CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004051
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Angiotensin-converting enzyme 
Protein Synonyms/Alias
 ACE; Dipeptidyl carboxypeptidase I; Kininase II; CD143; Angiotensin-converting enzyme, soluble form 
Gene Name
 ACE 
Gene Synonyms/Alias
 DCP; DCP1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
718QLQNTTIKRIIKKVQubiquitination[1, 2]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789
Functional Description
 Converts angiotensin I to angiotensin II by release of the terminal His-Leu, this results in an increase of the vasoconstrictor activity of angiotensin. Also able to inactivate bradykinin, a potent vasodilator. Has also a glycosidase activity which releases GPI-anchored proteins from the membrane by cleaving the mannose linkage in the GPI moiety. 
Sequence Annotation
 REGION 30 630 Peptidase M2 1.
 REGION 631 1232 Peptidase M2 2.
 ACT_SITE 391 391 1.
 ACT_SITE 989 989 2.
 METAL 390 390 Zinc 1; catalytic.
 METAL 394 394 Zinc 1; catalytic.
 METAL 418 418 Zinc 1; catalytic.
 METAL 988 988 Zinc 2; catalytic.
 METAL 992 992 Zinc 2; catalytic.
 METAL 1016 1016 Zinc 2; catalytic.
 BINDING 231 231 Chloride 1.
 BINDING 529 529 Chloride 1.
 BINDING 791 791 Chloride 2.
 BINDING 829 829 Chloride 3.
 BINDING 1090 1090 Chloride 2.
 BINDING 1094 1094 Chloride 2.
 BINDING 1127 1127 Chloride 3.
 MOD_RES 1299 1299 Phosphoserine.
 CARBOHYD 38 38 N-linked (GlcNAc...) (Probable).
 CARBOHYD 54 54 N-linked (GlcNAc...).
 CARBOHYD 74 74 N-linked (GlcNAc...).
 CARBOHYD 111 111 N-linked (GlcNAc...).
 CARBOHYD 146 146 N-linked (GlcNAc...).
 CARBOHYD 160 160 N-linked (GlcNAc...) (Potential).
 CARBOHYD 318 318 N-linked (GlcNAc...).
 CARBOHYD 445 445 N-linked (GlcNAc...).
 CARBOHYD 509 509 N-linked (GlcNAc...).
 CARBOHYD 677 677 N-linked (GlcNAc...) (Potential).
 CARBOHYD 695 695 N-linked (GlcNAc...) (complex).
 CARBOHYD 714 714 N-linked (GlcNAc...) (complex).
 CARBOHYD 760 760 N-linked (GlcNAc...); partial.
 CARBOHYD 942 942 N-linked (GlcNAc...); partial.
 CARBOHYD 1191 1191 N-linked (GlcNAc...); partial.
 DISULFID 157 165
 DISULFID 757 763
 DISULFID 957 975
 DISULFID 1143 1155  
Keyword
 3D-structure; Alternative splicing; Carboxypeptidase; Cell membrane; Complete proteome; Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase; Membrane; Metal-binding; Metalloprotease; Phosphoprotein; Polymorphism; Protease; Reference proteome; Repeat; Secreted; Signal; Transmembrane; Transmembrane helix; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1306 AA 
Protein Sequence
MGAASGRRGP GLLLPLPLLL LLPPQPALAL DPGLQPGNFS ADEAGAQLFA QSYNSSAEQV 60
LFQSVAASWA HDTNITAENA RRQEEAALLS QEFAEAWGQK AKELYEPIWQ NFTDPQLRRI 120
IGAVRTLGSA NLPLAKRQQY NALLSNMSRI YSTAKVCLPN KTATCWSLDP DLTNILASSR 180
SYAMLLFAWE GWHNAAGIPL KPLYEDFTAL SNEAYKQDGF TDTGAYWRSW YNSPTFEDDL 240
EHLYQQLEPL YLNLHAFVRR ALHRRYGDRY INLRGPIPAH LLGDMWAQSW ENIYDMVVPF 300
