ID Q4S4M8_TETNG Unreviewed; 1144 AA.
AC Q4S4M8;
DT 19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Angiotensin-converting enzyme {ECO:0000256|RuleBase:RU361144};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361144};
DE Flags: Fragment;
GN ORFNames=GSTENG00024111001 {ECO:0000313|EMBL:CAG04404.1};
OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883 {ECO:0000313|EMBL:CAG04404.1};
RN [1] {ECO:0000313|EMBL:CAG04404.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496914; DOI=10.1038/nature03025;
RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT early vertebrate proto-karyotype.";
RL Nature 431:946-957(2004).
RN [2] {ECO:0000313|EMBL:CAG04404.1}
RP NUCLEOTIDE SEQUENCE.
RG Genoscope;
RG Whitehead Institute Centre for Genome Research;
RL Submitted (FEB-2004) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CAG04404.1}.
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DR EMBL; CAAE01014738; CAG04404.1; -; Genomic_DNA.
DR AlphaFoldDB; Q4S4M8; -.
DR MEROPS; M02.004; -.
DR KEGG; tng:GSTEN00024111G001; -.
DR HOGENOM; CLU_006219_0_0_1; -.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
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 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 Metal-binding {ECO:0000256|RuleBase:RU361144};
KW Metalloprotease {ECO:0000256|RuleBase:RU361144};
KW Protease {ECO:0000256|RuleBase:RU361144};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Zinc {ECO:0000256|RuleBase:RU361144}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CAG04404.1"
FT NON_TER 1144
FT /evidence="ECO:0000313|EMBL:CAG04404.1"
SQ SEQUENCE 1144 AA; 132127 MW; 3DC93A1B63C9A2F3 CRC64;
QVNATLEDQA FTEAWGLKAK TTFSSSLDLL SNSEKKMMSK IKVLGSANLP LNEREEYNTI
LSNMERIYST AKVHPEPNVS WSLEPDLTEI MANSRSYKKL LFAWEGWHNE SGAPLRADYE
KFVRLSNKAS AADGFTDTGD YWRSWYESDT FEQDLEDLYK TIQPLYQNLH AFVRRKLYNQ
YGPKYINLKG PIPAHLLGNM WAQTWNNLYE LMIPFPDKPN IDVTKEMLAQ GYNATHMFRV
AEDFFESLNL DGMPDEFWEG SMLVKPTDRE VVCHASAWDF YNRKDFRIKQ CTTVTMEQLF
TVHHEMGHIQ YYLQYKHQPV GFRRGANPGF HEAIGDVLSL SVSTPKHLHS IKLLDSLVTD
SEMDTNYLLK MALEKIAFLP FGYLIDQWRW GVFSGRTPPE KYNSEWWFLR TKYQGICPGT
KRTEAHFDPG AKFHIPGNTP YIRYFVSFIL QFQLHEKLCE AANHTGPLHR CDIYRSAEAG
AILKNILQAG SSKAWPDVLQ DAIGVNKLNA SALMKYFKPI TDWLEIQNEN ETLGWPEISW
VPPIPEGYPG DIGMNTDEAD AVMLLTDYNS TAEVVWNAYT EASWKYNTDI NKDNEDAMLK
KNLEMSAHTL EYGQKARKYD TTDFQDASVK RIIEKLSDIE RAALSKDELE EYNTLLSSME
TKYSVATVCR EGGPCLPLDP DLQKIMAESR DYDELLFAWK GWRESAGKVL RQDYKRYVEL
ANKAATLNGH TDNGAFWRSL YETPTFEQDL EVLWKDLEPL YHNVHAYVRR ALYKKYGPKR
INLKGPIPAH LLGNMWAQTW SGIMDLVIPY PDATQVDATP AMVEQNWNAT RMFQESDRFF
TSLGLEPMPQ EFWDKSMLEK PSDGRKVVCH ASAWDFYNRK DFRIKQCTVV TMDDLITVHH
EMGHVQYFLQ YKDQPVSFRD GANPGFHEAI GDVLALSVST PKHLKSIGLL DKVENNYESD
INFLLSMALD KISFLPFGYL MDQWRWKVFD GRISSSEYNK EWWNLRMKYQ GLCPPIARTE
EDFDPGAKFH IPANVPYVRY FVSFVIQFQF HKALCEAAKH NGSLHTCDIY QSKEAGKLLG
DVMKLGASKP WPEAMAMMTG QPKMSAKPLM EYFSPLIDWL EKQNKENNDI LGWPEYDWKP
ENSS
//
