ID   A0A091D6K2_FUKDA        Unreviewed;      1328 AA.
AC   A0A091D6K2;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Angiotensin-converting enzyme {ECO:0000256|RuleBase:RU361144};
DE            EC=3.4.-.- {ECO:0000256|RuleBase:RU361144};
GN   ORFNames=H920_10956 {ECO:0000313|EMBL:KFO27694.1};
OS   Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC   Fukomys.
OX   NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO27694.1, ECO:0000313|Proteomes:UP000028990};
RN   [1] {ECO:0000313|EMBL:KFO27694.1, ECO:0000313|Proteomes:UP000028990}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Liver {ECO:0000313|EMBL:KFO27694.1};
RA   Gladyshev V.N., Fang X.;
RT   "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT   African mole rats.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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; KN122870; KFO27694.1; -; Genomic_DNA.
DR   STRING; 885580.ENSFDAP00000018719; -.
DR   MEROPS; M02.004; -.
DR   eggNOG; KOG3690; Eukaryota.
DR   Proteomes; UP000028990; Unassembled WGS sequence.
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   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   3: Inferred from homology;
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:UP000028990};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|RuleBase:RU361144}.
FT   TRANSMEM        1286..1307
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          29..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          590..665
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        615..643
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        644..658
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1328 AA;  153097 MW;  C43D4F23E9705FCC CRC64;
     MCDCLCQAPD SLCPQRVGGK VLLHLYSSPN TTTTSIPPRL PGRPPAQPRS QEEAALLSQE
     FSEAWGQKAK ELYEHIWQNF TDPQLRRVIQ SVSTLGPANL PLAKRHQYNS LLSNMSRIYS
     TGKVCFPNKT ATCWSLDPEL TNILASSRSY AMLLFAWEGW HNSVGIPLKP LYQDFTTLSN
     EAYKQDGFSD TGAYWRSWYD SPTFEKDLEH LYHQLEPLYL NLHAYVRRTL YRRYGDKYIN
     LRGPIPAHLL GNMWAQSWEN IYDMVVPFPD KPNLDVTSTM VEKGWNATHM FRVAEEFFTS
     LGLSPMPPEF WAESMLEKPS DGREVVCHAS AWDFYNRKDF RIKQCTRVTM DHLYTVHHEM
     GHVQYYLQYK ELPVSLRRGA NPGFHEAIGD VLALSVSTPA HLHKIGLLER VTNDSESDIN
     YLLKMALEKI AFLPFGYLVD QWRWEVFSGR TPPSRYNFDW WYLRTKYQGI CPPVVRNETH
     FDAGAKFHVP NVTPYVRYFV SFVLQFQFHQ ALCKEAGHQG PLHQCDIYQS SQAGAKLREV
     LQAGCSRPWQ EVLKDLVGSD ALDAQPLLSY FQPVSKWLQE QNQRNGEVLG WPEYQWRPPL
     PNNYPEGIGD GQPGDSRPSV NQKPDNSPRN NQPENTQTDH SPPENPEPKW DHRERPGSWG
     NGEAGMADLV TDEAEANKFV EEYDRTSQVV WNEYSEANWN YNTNITAEAS KVLLQKNMEV
     ANHTLKYGTW AKQFDVSHLQ NATTKRIIKK VQDLDRAALP TQELEEYNQI LLDMETTYSV
     ANVCCTNGTC LHLEPDLTNV MATSRKYEEL LWVWKSWRDK VGRAILPFFP KYVELSNKAA
     RLNGYVDAGD SWRSMYETPS LEQDLERLFQ ELQPLYLNLH AYVRRALHRH YGPEHINLEG
     PIPAHLLGNM WAQTWSNIYD LVVPFPSAPK MDATEAMIQQ GWTPRRMFKE ADDFFTSLGL
     LPVPPEFWNK SMLEKPTDGR EVVCHASAWD FYNGKDFRIK QCTTVNMEEL VVVHHEMGHI
     QYFMQYKDLP LAFREGANPG FHEAIGDVLA LSVSTPKHLH SLNLLSSEGD SYEHDINFLM
     KMALDKIAFI PFSYLIDQWR WRVFDGSITK ENYNQEWWSL RLKYQGLCPP VPRSQDDFDP
     GAKFHVPSSV PYIRYFVSFI IQFQFHEALC QAAGHQGPLH KCDIYQSKEA GKRLGDTMKL
     GFSKPWPEAM KQITGQPNMS GLAMMNYFKP LMDWLVTENG RHGEKLGWPQ YNWTPNSARS
     ENFSDSGRVN FLGMNLEPQQ ARMGQWVLLF LGVALLVATL GLTQRLFSIR HHSLRQPQFG
     SEVELRHS
//