFVSVGL PNMTQGFWEN SMLTEPGDSR KVVCHPTAWD LGKGDFRIKM
CTKVTMDDFL TAHHEMGHIQ YDMAYAVQPF LLRNGANEGF HEAVGEIMSL SAATPNHLKT
IGLLSPGFSE DSETEINFLL KQALTIVGTL PFTYMLEKWR WMVFKGEIPK EQWMQKWWEM
KREIVGVVEP VPHDETYCDP ASLFHVANDY SFIRYYTRTI YQFQFQEALC RIAKHEGPLH
KCDISNSSEA GKKLLQMLTL GKSKPWTLAL EHVVGEKKMN VTPLLKYFEP LFTWLKEQNR
NSFVGWNTDW RPYADQSIKV RISLKSALGD EAYEWNDNEM YLFRSSVAYA MREYFSKVKN
QTIPFVEDNV WVSNLKPRIS FNFFVTASKN VSDVIPRSEV EEAIRMSRSR INDAFRLDDN
SLEFLGIQPT LSPPYQPPVT IWLIVFGVVM GVVVVGIVLL IVSGIRNRRK NNQARSEENP
YASVDLSKGE NNPGFQHADD VQTSF


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