ID F6X3S4_HUMAN Unreviewed; 739 AA. AC F6X3S4; L7MUH0; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 2. DT 16-JAN-2019, entry version 62. DE RecName: Full=Angiotensin-converting enzyme {ECO:0000256|RuleBase:RU361144}; DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361144}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000464149, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000464149, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., RA Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in RT the human lineage."; RL Nature 440:1045-1049(2006). RN [2] {ECO:0000313|Ensembl:ENSP00000464149} RP IDENTIFICATION. RG Ensembl; RL Submitted (JAN-2013) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|RuleBase:RU361144}; CC Note=Binds 1 zinc ion per subunit. CC {ECO:0000256|RuleBase:RU361144}; CC -!- SIMILARITY: Belongs to the peptidase M2 family. CC {ECO:0000256|RuleBase:RU361144}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AC113554; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; F6X3S4; -. DR SMR; F6X3S4; -. DR STRING; 9606.ENSP00000464149; -. DR iPTMnet; F6X3S4; -. DR BioMuta; ENSG00000264813; -. DR jPOST; F6X3S4; -. DR PaxDb; F6X3S4; -. DR PeptideAtlas; F6X3S4; -. DR PRIDE; F6X3S4; -. DR Ensembl; ENST00000577647; ENSP00000464149; ENSG00000264813. DR UCSC; uc060inx.1; human. DR EuPathDB; HostDB:ENSG00000264813.6; -. DR GeneCards; ENSG00000264813; -. DR OpenTargets; ENSG00000264813; -. DR eggNOG; KOG3690; Eukaryota. DR eggNOG; ENOG410XPJ3; LUCA. DR GeneTree; ENSGT00940000163600; -. DR OMA; GWTTSNK; -. DR Proteomes; UP000005640; Chromosome 17. DR Bgee; ENSG00000264813; Expressed in 8 organ(s), highest expression level in right testis. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW. DR GO; GO:0008239; F:dipeptidyl-peptidase activity; IBA:GO_Central. DR GO; GO:0008238; F:exopeptidase activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008237; F:metallopeptidase activity; IBA:GO_Central. DR GO; GO:0008241; F:peptidyl-dipeptidase activity; IBA:GO_Central. DR GO; GO:0045777; P:positive regulation of blood pressure; IBA:GO_Central. DR GO; GO:0003084; P:positive regulation of systemic arterial blood pressure; IBA:GO_Central. DR GO; GO:0003081; P:regulation of systemic arterial blood pressure by renin-angiotensin; IBA:GO_Central. DR CDD; cd06461; M2_ACE; 1. DR InterPro; IPR001548; Peptidase_M2. DR PANTHER; PTHR10514; PTHR10514; 1. DR Pfam; PF01401; Peptidase_M2; 1. DR PRINTS; PR00791; PEPDIPTASEA. PE 3: Inferred from homology; KW Carboxypeptidase {ECO:0000256|RuleBase:RU361144}; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Glycoprotein {ECO:0000256|RuleBase:RU361144}; KW 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 Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}; KW Zinc {ECO:0000256|RuleBase:RU361144}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 739 Angiotensin-converting enzyme. FT {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5009955082. SQ SEQUENCE 739 AA; 83989 MW; 9F57FF3922654E04 CRC64; MGQGWATAGL PSLLFLLLCY GHPLLVPSQE ASQQVTVTHG TSSQATTSSQ TTTHQATAHQ TSAQSPNLVT DEAEASKFVE EYDRTSQVVW NEYAEANWNY NTNITTETSK ILLQKNMQIA NHTLKYGTQA RKFDVNQLQN TTIKRIIKKV QDLERAALPA QELEEYNKIL LDMETTYSVA TVCHPNGSCL QLEPDLTNVM ATSRKYEDLL WAWEGWRDKA GRAILQFYPK YVELINQAAR LNGYVDAGDS WRSMYETPSL EQDLERLFQE LQPLYLNLHA YVRRALHRHY GAQHINLEGP IPAHLLGNMW AQTWSNIYDL VVPFPSAPSM DTTEAMLKQG WTPRRMFKEA DDFFTSLGLL PVPPEFWNKS MLEKPTDGRE VVCHASAWDF YNGKDFRIKQ CTTVNLEDLV VAHHEMGHIQ YFMQYKDLPV ALREGANPGF HEAIGDVLAL SVSTPKHLHS LNLLSSEGGS DEHDINFLMK MALDKIAFIP FSYLVDQWRW RVFDGSITKE NYNQEWWSLR LKYQGLCPPV PRTQGDFDPG AKFHIPSSVP YIRYFVSFII QFQFHEALCQ AAGHTGPLHK CDIYQSKEAG QRLATAMKLG FSRPWPEAMQ LITGQPNMSA SAMLSYFKPL LDWLRTENEL HGEKLGWPQY NWTPNSDDFY NETETKIFLQ FYDQTGIWDH GAPHLLPPSQ ARGTREAPVY MSKRAASSGP PGSPKLPPAA QGHGEVPVHD LLWHPGPPV //