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

Q50JE5 (ACE_MESAU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 50. 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
OrganismMesocricetus auratus (Golden hamster)
Taxonomic identifier10036 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeMesocricetus

Protein attributes

Sequence length1314 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

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. This GPIase activity seems to be crucial for the egg-binding ability of the sperm 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 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.

Tissue specificity

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

Post-translational modification

Phosphorylated by CK2 on Ser-1307; 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. [Select]
Isoform Somatic (identifier: Q50JE5-1)

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: Q50JE5-2)

Also known as: ACE-T;

The sequence of this isoform is not available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3535 By similarity
Chain36 – 13141279Angiotensin-converting enzyme
PRO_0000028536
Chain36 – 12381203Angiotensin-converting enzyme, soluble form
PRO_0000028537
Propeptide1239 – 131476Removed in secreted form By similarity
PRO_0000028538

Regions

Topological domain36 – 12651230Extracellular Potential
Transmembrane1266 – 128217Helical; Potential
Topological domain1283 – 131432Cytoplasmic Potential
Region36 – 636601Peptidase M2 1
Region637 – 1238602Peptidase M2 2

Sites

Active site39711 By similarity
Active site99512 By similarity
Metal binding3961Zinc 1; catalytic By similarity
Metal binding4001Zinc 1; catalytic By similarity
Metal binding4241Zinc 1; catalytic By similarity
Metal binding9941Zinc 2; catalytic By similarity
Metal binding9981Zinc 2; catalytic By similarity
Metal binding10221Zinc 2; catalytic By similarity
Binding site2371Chloride 1 By similarity
Binding site5351Chloride 1 By similarity
Binding site7971Chloride 2 By similarity
Binding site8351Chloride 3 By similarity
Binding site10961Chloride 2 By similarity
Binding site11001Chloride 2 By similarity
Binding site11331Chloride 3 By similarity

Amino acid modifications

Modified residue13071Phosphoserine By similarity
Glycosylation441N-linked (GlcNAc...) Potential
Glycosylation601N-linked (GlcNAc...) Potential
Glycosylation801N-linked (GlcNAc...) Potential
Glycosylation1171N-linked (GlcNAc...) Potential
Glycosylation1661N-linked (GlcNAc...) Potential
Glycosylation3241N-linked (GlcNAc...) Potential
Glycosylation5151N-linked (GlcNAc...) Potential
Glycosylation6831N-linked (GlcNAc...) Potential
Glycosylation7011N-linked (GlcNAc...) Potential
Glycosylation7201N-linked (GlcNAc...) Potential
Glycosylation7661N-linked (GlcNAc...) Potential
Glycosylation9481N-linked (GlcNAc...) Potential
Glycosylation11971N-linked (GlcNAc...) Potential
Disulfide bond163 ↔ 171 By similarity
Disulfide bond763 ↔ 769 By similarity
Disulfide bond963 ↔ 981 By similarity
Disulfide bond1149 ↔ 1161 By similarity

Sequences

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

Last modified June 7, 2005. Version 1.
Checksum: 74E29238E87F157E

FASTA1,314151,595
        10         20         30         40         50         60 
MGAASGQRGQ GPPSPLLLLW LSLLLLLLPP SPAPALDPGL QPGNFSADEI GAHLFAESYN 

        70         80         90        100        110        120 
SSAEQVIFQS TVASWAYDTN MTEENARLQE EAELIWQEFA EVWGKKAKEL FDAIRQNFTD 

       130        140        150        160        170        180 
SKLRRVIETI RTLGPANLPL ARRQQYNSLQ NNMNRIYSTS KVCLPNKTAT CWSLEPELTN 

       190        200        210        220        230        240 
ILASSRSYAK LLFAWESWHD VVGIPLKPLY QDFTALSNEA YKQDGFSDTG AYWRSAYDSP 

       250        260        270        280        290        300 
SFEETLEHLY HQLEPLYLNL HAYVRRALHR RYGDKYINLR GPIPAHLLGD MWAQSWDNIY 

       310        320        330        340        350        360 
DMVVPFPNKP NLDVTNTMVQ KGWNVTHMFR VAEEFFTSMG LSPMPPEFWA ESMLEKPTDG 

       370        380        390        400        410        420 
REVVCHASAW DFFNRKDFRI KQCTRITMEQ LSTVHHEMGH VQYYLQYKDL TVPLRRGANP 

       430        440        450        460        470        480 
GFHEAIGDVL ALSVSTPAHL HKIGLLDRVA NDLESDINYL LKMALEKIAF LPFGYLVDQW 

       490        500        510        520        530        540 
RWGVFSGHTP PSRYNFDWWY FRTKYQGICP PVVRNETHFD AGAKFHIPSG TPYIRYFVSF 

       550        560        570        580        590        600 
ILQFQFHQAL CKEAGHQGPL HQCDIYQSTQ AGAKLQRVLQ AGYSRPWQEV LKEMVGSDTL 

       610        620        630        640        650        660 
DAQALLEYFQ PVIRWLQEQN QRNGEVLGWP EYQWRPPLPD NYPEGIDLVT DETEAERFVE 

       670        680        690        700        710        720 
EYDRTARVLW NEYAEANWQY NTNITLEASK ILLQKNKKVA NHTLKYGTLA KKFDVSNFQN 

       730        740        750        760        770        780 
YTIKRIIKKV QNMDRAVLPP KELEEYNQIL MDMETTYSIA NVCYLNGTCL HLEPDLTNVM 

       790        800        810        820        830        840 
ATSRKYEELL WVWKSWRDKV GRAILPLFPK YVELSNKIAH LNGYADGGDS WRSSYESKSL 

       850        860        870        880        890        900 
EQDLEQLYQE LQPLYLNLHA YVRRSLHRHY GSQHINLDGP IPAHLLGNMW AQTWSNIYDL 

       910        920        930        940        950        960 
VAPFPSAPNL DATEAMIKQG WTPRRIFKEA DDFFTSLGLL PVSEEFWNKS MLEKPGDGRE 

       970        980        990       1000       1010       1020 
VVCHASAWDF YNGKDFRIKQ CTSVNMEDLV IAHHEMGHIQ YFMQYKDLPV TFREGANPGF 

      1030       1040       1050       1060       1070       1080 
HEAIGDVLAL SVSTPKHLHS LNLLSSEGGG YEHDINFLMK MALDKIAFIP FSYLIDQWRW 

      1090       1100       1110       1120       1130       1140 
RVFDGSITKE NYNQEWWSLR LKYQGLCPPV PRSQDDFDPG SKFHVPANVP YIRYFVSFII 

      1150       1160       1170       1180       1190       1200 
QFQFHEALCR AAGHTGPLHK CDIYQSKEAG KLLADTMKMG YSKPWPEAMK LITGQPNMSA 

      1210       1220       1230       1240       1250       1260 
SAMMNYFKPL TEWLVTENRR HGETLGWPEY NWTPNTARSE GPFPESGRVN FLGMYLEPQQ 

      1270       1280       1290       1300       1310 
ARVGQWVLLF LGVSLLVATL GLTHRLFSIR QHGHSLHRPH RGPQFGSEVE LRHS 

« Hide

Isoform Testis-specific (ACE-T) (Sequence not available).

References

[1]"cDNA cloning of hamster angiotensin-converting enzyme and mRNA expression."
Uchide T., Fujimori Y., Fukushima U., Uechi M., Sasaki T., Temma K.
DNA Seq. 17:319-325(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB212958 mRNA. Translation: BAD98304.1.
RefSeqNP_001268510.1. NM_001281581.1. [Q50JE5-1]

3D structure databases

ProteinModelPortalQ50JE5.
SMRQ50JE5. Positions 36-647, 651-1234.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSM02.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID101824864.

Phylogenomic databases

HOVERGENHBG000264.

Enzyme and pathway databases

BRENDA3.4.15.1. 3239.

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...

Entry information

Entry nameACE_MESAU
AccessionPrimary (citable) accession number: Q50JE5
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: June 7, 2005
Last modified: May 14, 2014
This is version 50 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