Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9GLN7 (ACE_PANTR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Angiotensin-converting enzyme

Short name=ACE
EC=3.2.1.-
EC=3.4.15.1
Alternative name(s):
Dipeptidyl carboxypeptidase I
Kininase II
CD_antigen=CD143

Cleaved into the following chain:

  1. Angiotensin-converting enzyme, soluble form
Gene names
Name:ACE
Synonyms:DCP1
OrganismPan troglodytes (Chimpanzee) [Reference proteome]
Taxonomic identifier9598 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePan

Protein attributes

Sequence length1304 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 By similarity.

Catalytic activity

Release of a C-terminal dipeptide, oligopeptide-|-Xaa-Yaa, when Xaa is not Pro, and Yaa is neither Asp nor Glu. Thus, conversion of angiotensin I to angiotensin II, with increase in vasoconstrictor activity, but no action on angiotensin II.

Cofactor

Binds 2 zinc ions per subunit. Isoform Testis-specific only binds 1 zinc ion per subunit By similarity.

Binds 3 chloride ions per subunit By similarity.

Subcellular location

Angiotensin-converting enzyme, soluble form: Secreted By similarity.

Cell membrane; Single-pass type I membrane protein By similarity.

Post-translational modification

Phosphorylated by CK2 on Ser-1297; which allows membrane retention By similarity.

Sequence similarities

Belongs to the peptidase M2 family.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Somatic (identifier: Q9GLN7-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform Testis-specific (identifier: Q9GLN7-2)

Also known as: ACE-T;

The sequence of this isoform differs from the canonical sequence as follows:
     1-572: Missing.
     573-639: AGSSRPWQEV...LPDNYPEGID → MGQGWATAGL...AHQTSAQSPN

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 By similarity
Chain28 – 13041277Angiotensin-converting enzyme
PRO_0000028545
Chain28 – 12301203Angiotensin-converting enzyme, soluble form
PRO_0000028546
Propeptide1231 – 130474Removed in secreted form By similarity
PRO_0000028547

Regions

Topological domain28 – 12571230Extracellular Potential
Transmembrane1258 – 127417Helical; Potential
Topological domain1275 – 130430Cytoplasmic Potential
Region28 – 628601Peptidase M2 1
Region629 – 1230602Peptidase M2 2

Sites

Active site38911 By similarity
Active site98712 By similarity
Metal binding3881Zinc 1; catalytic By similarity
Metal binding3921Zinc 1; catalytic By similarity
Metal binding4161Zinc 1; catalytic By similarity
Metal binding9861Zinc 2; catalytic By similarity
Metal binding9901Zinc 2; catalytic By similarity
Metal binding10141Zinc 2; catalytic By similarity
Binding site2291Chloride 1 By similarity
Binding site5271Chloride 1 By similarity
Binding site7891Chloride 2 By similarity
Binding site8271Chloride 3 By similarity
Binding site10881Chloride 2 By similarity
Binding site10921Chloride 2 By similarity
Binding site11251Chloride 3 By similarity

Amino acid modifications

Modified residue12971Phosphoserine By similarity
Glycosylation361N-linked (GlcNAc...) Potential
Glycosylation521N-linked (GlcNAc...) Potential
Glycosylation721N-linked (GlcNAc...) Potential
Glycosylation1091N-linked (GlcNAc...) Potential
Glycosylation1441N-linked (GlcNAc...) Potential
Glycosylation1581N-linked (GlcNAc...) Potential
Glycosylation3161N-linked (GlcNAc...) Potential
Glycosylation4401N-linked (GlcNAc...) Potential
Glycosylation4431N-linked (GlcNAc...) Potential
Glycosylation5071N-linked (GlcNAc...) Potential
Glycosylation6751N-linked (GlcNAc...) Potential
Glycosylation6931N-linked (GlcNAc...) (complex) By similarity
Glycosylation7121N-linked (GlcNAc...) (complex) By similarity
Glycosylation7581N-linked (GlcNAc...) Potential
Glycosylation9401N-linked (GlcNAc...) Potential
Glycosylation11891N-linked (GlcNAc...) Potential
Disulfide bond155 ↔ 163 By similarity
Disulfide bond755 ↔ 761 By similarity
Disulfide bond955 ↔ 973 By similarity
Disulfide bond1141 ↔ 1153 By similarity

Natural variations

Alternative sequence1 – 572572Missing in isoform Testis-specific.
VSP_037640
Alternative sequence573 – 63967AGSSR…PEGID → MGQGWATAGLPSLLFLLLCY GHPLLVPSQEAPRQVTVTHG TSSQATTSGQTTTHQATAHQ TSAQSPN in isoform Testis-specific.
VSP_037641

Sequences

Sequence LengthMass (Da)Tools
Isoform Somatic [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: DCF728D0BA0F1314

FASTA1,304149,370
        10         20         30         40         50         60 
MGAASGRRGP GLLLPLLLLL PPQPALALDP GLQPGNFSAD EAGAQLFAQS YNSSAEQVLF 

        70         80         90        100        110        120 
QSVAASWAHD TNITAENARR QEEAALLSQE FAEAWGQKAK ELYEPVWQNF TDPQLRRIIG 

       130        140        150        160        170        180 
AVRTLGSANL PLAKRQQYNA LLSNMSRIYS TAKVCLPNKT ATCWSLDPDL TNILASSRSY 

       190        200        210        220        230        240 
AMLLFAWEGW HNAAGIPLKP LYEDFTALSN EAYKQDGFTD TGAYWRSWYN SPTFEDDLEH 