PDKPNLDVTS TMLQQGWNAT HMFRVAEEFF TSLELSPMPP EFWEGSMLEK PADGREVVCH 360
ASAWDFYNRK DFRIKQCTRV TMDQLSTVHH EMGHIQYYLQ YKDLPVSLRR GANPGFHEAI 420
GDVLALSVST PEHLHKIGLL DRVTNDTESD INYLLKMALE KIAFLPFGYL VDQWRWGVFS 480
GRTPPSRYNF DWWYLRTKYQ GICPPVTRNE THFDAGAKFH VPNVTPYIRY FVSFVLQFQF 540
HEALCKEAGY EGPLHQCDIY RSTKAGAKLR KVLQAGSSRP WQEVLKDMVG LDALDAQPLL 600
KYFQPVTQWL QEQNQQNGEV LGWPEYQWHP PLPDNYPEGI DLVTDEAEAS KFVEEYDRTS 660
QVVWNEYAEA NWNYNTNITT ETSKILLQKN MQIANHTLKY GTQARKFDVN QLQNTTIKRI 720
IKKVQDLERA ALPAQELEEY NKILLDMETT YSVATVCHPN GSCLQLEPDL TNVMATSRKY 780
EDLLWAWEGW RDKAGRAILQ FYPKYVELIN QAARLNGYVD AGDSWRSMYE TPSLEQDLER 840
LFQELQPLYL NLHAYVRRAL HRHYGAQHIN LEGPIPAHLL GNMWAQTWSN IYDLVVPFPS 900
APSMDTTEAM LKQGWTPRRM FKEADDFFTS LGLLPVPPEF WNKSMLEKPT DGREVVCHAS 960
AWDFYNGKDF RIKQCTTVNL EDLVVAHHEM GHIQYFMQYK DLPVALREGA NPGFHEAIGD 1020
VLALSVSTPK HLHSLNLLSS EGGSDEHDIN FLMKMALDKI AFIPFSYLVD QWRWRVFDGS 1080
ITKENYNQEW WSLRLKYQGL CPPVPRTQGD FDPGAKFHIP SSVPYIRYFV SFIIQFQFHE 1140
ALCQAAGHTG PLHKCDIYQS KEAGQRLATA MKLGFSRPWP EAMQLITGQP NMSASAMLSY 1200
FKPLLDWLRT ENELHGEKLG WPQYNWTPNS ARSEGPLPDS GRVSFLGLDL DAQQARVGQW 1260
LLLFLGIALL VATLGLSQRL FSIRHRSLHR HSHGPQFGSE VELRHS 1306 
Gene Ontology
 GO:0005768; C:endosome; IDA:BHF-UCL.
 GO:0009897; C:external side of plasma membrane; IDA:BHF-UCL.
 GO:0005615; C:extracellular space; IDA:UniProtKB.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005886; C:plasma membrane; IDA:UniProtKB.
 GO:0003779; F:actin binding; IDA:UniProtKB.
 GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
 GO:0031404; F:chloride ion binding; IDA:BHF-UCL.
 GO:0008144; F:drug binding; IDA:BHF-UCL.
 GO:0004175; F:endopeptidase activity; IDA:UniProtKB.
 GO:0008237; F:metallopeptidase activity; IDA:UniProtKB.
 GO:0008241; F:peptidyl-dipeptidase activity; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IDA:BHF-UCL.
 GO:0002005; P:angiotensin catabolic process in blood; IC:UniProtKB.
 GO:0002003; P:angiotensin maturation; TAS:Reactome.
 GO:0050482; P:arachidonic acid secretion; IDA:BHF-UCL.
 GO:0001974; P:blood vessel remodeling; IC:BHF-UCL.
 GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
 GO:0060218; P:hematopoietic stem cell differentiation; IC:BHF-UCL.
 GO:0042447; P:hormone catabolic process; IDA:BHF-UCL.
 GO:0001822; P:kidney development; IMP:BHF-UCL.
 GO:0032943; P:mononuclear cell proliferation; IC:BHF-UCL.
 GO:0043171; P:peptide catabolic process; IDA:BHF-UCL.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
 GO:0002019; P:regulation of renal output by angiotensin; IC:BHF-UCL.
 GO:0014910; P:regulation of smooth muscle cell migration; ISS:BHF-UCL.
 GO:0019229; P:regulation of vasoconstriction; IC:UniProtKB.
 GO:0042312; P:regulation of vasodilation; IC:BHF-UCL. 
Interpro
 IPR001548; Peptidase_M2. 
Pfam
 PF01401; Peptidase_M2 
SMART
  
PROSITE
 PS00142; ZINC_PROTEASE 
PRINTS
 PR00791; PEPDIPTASEA.