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Protein

Angiotensin-converting enzyme

Gene

ACE

Organism
Pan troglodytes (Chimpanzee)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Protein inferred from homologyi

Functioni

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).By similarity

Catalytic activityi

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.

Cofactori

Protein has several cofactor binding sites:
  • Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit. Isoform Testis-specific only binds 1 Zn2+ ion per subunit.By similarity
  • chlorideBy similarityNote: Binds 3 chloride ions per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei229Chloride 1By similarity1
Metal bindingi388Zinc 1; catalyticBy similarity1
Active sitei3891PROSITE-ProRule annotation1
Metal bindingi392Zinc 1; catalyticBy similarity1
Metal bindingi416Zinc 1; catalyticBy similarity1
Binding sitei527Chloride 1By similarity1
Binding sitei789Chloride 2By similarity1
Binding sitei827Chloride 3By similarity1
Metal bindingi986Zinc 2; catalyticBy similarity1
Active sitei9872PROSITE-ProRule annotation1
Metal bindingi990Zinc 2; catalyticBy similarity1
Metal bindingi1014Zinc 2; catalyticBy similarity1
Binding sitei1088Chloride 2By similarity1
Binding sitei1092Chloride 2By similarity1
Binding sitei1125Chloride 3By similarity1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Angiotensin-converting enzyme (EC:3.2.1.-, EC:3.4.15.1)
Short name:
ACE
Alternative name(s):
Dipeptidyl carboxypeptidase I
Kininase II
CD_antigen: CD143
Cleaved into the following chain:
Gene namesi
Name:ACE
Synonyms:DCP1
OrganismiPan troglodytes (Chimpanzee)
Taxonomic identifieri9598 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePan
Proteomesi
  • UP000002277 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini28 – 1257ExtracellularSequence analysisAdd BLAST1230
Transmembranei1258 – 1274HelicalSequence analysisAdd BLAST17
Topological domaini1275 – 1304CytoplasmicSequence analysisAdd BLAST30

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 27By similarityAdd BLAST27
ChainiPRO_000002854528 – 1304Angiotensin-converting enzymeAdd BLAST1277
ChainiPRO_000002854628 – 1230Angiotensin-converting enzyme, soluble formAdd BLAST1203
PropeptideiPRO_00000285471231 – 1304Removed in secreted formBy similarityAdd BLAST74

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi36N-linked (GlcNAc...)Sequence analysis1
Glycosylationi52N-linked (GlcNAc...)Sequence analysis1
Glycosylationi72N-linked (GlcNAc...)Sequence analysis1
Glycosylationi109N-linked (GlcNAc...)Sequence analysis1
Glycosylationi144N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi155 ↔ 163By similarity
Glycosylationi158N-linked (GlcNAc...)Sequence analysis1
Glycosylationi316N-linked (GlcNAc...)Sequence analysis1
Glycosylationi440N-linked (GlcNAc...)Sequence analysis1
Glycosylationi443N-linked (GlcNAc...)Sequence analysis1
Glycosylationi507N-linked (GlcNAc...)Sequence analysis1
Glycosylationi675N-linked (GlcNAc...)Sequence analysis1
Glycosylationi693N-linked (GlcNAc...) (complex)By similarity1
Glycosylationi712N-linked (GlcNAc...) (complex)By similarity1
Disulfide bondi755 ↔ 761By similarity
Glycosylationi758N-linked (GlcNAc...)Sequence analysis1
Glycosylationi940N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi955 ↔ 973By similarity
Disulfide bondi1141 ↔ 1153By similarity
Glycosylationi1189N-linked (GlcNAc...)Sequence analysis1
Modified residuei1297PhosphoserineBy similarity1

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PRIDEiQ9GLN7.

Structurei

3D structure databases

ProteinModelPortaliQ9GLN7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni28 – 628Peptidase M2 1Add BLAST601
Regioni629 – 1230Peptidase M2 2Add BLAST602

Sequence similaritiesi

Belongs to the peptidase M2 family.Curated

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG000264.
InParanoidiQ9GLN7.
KOiK01283.

