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

 ACE2_PAGLA              Reviewed;         805 AA.
Q56NL1;
19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
10-MAY-2005, sequence version 1.
22-NOV-2017, entry version 73.
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;
Paguma larvata (Masked palm civet).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Feliformia; Viverridae;
Paradoxurinae; Paguma.
NCBI_TaxID=9675;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH SARS-COV S PROTEIN.
PubMed=15791205; DOI=10.1038/sj.emboj.7600640;
Li W., Zhang C., Sui J., Kuhn J.H., Moore M.J., Luo S., Wong S.-K.,
Huang I.-C., Xu K., Vasilieva N., Murakami A., He Y., Marasco W.A.,
Guan Y., Choe H., Farzan M.;
"Receptor and viral determinants of SARS-coronavirus adaptation to
human ACE2.";
EMBO J. 24:1634-1643(2005).
[2]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 19-613, ZINC-BINDING SITES,
AND DISULFIDE BONDS.
PubMed=22291007; DOI=10.1074/jbc.M111.325803;
Wu K., Peng G., Wilken M., Geraghty R.J., Li F.;
"Mechanisms of host receptor adaptation by severe acute respiratory
syndrome coronavirus.";
J. Biol. Chem. 287:8904-8911(2012).
-!- 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). Functional receptor
for human coronavirus SARS. {ECO:0000250}.
-!- CATALYTIC ACTIVITY: Angiotensin II + H(2)O = angiotensin-(1-7) +
L-phenylalanine.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Note=Binds 1 zinc ion per subunit.;
-!- COFACTOR:
Name=chloride; Xref=ChEBI:CHEBI:17996;
Note=Binds 1 Cl(-) ion per subunit.;
-!- SUBUNIT: Interacts with ITGB1 and the catalytically active form of
TMPRSS2 (By similarity). Interacts with SARS-CoV S protein.
{ECO:0000250, ECO:0000269|PubMed:15791205}.
-!- 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; AY881174; AAX63775.1; -; mRNA.
PDB; 3D0G; X-ray; 2.80 A; A/B=19-55.
PDB; 3D0H; X-ray; 3.10 A; A/B=19-55.
PDB; 3D0I; X-ray; 2.90 A; A/B=19-55.
PDB; 3SCK; X-ray; 3.00 A; A/B=19-82.
PDB; 3SCL; X-ray; 3.00 A; A/B=19-82.
PDBsum; 3D0G; -.
PDBsum; 3D0H; -.
PDBsum; 3D0I; -.
PDBsum; 3SCK; -.
PDBsum; 3SCL; -.
ProteinModelPortal; Q56NL1; -.
SMR; Q56NL1; -.
MEROPS; M02.006; -.
HOVERGEN; HBG000265; -.
EvolutionaryTrace; Q56NL1; -.
GO; GO:0009986; C:cell surface; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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: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.
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.
1: Evidence at protein level;
3D-structure; Carboxypeptidase; Cell membrane; Chloride; Cytoplasm;
Disulfide bond; Glycoprotein; Hydrolase; Membrane; Metal-binding;
Metalloprotease; Protease; Secreted; Signal; Transmembrane;
Transmembrane helix; Zinc.
SIGNAL 1 17 {ECO:0000255}.
CHAIN 18 805 Angiotensin-converting enzyme 2.
/FTId=PRO_0000028572.
CHAIN 18 708 Processed angiotensin-converting enzyme
2.
/FTId=PRO_0000292270.
TOPO_DOM 18 740 Extracellular. {ECO:0000255}.
TRANSMEM 741 761 Helical. {ECO:0000255}.
TOPO_DOM 762 805 Cytoplasmic. {ECO:0000255}.
REGION 30 41 Interaction with SARS S protein.
REGION 82 84 Interaction with SARS S protein.
{ECO:0000250}.
REGION 90 93 Interaction with SARS S protein.
REGION 353 357 Interaction with SARS S protein.
{ECO:0000250}.
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.
METAL 378 378 Zinc; catalytic.
METAL 402 402 Zinc; catalytic.
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 216 216 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:0000269|PubMed:22291007}.
DISULFID 344 361 {ECO:0000269|PubMed:22291007}.
DISULFID 530 542 {ECO:0000269|PubMed:22291007}.
HELIX 21 52 {ECO:0000244|PDB:3D0G}.
SEQUENCE 805 AA; 92611 MW; CF6406851F73E378 CRC64;
MSGSFWLLLS FAALTAAQST TEELAKTFLE TFNYEAQELS YQSSVASWNY NTNITDENAK
NMNEAGAKWS AYYEEQSKLA QTYPLAEIQD AKIKRQLQAL QQSGSSVLSA DKSQRLNTIL
NAMSTIYSTG KACNPNNPQE CLLLEPGLDN IMENSKDYNE RLWAWEGWRA EVGKQLRPLY
EEYVALKNEM ARANNYEDYG DYWRGDYEEE WTGGYNYSRN QLIQDVEDTF EQIKPLYQHL
HAYVRAKLMD TYPSRISRTG CLPAHLLGDM WGRFWTNLYP LTVPFGQKPN IDVTDAMVNQ
NWDARRIFKE AEKFFVSVGL PNMTQGFWEN SMLTEPGDGR KVVCHPTAWD LGKGDFRIKM
CTKVTMDDFL TAHHEMGHIQ YDMAYAAQPF LLRNGANEGF HEAVGEIMSL SAATPNHLKT
IGLLSPAFSE DNETEINFLL KQALTIVGTL PFTYMLEKWR WMVFKGAIPK EQWMQKWWEM
KRNIVGVVEP VPHDETYCDP ASLFHVANDY SFIRYYTRTI YQFQFQEALC QIAKHEGPLH
KCDISNSTEA GKKLLEMLSL GRSEPWTLAL ERVVGAKNMN VTPLLNYFEP LFTWLKEQNR
NSFVGWDTDW RPYSDQSIKV RISLKSALGE KAYEWNDNEM YLFRSSIAYA MREYFSKVKN
QTIPFVEDNV WVSDLKPRIS FNFFVTFSNN VSDVIPRSEV EDAIRMSRSR INDAFRLDDN
SLEFLGIEPT LSPPYRPPVT IWLIVFGVVM GAIVVGIVLL IVSGIRNRRK NDQAGSEENP
YASVDLNKGE NNPGFQHADD VQTSF


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