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

 ACE2_BOVIN              Reviewed;         804 AA.
Q58DD0;
19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
26-APR-2005, sequence version 1.
25-OCT-2017, entry version 113.
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;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=16305752; DOI=10.1186/1471-2164-6-166;
Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
"Characterization of 954 bovine full-CDS cDNA sequences.";
BMC Genomics 6:166-166(2005).
-!- 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; BT021667; AAX46514.1; -; mRNA.
RefSeq; XP_005228486.1; XM_005228429.3.
UniGene; Bt.28278; -.
ProteinModelPortal; Q58DD0; -.
SMR; Q58DD0; -.
STRING; 9913.ENSBTAP00000045721; -.
MEROPS; M02.006; -.
PaxDb; Q58DD0; -.
PRIDE; Q58DD0; -.
Ensembl; ENSBTAT00000048730; ENSBTAP00000045721; ENSBTAG00000034402.
GeneID; 509235; -.
CTD; 59272; -.
eggNOG; KOG3690; Eukaryota.
eggNOG; ENOG410XPJ3; LUCA.
GeneTree; ENSGT00520000055576; -.
HOGENOM; HOG000292210; -.
HOVERGEN; HBG000265; -.
InParanoid; Q58DD0; -.
OMA; DFLTAHH; -.
OrthoDB; EOG091G033S; -.
TreeFam; TF312861; -.
Reactome; R-BTA-2022377; Metabolism of Angiotensinogen to Angiotensins.
Proteomes; UP000009136; Chromosome X.
Bgee; ENSBTAG00000034402; -.
GO; GO:0009986; C:cell surface; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; 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 18 804 Angiotensin-converting enzyme 2.
/FTId=PRO_0000028568.
CHAIN 18 707 Processed angiotensin-converting enzyme
2.
/FTId=PRO_0000292266.
TOPO_DOM 18 739 Extracellular. {ECO:0000255}.
TRANSMEM 740 760 Helical. {ECO:0000255}.
TOPO_DOM 761 804 Cytoplasmic. {ECO:0000255}.
REGION 651 658 Essential for cleavage by ADAM17.
{ECO:0000250}.
REGION 696 715 Essential for cleavage by TMPRSS11D and
TMPRSS2. {ECO:0000250}.
ACT_SITE 374 374 {ECO:0000255|PROSITE-ProRule:PRU10095}.
ACT_SITE 504 504 {ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 373 373 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 377 377 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 401 401 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
BINDING 168 168 Chloride. {ECO:0000250}.
BINDING 272 272 Substrate. {ECO:0000250}.
BINDING 344 344 Substrate. {ECO:0000250}.
BINDING 345 345 Substrate; via carbonyl oxygen.
{ECO:0000250}.
BINDING 370 370 Substrate. {ECO:0000250}.
BINDING 476 476 Chloride. {ECO:0000250}.
BINDING 480 480 Chloride. {ECO:0000250}.
BINDING 514 514 Substrate. {ECO:0000250}.
CARBOHYD 53 53 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 90 90 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 298 298 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 431 431 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 545 545 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 659 659 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 689 689 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 343 360 {ECO:0000250}.
DISULFID 529 541 {ECO:0000250}.
SEQUENCE 804 AA; 93067 MW; E81570A96872A963 CRC64;
MTGSFWLLLS LVAVTAAQST TEEQAKTFLE KFNHEAEDLS YQSSLASWNY NTNITDENVQ
KMNEARAKWS AFYEEQSRMA KTYSLEEIQN LTLKRQLKAL QHSGTSALSA EKSKRLNTIL
NKMSTIYSTG KVLDPNTQEC LALEPGLDDI MENSRDYNRR LWAWEGWRAE VGKQLRPLYE
EYVVLENEMA RANNYEDYGD YWRGDYEVTG AGDYDYSRDQ LMKDVERTFA EIKPLYEQLH
AYVRAKLMHT YPSYISPTGC LPAHLLGDMW GRFWTNLYSL TVPFEHKPSI DVTEKMENQS
WDAERIFKEA EKFFVSISLP YMTQGFWDNS MLTEPGDGRK VVCHPTAWDL GKGDFRIKMC
TKVTMDDFLT AHHEMGHIQY DMAYAAQPYL LRNGANEGFH EAVGEIMSLS AATPHYLKAL
GLLAPDFHED NETEINFLLK QALTIVGTLP FTYMLEKWRW MVFKGEIPKQ QWMEKWWEMK
REIVGVVEPL PHDETYCDPA CLFHVAEDYS FIRYYTRTIY QFQFHEALCK TAKHEGALFK
CDISNSTEAG QRLLQMLRLG KSEPWTLALE NIVGIKTMDV KPLLNYFEPL FTWLKEQNRN
SFVGWSTEWT PYSDQSIKVR ISLKSALGEN AYEWNDNEMY LFQSSVAYAM RKYFSEARNE
TVLFGEDNVW VSDKKPRISF KFFVTSPNNV SDIIPRTEVE NAIRLSRDRI NDVFQLDDNS
LEFLGIQPTL GPPYEPPVTI WLIIFGVVMG VVVIGIVVLI FTGIRNRRKK NQASSEENPY
GSVDLNKGEN NSGFQNIDDV QTSL


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