Family and domain databases

CDDicd06461. M2_ACE. 2 hits.
InterProiIPR001548. Peptidase_M2.
[Graphical view]
PfamiPF01401. Peptidase_M2. 2 hits.
[Graphical view]
PRINTSiPR00791. PEPDIPTASEA.
PROSITEiPS00142. ZINC_PROTEASE. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Somatic (identifier: Q9GLN7-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MGAASGRRGP GLLLPLLLLL PPQPALALDP GLQPGNFSAD EAGAQLFAQS
60 70 80 90 100
YNSSAEQVLF QSVAASWAHD TNITAENARR QEEAALLSQE FAEAWGQKAK
110 120 130 140 150
ELYEPVWQNF TDPQLRRIIG AVRTLGSANL PLAKRQQYNA LLSNMSRIYS
160 170 180 190 200
TAKVCLPNKT ATCWSLDPDL TNILASSRSY AMLLFAWEGW HNAAGIPLKP
210 220 230 240 250
LYEDFTALSN EAYKQDGFTD TGAYWRSWYN SPTFEDDLEH LYQQLEPLYL
260 270 280 290 300
NLHAFVRRAL HRRYGDRYIN LRGPIPAHLL GDMWAQSWEN IYDMVVPFPD
310 320 330 340 350
KPNLDVTSTM LQQGWNATHM FRVAEEFFTS LELSPMPPEF WEGSMLEKPA
360 370 380 390 400
DGREVVCHAS AWDFYNRKDF RIKQCTRVTM DQLSTVHHEM GHIQYYLQYK
410 420 430 440 450
DLPVSLRGGA NPGFHEAIGD VLALSVSTPA HLHKIGLLDN VTNDTESDIN
460 470 480 490 500
YLLKMALEKI AFLPFGYLVD QWRWGVFSGR TPNSRYNFDW WYLRTKYQGI
510 520 530 540 550
CPPVTRNETH FDAGAKFHVP NVTPYIRYFV SFVLQFQFHE ALCKEAGYEG
560 570 580 590 600
PLHQCDIYQS TKAGAKLRKV LQAGSSRPWQ EVLKDMVGLD ALDAQPLLKY
610 620 630 640 650
FQPVTQWLQE QNQQNGEVLG WPEYQWHPPL PDNYPEGIDL VTDEAEASKF
660 670 680 690 700
VEEYDRTSQV VWNEYAEANW NYNTNITTET SKILLQKNMQ IANHTLKYGT
710 720 730 740 750
QARRFDVNQL QNTTIKRIIK KVQDLERAAL PAQELEEYNK ILLDMETTYS
760 770 780 790 800
VATVCHTNGS CLQLEPDLTN VMATSRKYED LLWAWEGWRD KAGRAILQFY
810 820 830 840 850
PKYVELINQA ARLNGYVDAG DSWRSMYETP SLEQDLERLF QELQPLYLNL
860 870 880 890 900
HAYVRRALHR HYGAQHINLE GPIPAHLLGN MWAQTWSNIY DLVVPFPSAP
910 920 930 940 950
SMDTTEAMLK QGWTPRRMFK EADDFFTSLG LLPVPPEFWN KSMLEKPTDG
960 970 980 990 1000
REVVCHASAW DFYNGKDFRI KQCTTVNLED LVVAHHEMGH IQYFMQYKDL
1010 1020 1030 1040 1050
PVALREGANP GFHEAIGDVL ALSVSTPKHL HSLNLLSSEG GSDEHDINFL
1060 1070 1080 1090 1100
MKMALDKIAF IPFSYLVDQW RWRVFDGSIT KENYNQEWWS LRLKYQGLCP
1110 1120 1130 1140 1150
PVPRTQGDFD PGAKFHIPSS VPYIRYFVSF IIQFQFHEAL CQAAGHTGPL
1160 1170 1180 1190 1200
HKCDIYQSKE AGQRLATAMK LGFSRPWPEA MQLITGQPNM SASAMLSYFK
1210 1220 1230 1240 1250
PLLDWLRTEN ELHGEKLGWP QYNWTPNSAR SEGPLPDSGR VSFLGLDLDA
1260 1270 1280 1290 1300
QQARVGQWLL LFLGIALLVA TLGLSQRLFS IRHRSLHRHS HGPQFDSEVE

LRHS
Length:1,304
Mass (Da):149,370
Last modified:March 1, 2001 - v1
Checksum:iDCF728D0BA0F1314
GO
Isoform Testis-specific (identifier: Q9GLN7-2) [UniParc] [UniParc]FASTAAdd to basket
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

Show »
Length:732
Mass (Da):83,429
Checksum:iC43D06443A47E74B
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0376401 – 572Missing in isoform Testis-specific. CuratedAdd BLAST572
Alternative sequenceiVSP_037641573 – 639AGSSR…PEGID → MGQGWATAGLPSLLFLLLCY GHPLLVPSQEAPRQVTVTHG TSSQATTSGQTTTHQATAHQ TSAQSPN in isoform Testis-specific. CuratedAdd BLAST67

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF193486
, 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
, AF193473, AF193474, AF193475, AF193476, AF193477, AF193478, AF193479, AF193480, AF193481, AF193482, AF193483, AF193484, AF193485 Genomic DNA. Translation: AAG31359.1.
RefSeqiXP_016785980.1. XM_016930491.1. [Q9GLN7-2]

Genome annotation databases

GeneIDi449567.
KEGGiptr:449567.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF193486
, 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
, AF193473, AF193474, AF193475, AF193476, AF193477, AF193478, AF193479, AF193480, AF193481, AF193482, AF193483, AF193484, AF193485 Genomic DNA. Translation: AAG31359.1.
RefSeqiXP_016785980.1. XM_016930491.1. [Q9GLN7-2]

3D structure databases

ProteinModelPortaliQ9GLN7.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ9GLN7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi449567.
KEGGiptr:449567.

Organism-specific databases

CTDi1636.

Phylogenomic databases

HOVERGENiHBG000264.
InParanoidiQ9GLN7.
KOiK01283.

Family and domain databases

CDDicd06461. M2_ACE. 2 hits.
InterProiIPR001548. Peptidase_M2.
[Graphical view]
PfamiPF01401. Peptidase_M2. 2 hits.
[Graphical view]
PRINTSiPR00791. PEPDIPTASEA.
PROSITEiPS00142. ZINC_PROTEASE. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiACE_PANTR
AccessioniPrimary (citable) accession number: Q9GLN7
Secondary accession number(s): Q9GLN6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: March 1, 2001
Last modified: November 30, 2016
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.