       250        260        270        280        290        300 
LYQQLEPLYL NLHAFVRRAL HRRYGDRYIN LRGPIPAHLL GDMWAQSWEN IYDMVVPFPD 

       310        320        330        340        350        360 
KPNLDVTSTM LQQGWNATHM FRVAEEFFTS LELSPMPPEF WEGSMLEKPA DGREVVCHAS 

       370        380        390        400        410        420 
AWDFYNRKDF RIKQCTRVTM DQLSTVHHEM GHIQYYLQYK DLPVSLRGGA NPGFHEAIGD 

       430        440        450        460        470        480 
VLALSVSTPA HLHKIGLLDN VTNDTESDIN YLLKMALEKI AFLPFGYLVD QWRWGVFSGR 

       490        500        510        520        530        540 
TPNSRYNFDW WYLRTKYQGI CPPVTRNETH FDAGAKFHVP NVTPYIRYFV SFVLQFQFHE 

       550        560        570        580        590        600 
ALCKEAGYEG PLHQCDIYQS TKAGAKLRKV LQAGSSRPWQ EVLKDMVGLD ALDAQPLLKY 

       610        620        630        640        650        660 
FQPVTQWLQE QNQQNGEVLG WPEYQWHPPL PDNYPEGIDL VTDEAEASKF VEEYDRTSQV 

       670        680        690        700        710        720 
VWNEYAEANW NYNTNITTET SKILLQKNMQ IANHTLKYGT QARRFDVNQL QNTTIKRIIK 

       730        740        750        760        770        780 
KVQDLERAAL PAQELEEYNK ILLDMETTYS VATVCHTNGS CLQLEPDLTN VMATSRKYED 

       790        800        810        820        830        840 
LLWAWEGWRD KAGRAILQFY PKYVELINQA ARLNGYVDAG DSWRSMYETP SLEQDLERLF 

       850        860        870        880        890        900 
QELQPLYLNL HAYVRRALHR HYGAQHINLE GPIPAHLLGN MWAQTWSNIY DLVVPFPSAP 

       910        920        930        940        950        960 
SMDTTEAMLK QGWTPRRMFK EADDFFTSLG LLPVPPEFWN KSMLEKPTDG REVVCHASAW 

       970        980        990       1000       1010       1020 
DFYNGKDFRI KQCTTVNLED LVVAHHEMGH IQYFMQYKDL PVALREGANP GFHEAIGDVL 

      1030       1040       1050       1060       1070       1080 
ALSVSTPKHL HSLNLLSSEG GSDEHDINFL MKMALDKIAF IPFSYLVDQW RWRVFDGSIT 

      1090       1100       1110       1120       1130       1140 
KENYNQEWWS LRLKYQGLCP PVPRTQGDFD PGAKFHIPSS VPYIRYFVSF IIQFQFHEAL 

      1150       1160       1170       1180       1190       1200 
CQAAGHTGPL HKCDIYQSKE AGQRLATAMK LGFSRPWPEA MQLITGQPNM SASAMLSYFK 

      1210       1220       1230       1240       1250       1260 
PLLDWLRTEN ELHGEKLGWP QYNWTPNSAR SEGPLPDSGR VSFLGLDLDA QQARVGQWLL 

      1270       1280       1290       1300 
LFLGIALLVA TLGLSQRLFS IRHRSLHRHS HGPQFDSEVE LRHS 

« Hide

Isoform Testis-specific (ACE-T) [UniParc] [UniParc].

Checksum: C43D06443A47E74B
Show »

FASTA73283,429

References

[1]"Human-chimpanzee DNA sequence variation in the four major genes of the renin angiotensin system."
Dufour C., Casane D., Denton D., Wickings J., Corvol P., Jeunemaitre X.
Genomics 69:14-26(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF193486 expand/collapse EMBL AC list , AF193462, AF193464, AF193463, AF193465, AF193467, AF193469, AF193471, AF193473, AF193482, AF193481, AF193480, AF193479, AF193478, AF193477, AF193476, AF193475, AF193474, AF193485, AF193484, AF193483, AF193472, AF193470, AF193468, AF193466 Genomic DNA. Translation: AAG31358.1.
AF193486 expand/collapse EMBL AC list , AF193473, AF193474, AF193475, AF193476, AF193477, AF193478, AF193479, AF193480, AF193481, AF193482, AF193483, AF193484, AF193485 Genomic DNA. Translation: AAG31359.1.
RefSeqNP_001008995.1. NM_001008995.2.
UniGenePtr.6266.

3D structure databases

ProteinModelPortalQ9GLN7.
SMRQ9GLN7. Positions 28-639, 643-1226.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9598.ENSPTRP00000038991.

Protein family/group databases

MEROPSM02.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID449567.
KEGGptr:449567.

Organism-specific databases

CTD1636.

Phylogenomic databases

eggNOGNOG71044.
HOVERGENHBG000264.
KOK01283.

Family and domain databases

InterProIPR001548. Peptidase_M2.
[Graphical view]
PANTHERPTHR10514. PTHR10514. 1 hit.
PfamPF01401. Peptidase_M2. 2 hits.
[Graphical view]
PRINTSPR00791. PEPDIPTASEA.
PROSITEPS00142. ZINC_PROTEASE. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio20832682.

Entry information

Entry nameACE_PANTR
AccessionPrimary (citable) accession number: Q9GLN7
Secondary accession number(s): Q9GLN6
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: March 1, 2001
Last modified: February 19, 2014
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries