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Protein

Angiotensin-converting enzyme

Gene

Ace

Organism
Mesocricetus auratus (Golden hamster)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

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. This GPIase activity seems to be crucial for the egg-binding ability of the sperm (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.By similarity
  • chlorideBy similarityNote: Binds 3 chloride ions per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei237Chloride 1By similarity1
Metal bindingi396Zinc 1; catalyticBy similarity1
Active sitei3971PROSITE-ProRule annotation1
Metal bindingi400Zinc 1; catalyticBy similarity1
Metal bindingi424Zinc 1; catalyticBy similarity1
Binding sitei535Chloride 1By similarity1
Binding sitei797Chloride 2By similarity1
Binding sitei835Chloride 3By similarity1
Metal bindingi994Zinc 2; catalyticBy similarity1
Active sitei9952PROSITE-ProRule annotation1
Metal bindingi998Zinc 2; catalyticBy similarity1
Metal bindingi1022Zinc 2; catalyticBy similarity1
Binding sitei1096Chloride 2By similarity1
Binding sitei1100Chloride 2By similarity1
Binding sitei1133Chloride 3By similarity1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.15.1. 3239.

Protein family/group databases

MEROPSiM02.001.

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
OrganismiMesocricetus auratus (Golden hamster)
Taxonomic identifieri10036 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeMesocricetus

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini36 – 1265ExtracellularSequence analysisAdd BLAST1230
Transmembranei1266 – 1282HelicalSequence analysisAdd BLAST17
Topological domaini1283 – 1314CytoplasmicSequence analysisAdd BLAST32

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 – 35By similarityAdd BLAST35
ChainiPRO_000002853636 – 1314Angiotensin-converting enzymeAdd BLAST1279
ChainiPRO_000002853736 – 1238Angiotensin-converting enzyme, soluble formAdd BLAST1203
PropeptideiPRO_00000285381239 – 1314Removed in secreted formBy similarityAdd BLAST76

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi44N-linked (GlcNAc...)Sequence analysis1
Glycosylationi60N-linked (GlcNAc...)Sequence analysis1
Glycosylationi80N-linked (GlcNAc...)Sequence analysis1
Glycosylationi117N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi163 ↔ 171By similarity
Glycosylationi166N-linked (GlcNAc...)Sequence analysis1
Glycosylationi324N-linked (GlcNAc...)Sequence analysis1
Glycosylationi515N-linked (GlcNAc...)Sequence analysis1
Glycosylationi683N-linked (GlcNAc...)Sequence analysis1
Glycosylationi701N-linked (GlcNAc...)Sequence analysis1
Glycosylationi720N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi763 ↔ 769By similarity
Glycosylationi766N-linked (GlcNAc...)Sequence analysis1
Glycosylationi948N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi963 ↔ 981By similarity
Disulfide bondi1149 ↔ 1161By similarity
Glycosylationi1197N-linked (GlcNAc...)Sequence analysis1
Modified residuei1307PhosphoserineBy similarity1

Post-translational modificationi

Phosphorylated by CK2 on Ser-1307; which allows membrane retention.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PRIDEiQ50JE5.

Expressioni

Tissue specificityi

Widely expressed with dominant expression in lung and kidney.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ50JE5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni36 – 636Peptidase M2 1Add BLAST601
Regioni637 – 1238Peptidase M2 2Add BLAST602

Sequence similaritiesi

Belongs to the peptidase M2 family.Curated

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG000264.
OrthoDBiEOG091G033S.

Family and domain databases

CDDicd06461. M2_ACE. 2 hits.
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. AlignAdd to basket

