ID M4AJE2_XIPMA Unreviewed; 1290 AA.
AC M4AJE2;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Angiotensin-converting enzyme {ECO:0000256|RuleBase:RU361144};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361144};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000014586.1, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000014586.1}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000014586.1};
RG Ensembl;
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 RefSeq; XP_014329010.1; XM_014473524.1.
DR STRING; 8083.ENSXMAP00000014586; -.
DR Ensembl; ENSXMAT00000014606.2; ENSXMAP00000014586.1; ENSXMAG00000014511.2.
DR GeneID; 102221242; -.
DR KEGG; xma:102221242; -.
DR eggNOG; KOG3690; Eukaryota.
DR GeneTree; ENSGT00940000163600; -.
DR HOGENOM; CLU_006219_0_0_1; -.
DR InParanoid; M4AJE2; -.
DR OMA; DYSDFQD; -.
DR OrthoDB; 2898149at2759; -.
DR Proteomes; UP000002852; 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 Gene3D; 1.10.1370.30; -; 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:UP000002852};
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..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..1290
FT /note="Angiotensin-converting enzyme"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004047757"
FT TRANSMEM 1251..1269
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 1290 AA; 148620 MW; 255114391748F3DE CRC64;
MGAMVPEARR LLRAALLLLP ALLLLCEALP AAWLPGDYVD SVDDAQRFLG DYNSTAEEVS
FYSVSASWNY NTNLTEHNSK LQVAASLEEQ AFVEAWGGKA KQVFSLDTLN SLSTADKKLI
EKIKSLGAAN LPQAEREEYN TILSTMDSIY STAKVYPEPD ISWSLEPELT EILANSRSYK
KLLFAWEGWH NASGVPLKEH YPRFVELSNN ASKLDGFNDT GADWRSWYET ETFQQDLENL
YKTIEPLYLN LHAFVRRKLY NFYGPKYINL KGPIPAHLLG NMWAQAWNNI YDMMIPFPDK
PNLDVTNEMV KQGYNATHMF RVAEEFFTSL GLKEMPPEFW DGSMLVKPED REVVCHASAW
DFYNRRDFRI KQCTTVTMEQ LFTVHHEMGH IQYYLQYKDQ PIGYRRGANP GFHEAIGDVM
SLSVSTPKHL HEINLLESVT TDAETDLNFL LKTALEKIAF LPFGYLIDLW RWGVFSGSIP
PEKYNSEWWY LRTKYQGICP PTSRTEEHFD PGAKYHIPGN TPYIRYFVSF ILQFQFHEKL
CEAAKHTGPL HTCDIYRSAE AGEILRNVLE AGSSKPWPEV LQEAIGTNKM NAASLMKYFD
PIIKWLEQQN VNETLGWPEF NWVPPIPEGY PEDIDKNTDE LHAKQFLDEY NSTVEIVWNA
YTEANWKYNT NITGANNQEV LKKDLEMAAH TLEYGLKARQ YDTSDFQDPS VKRIIKKLSD
LEKAALPTAE LEELNNIMSN METKYSVAEV CRENGKCHPL DPDLQRIMAE SRDYDELLFA
WKGWRDAAGK VIRDDYKRYV ELANKAATLN GHSDNGAFWR SLYETPTFEE DLEALWKELE
PLYLNVHAYV RRALYKKYGS DSINLKGPIP AHLLGNMWAQ TWSGIMDLVM PYPDATQVDA
TPAMVSQGWN ATRMFQESDR FFTSLGLLPM PQEFWDKSML EKPTDGRQVV CHASAWDFFN
RKDFRIKQCT VVTMDDLITV HHEMGHVQYF LQYKDQPVSF RTGANPGFHE AIGDVLALSV
STPKHLQSIG LLDKVESNHE SDINFLMSMA LDKIAFLPFG YLMDQWRWKV FDGRIPSSDY
NKEWWNLRLK YQGLCPPVTR TEDDFDPGAK FHVPASVPYV RYFISFVIQF QFHKALCDAA
KHDGPLHTCD IYRSKEAGKL LGDVMRLGYS KPWPEAMAMI TGQSKMSVQP LMQYFQPLIT
WLEEENKKNN EVRGWPDYNW RPSDPDVATN DEKVEFLGLK VDKAAAKAGQ WLLLSISLAF
LVVIIQLAYK YRKSKKRNKS LSMMELKQKD
//
