ID   B0JZU8_XENTR            Unreviewed;      1284 AA.
AC   B0JZU8;
DT   18-MAR-2008, integrated into UniProtKB/TrEMBL.
DT   18-MAR-2008, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   RecName: Full=Angiotensin-converting enzyme {ECO:0000256|RuleBase:RU361144};
DE            EC=3.4.-.- {ECO:0000256|RuleBase:RU361144};
GN   Name=ace {ECO:0000313|EMBL:AAI59327.1,
GN   ECO:0000313|RefSeq:NP_001116882.1,
GN   ECO:0000313|Xenbase:XB-GENE-479789};
GN   Synonyms=ace1 {ECO:0000313|RefSeq:NP_001116882.1}, cd143
GN   {ECO:0000313|RefSeq:NP_001116882.1}, dcp
GN   {ECO:0000313|RefSeq:NP_001116882.1}, dcp1
GN   {ECO:0000313|RefSeq:NP_001116882.1}, xace
GN   {ECO:0000313|RefSeq:NP_001116882.1};
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364 {ECO:0000313|EMBL:AAI59327.1};
RN   [1] {ECO:0000313|RefSeq:NP_001116882.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=12454917; DOI=10.1002/dvdy.10174;
RA   Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA   Richardson P.;
RT   "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT   initiative.";
RL   Dev. Dyn. 225:384-391(2002).
RN   [2] {ECO:0000313|EMBL:AAI59327.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=TGA IC {ECO:0000313|EMBL:AAI59327.1};
RC   TISSUE=Testes {ECO:0000313|EMBL:AAI59327.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|RefSeq:NP_001116882.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU361144};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|RuleBase:RU361144};
CC   -!- COFACTOR:
CC       Name=chloride; Xref=ChEBI:CHEBI:17996;
CC         Evidence={ECO:0000256|ARBA:ARBA00001923};
CC   -!- SIMILARITY: Belongs to the peptidase M2 family.
CC       {ECO:0000256|ARBA:ARBA00008139, ECO:0000256|RuleBase:RU361144}.
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DR   EMBL; BC159326; AAI59327.1; -; mRNA.
DR   RefSeq; NP_001116882.1; NM_001123410.1.
DR   MEROPS; M02.001; -.
DR   GeneID; 100144634; -.
DR   KEGG; xtr:100144634; -.
DR   AGR; Xenbase:XB-GENE-479789; -.
DR   CTD; 1636; -.
DR   Xenbase; XB-GENE-479789; ace.
DR   OMA; DYSDFQD; -.
DR   OrthoDB; 2898149at2759; -.
DR   Proteomes; UP000008143; Chromosome 10.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 2.
DR   Gene3D; 1.10.1370.30; -; 3.
DR   InterPro; IPR001548; Peptidase_M2.
DR   PANTHER; PTHR10514; ANGIOTENSIN-CONVERTING ENZYME; 1.
DR   PANTHER; PTHR10514:SF27; ANGIOTENSIN-CONVERTING ENZYME; 1.
DR   Pfam; PF01401; Peptidase_M2; 2.
DR   PRINTS; PR00791; PEPDIPTASEA.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 2.
PE   2: Evidence at transcript level;
KW   Carboxypeptidase {ECO:0000256|RuleBase:RU361144};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180,
KW   ECO:0000256|RuleBase:RU361144}; Hydrolase {ECO:0000256|RuleBase:RU361144};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|RuleBase:RU361144};
KW   Metalloprotease {ECO:0000256|RuleBase:RU361144};
KW   Protease {ECO:0000256|RuleBase:RU361144};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008143};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|RuleBase:RU361144}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..1284
FT                   /note="Angiotensin-converting enzyme"
FT                   /evidence="ECO:0000256|SAM:SignalP,
FT                   ECO:0000313|RefSeq:NP_001116882.1"
FT                   /id="PRO_5033207444"
FT   TRANSMEM        1247..1267
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   1284 AA;  148040 MW;  81BE5E5F44FDF291 CRC64;
     MRVLLLGLLL LVGTNSALDS SFLPGTYPKD EAGARDFADA YNSTAEVILF KSVEASWAYN
     TNLTDYNSKQ QILASMEEQE FNEAWGMKAK ELFNDVWENF TDPLLKKIIS SIRTLGASNL
     NLTAREEYNT ILSEMDSIYS TAKVCPPNAT AKCWSLEPEI TEIMATSRSY KKLLYAWEGW
     HNSAGIPLKE KYLRFVQLSN EAYRMDGYKD TGAYWRSWYA SPTFEEDLDG LYQQLEPLYL
     NLHAFVRRKL YERYGAKYIN LKGPIPAHLF GNMWSQQWNN IYDMMIPFPD KTNIDVTNTM
     REKGWNATHM FRVSEEFFTS LGLLEMPPEF WEKSMLEKPA DGREVVCHAS AWDFYNRKDF
     RIKQCTTVTM EQLFTVHHEM GHVEYYLQYK DQPVTYRRGA NPGFHEAIGD VLSLSVSTPG
     HLKTIGLLET VTNDKESDIN YLLKMALEKI AFLPFGFLID QWRWNVFSGR TPPTRYNYDW
     WNLRTKYQGI CPPISRDDNQ FDAGAKYHIP GNTPYIRYFV SFVLQFQFHK ALCTAAKHTG
     PLHTCDIYRS QEAGKILGDV LRSGSSKSWQ EVLKDMTGSE KMDVGPLLEY FTPVTQWLIE
     QNTKNNEILG WPDFSWTPPM PDGYPGDIEK IANEKEADTF LSDYTKSAEV VWNDYTEASW
     AYNTNITEAN KQVMLDKNLA MSGHTLQYGL QARNYDYSDF QDPETQRILR KLSEIDKAAL
     SEEEQKEYNQ ITSDMETIYS VAKVCKDGNT NCHPLDPDLT EILAKSRDYD ELLFAWKGWR
     DASGKQIREK YKRYVQLANK AAQLNGYNDN GAYWRSWYET PTLESDVEKL YDELQPLYLN
     LHAYVRRALY KKYGDKRINL KGPIPAHLLG NMWAQSWSNI YELLVPYPNA AQVDATPAMI
     AKNWTPKRMF EESDNFFKSL GLLPMPQEFW DKSMIEKPKD REVVCHASAW DFYNRKDFRI
     KQCTVVNMDD LITVHHEMGH VQYFLQYKDQ PILFREGANP GFHEAIGDVL ALSVSTPKHL
     QSIGLLDKVE DNPESDINYL MSIALDKIAF LPFGFLMDQW RWKVFDGRTP DSEYNQQWWN
     LRLKYQGLVP PVLRTENDFD PGAKFHIPAS VPYIRYFISF VIQFQFHEAL CKAANQEGPL
     HKCDIYQSTQ AGKLLGDAMK LGNSKPWPEA MQTITGQRNM SAHALLKYFQ PLTDWLIKEN
     TKNGETLGWP EYNWSPVQSV PLPPSGDSNS DFLGLAVSNS QAAAGQWILL ALGIVLIITT
     IVFGVLYSKM KSRAKMSSSQ MELK
//