Isoform Somatic (identifier: Q50JE5-1) [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
MGAASGQRGQ GPPSPLLLLW LSLLLLLLPP SPAPALDPGL QPGNFSADEI
60 70 80 90 100
GAHLFAESYN SSAEQVIFQS TVASWAYDTN MTEENARLQE EAELIWQEFA
110 120 130 140 150
EVWGKKAKEL FDAIRQNFTD SKLRRVIETI RTLGPANLPL ARRQQYNSLQ
160 170 180 190 200
NNMNRIYSTS KVCLPNKTAT CWSLEPELTN ILASSRSYAK LLFAWESWHD
210 220 230 240 250
VVGIPLKPLY QDFTALSNEA YKQDGFSDTG AYWRSAYDSP SFEETLEHLY
260 270 280 290 300
HQLEPLYLNL HAYVRRALHR RYGDKYINLR GPIPAHLLGD MWAQSWDNIY
310 320 330 340 350
DMVVPFPNKP NLDVTNTMVQ KGWNVTHMFR VAEEFFTSMG LSPMPPEFWA
360 370 380 390 400
ESMLEKPTDG REVVCHASAW DFFNRKDFRI KQCTRITMEQ LSTVHHEMGH
410 420 430 440 450
VQYYLQYKDL TVPLRRGANP GFHEAIGDVL ALSVSTPAHL HKIGLLDRVA
460 470 480 490 500
NDLESDINYL LKMALEKIAF LPFGYLVDQW RWGVFSGHTP PSRYNFDWWY
510 520 530 540 550
FRTKYQGICP PVVRNETHFD AGAKFHIPSG TPYIRYFVSF ILQFQFHQAL
560 570 580 590 600
CKEAGHQGPL HQCDIYQSTQ AGAKLQRVLQ AGYSRPWQEV LKEMVGSDTL
610 620 630 640 650
DAQALLEYFQ PVIRWLQEQN QRNGEVLGWP EYQWRPPLPD NYPEGIDLVT
660 670 680 690 700
DETEAERFVE EYDRTARVLW NEYAEANWQY NTNITLEASK ILLQKNKKVA
710 720 730 740 750
NHTLKYGTLA KKFDVSNFQN YTIKRIIKKV QNMDRAVLPP KELEEYNQIL
760 770 780 790 800
MDMETTYSIA NVCYLNGTCL HLEPDLTNVM ATSRKYEELL WVWKSWRDKV
810 820 830 840 850
GRAILPLFPK YVELSNKIAH LNGYADGGDS WRSSYESKSL EQDLEQLYQE
860 870 880 890 900
LQPLYLNLHA YVRRSLHRHY GSQHINLDGP IPAHLLGNMW AQTWSNIYDL
910 920 930 940 950
VAPFPSAPNL DATEAMIKQG WTPRRIFKEA DDFFTSLGLL PVSEEFWNKS
960 970 980 990 1000
MLEKPGDGRE VVCHASAWDF YNGKDFRIKQ CTSVNMEDLV IAHHEMGHIQ
1010 1020 1030 1040 1050
YFMQYKDLPV TFREGANPGF HEAIGDVLAL SVSTPKHLHS LNLLSSEGGG
1060 1070 1080 1090 1100
YEHDINFLMK MALDKIAFIP FSYLIDQWRW RVFDGSITKE NYNQEWWSLR
1110 1120 1130 1140 1150
LKYQGLCPPV PRSQDDFDPG SKFHVPANVP YIRYFVSFII QFQFHEALCR
1160 1170 1180 1190 1200
AAGHTGPLHK CDIYQSKEAG KLLADTMKMG YSKPWPEAMK LITGQPNMSA
1210 1220 1230 1240 1250
SAMMNYFKPL TEWLVTENRR HGETLGWPEY NWTPNTARSE GPFPESGRVN
1260 1270 1280 1290 1300
FLGMYLEPQQ ARVGQWVLLF LGVSLLVATL GLTHRLFSIR QHGHSLHRPH
1310
RGPQFGSEVE LRHS
Length:1,314
Mass (Da):151,595
Last modified:June 7, 2005 - v1
Checksum:i74E29238E87F157E
GO
Isoform Testis-specific (identifier: Q50JE5-2)
Also known as: ACE-T
Sequence is not available
Length:
Mass (Da):

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB212958 mRNA. Translation: BAD98304.1.
RefSeqiNP_001268510.1. NM_001281581.1. [Q50JE5-1]

Genome annotation databases

GeneIDi101824864.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB212958 mRNA. Translation: BAD98304.1.
RefSeqiNP_001268510.1. NM_001281581.1. [Q50JE5-1]

3D structure databases

ProteinModelPortaliQ50JE5.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiM02.001.

Proteomic databases

PRIDEiQ50JE5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi101824864.

Phylogenomic databases

HOVERGENiHBG000264.
OrthoDBiEOG091G033S.

Enzyme and pathway databases

BRENDAi3.4.15.1. 3239.

Family and domain databases

CDDicd06461. M2_ACE. 2 hits.
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]
ProtoNetiSearch...

Entry informationi

Entry nameiACE_MESAU
AccessioniPrimary (citable) accession number: Q50JE5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: June 7, 2005
Last modified: November 30, 2016
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.