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Q9GLN7

- ACE_PANTR

UniProt

Q9GLN7 - ACE_PANTR

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Protein

Angiotensin-converting enzyme

Gene

ACE

Organism
Pan troglodytes (Chimpanzee)
Status
Reviewed - 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

Binds 2 zinc ions per subunit. Isoform Testis-specific only binds 1 zinc ion per subunit (By similarity).By similarity
Binds 3 chloride ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei229 – 2291Chloride 1By similarity
Metal bindingi388 – 3881Zinc 1; catalyticBy similarity
Active sitei389 – 38911PROSITE-ProRule annotation
Metal bindingi392 – 3921Zinc 1; catalyticBy similarity
Metal bindingi416 – 4161Zinc 1; catalyticBy similarity
Binding sitei527 – 5271Chloride 1By similarity
Binding sitei789 – 7891Chloride 2By similarity
Binding sitei827 – 8271Chloride 3By similarity
Metal bindingi986 – 9861Zinc 2; catalyticBy similarity
Active sitei987 – 98712PROSITE-ProRule annotation
Metal bindingi990 – 9901Zinc 2; catalyticBy similarity
Metal bindingi1014 – 10141Zinc 2; catalyticBy similarity
Binding sitei1088 – 10881Chloride 2By similarity
Binding sitei1092 – 10921Chloride 2By similarity
Binding sitei1125 – 11251Chloride 3By similarity

GO - Molecular functioni

  1. carboxypeptidase activity Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. metallopeptidase activity Source: UniProtKB-KW
  4. peptidyl-dipeptidase activity Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM02.005.

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
ProteomesiUP000002277: Unplaced

Subcellular locationi

Cell membrane By similarity; Single-pass type I membrane protein By similarity. Cytoplasm By similarity
Note: Detected in both cell membrane and cytoplasm in neurons.By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. extracellular region Source: UniProtKB-KW
  3. integral component of membrane Source: UniProtKB-KW
  4. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727By similarityAdd
BLAST
Chaini28 – 13041277Angiotensin-converting enzymePRO_0000028545Add
BLAST
Chaini28 – 12301203Angiotensin-converting enzyme, soluble formPRO_0000028546Add
BLAST
Propeptidei1231 – 130474Removed in secreted formBy similarityPRO_0000028547Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi36 – 361N-linked (GlcNAc...)Sequence Analysis
Glycosylationi52 – 521N-linked (GlcNAc...)Sequence Analysis
Glycosylationi72 – 721N-linked (GlcNAc...)Sequence Analysis
Glycosylationi109 – 1091N-linked (GlcNAc...)Sequence Analysis
Glycosylationi144 – 1441N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi155 ↔ 163By similarity
Glycosylationi158 – 1581N-linked (GlcNAc...)Sequence Analysis
Glycosylationi316 – 3161N-linked (GlcNAc...)Sequence Analysis
Glycosylationi440 – 4401N-linked (GlcNAc...)Sequence Analysis
Glycosylationi443 – 4431N-linked (GlcNAc...)Sequence Analysis
Glycosylationi507 – 5071N-linked (GlcNAc...)Sequence Analysis
Glycosylationi675 – 6751N-linked (GlcNAc...)Sequence Analysis
Glycosylationi693 – 6931N-linked (GlcNAc...) (complex)By similarity
Glycosylationi712 – 7121N-linked (GlcNAc...) (complex)By similarity
Disulfide bondi755 ↔ 761By similarity
Glycosylationi758 – 7581N-linked (GlcNAc...)Sequence Analysis
Glycosylationi940 – 9401N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi955 ↔ 973By similarity
Disulfide bondi1141 ↔ 1153By similarity
Glycosylationi1189 – 11891N-linked (GlcNAc...)Sequence Analysis
Modified residuei1297 – 12971PhosphoserineBy similarity

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Interactioni

Protein-protein interaction databases

STRINGi9598.ENSPTRP00000038991.

Structurei

3D structure databases

ProteinModelPortaliQ9GLN7.
SMRiQ9GLN7. Positions 28-639, 643-1226.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini28 – 12571230ExtracellularSequence AnalysisAdd
BLAST
Topological domaini1275 – 130430CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei1258 – 127417HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni28 – 628601Peptidase M2 1Add
BLAST
Regioni629 – 1230602Peptidase M2 2Add
BLAST

Sequence similaritiesi

Belongs to the peptidase M2 family.Curated

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG71044.
HOVERGENiHBG000264.
InParanoidiQ9GLN7.
KOiK01283.

Family and domain databases

InterProiIPR001548. Peptidase_M2.
[Graphical view]
PANTHERiPTHR10514. PTHR10514. 1 hit.
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. Align

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)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 572572Missing in isoform Testis-specific. CuratedVSP_037640Add
BLAST
Alternative sequencei573 – 63967AGSSR…PEGID → MGQGWATAGLPSLLFLLLCY GHPLLVPSQEAPRQVTVTHG TSSQATTSGQTTTHQATAHQ TSAQSPN in isoform Testis-specific. CuratedVSP_037641Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
RefSeqiNP_001008995.1. NM_001008995.2. [Q9GLN7-1]
UniGeneiPtr.6266.

Genome annotation databases

GeneIDi449567.
KEGGiptr:449567.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
RefSeqi NP_001008995.1. NM_001008995.2. [Q9GLN7-1 ]
UniGenei Ptr.6266.

3D structure databases

ProteinModelPortali Q9GLN7.
SMRi Q9GLN7. Positions 28-639, 643-1226.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9598.ENSPTRP00000038991.

Protein family/group databases

MEROPSi M02.005.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 449567.
KEGGi ptr:449567.

Organism-specific databases

CTDi 1636.

Phylogenomic databases

eggNOGi NOG71044.
HOVERGENi HBG000264.
InParanoidi Q9GLN7.
KOi K01283.

Miscellaneous databases

NextBioi 20832682.

Family and domain databases

InterProi IPR001548. Peptidase_M2.
[Graphical view ]
PANTHERi PTHR10514. PTHR10514. 1 hit.
Pfami PF01401. Peptidase_M2. 2 hits.
[Graphical view ]
PRINTSi PR00791. PEPDIPTASEA.
PROSITEi PS00142. ZINC_PROTEASE. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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].

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: October 29, 2014
This is version 74 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

External Data

Dasty 3