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Q10751 (ACE_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 91. 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·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
Gene names
Name:ACE
Synonyms:DCP1
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length1193 AA.
Sequence statusFragment.
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.

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.

Subcellular location

Membrane; Single-pass type I membrane protein.

Sequence similarities

Belongs to the peptidase M2 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – 1193›1193Angiotensin-converting enzyme
PRO_0000078152

Regions

Topological domain‹1 – 1156›1156Extracellular Potential
Transmembrane1157 – 117317Helical; Potential
Topological domain1174 – 119320Cytoplasmic Potential
Repeat125 – 481357
Repeat723 – 1079357

Sites

Active site28911 By similarity
Active site88712 By similarity
Metal binding2881Zinc 1; catalytic By similarity
Metal binding2921Zinc 1; catalytic By similarity
Metal binding8861Zinc 2; catalytic By similarity
Metal binding8901Zinc 2; catalytic By similarity

Amino acid modifications

Glycosylation111N-linked (GlcNAc...) Potential
Glycosylation601N-linked (GlcNAc...) Potential
Glycosylation2161N-linked (GlcNAc...) Potential
Glycosylation4071N-linked (GlcNAc...) Potential
Glycosylation4471N-linked (GlcNAc...) Potential
Glycosylation4851N-linked (GlcNAc...) Potential
Glycosylation5131N-linked (GlcNAc...) Potential
Glycosylation5551N-linked (GlcNAc...) Potential
Glycosylation5751N-linked (GlcNAc...) Potential
Glycosylation6581N-linked (GlcNAc...) Potential
Glycosylation10891N-linked (GlcNAc...) Potential

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
Q10751 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 954472A18EA471C7

FASTA1,193137,821
        10         20         30         40         50         60 
AKELYGNIWS NFSDPQLKKI IGSIQTLGPS NLPLDKRQQY NTILSDMDKI YSTAKVCLDN 

        70         80         90        100        110        120 
GTCWDLEPDI SDIMATSRSY KKLLYAWEGW HNAAGNPLRA KYQEFVTLSN EAYQMDGFED 

       130        140        150        160        170        180 
TGSYWRSWYD STTFEDDLEH LYNQLEPLYL NLHAFVRRKL YDRYGPKYIN LKGPIPAHLL 

       190        200        210        220        230        240 
GNMWAQQWNN IYDLMVPYPD KPNLDVTNTM VNQGWNATHM FRVSEEFFTS LGLLEMPPEF 

       250        260        270        280        290        300 
WEKSMLEKPA DGREVVCHAS AWDFYNRKDF RIKQCTTVTM EQLFTVHHEM GHVQYYLQYK 

       310        320        330        340        350        360 
DQPVSFRGGA NPGFHEAIGD VLSLSVSTPS HLQKIGLLSS AVEDEESNIN YLLKMALEKI 

       370        380        390        400        410        420 
AFLPFGYLID QWRWNVFSGR TPPSRYNYDW WYLRTKYQGI CAPVSRNESN FDPGAKYHIP 

       430        440        450        460        470        480 
GNTPYIRYFV SFILQFQFHK ALCQAANHTG PLHTCDIYMS KEAGAKLREV LKAGSSKSWQ 

       490        500        510        520        530        540 
EILFNLTGTD KMDAGALLEY FSPVTTWLQE QNNKTNEVLG WPEFDWRSPI PEGYPEGIDK 

       550        560        570        580        590        600 
IVDEAQAKEF LSEYNSTAEV VWNAYTEASW EYNTNITDHN KEVMLEKNLA MSKHTIEYGM 

       610        620        630        640        650        660 
RARQFDPSDF QDETVTRILN KLSVLERAAL PEDELKEYNT LLSDMETTYS VAKVCRENNT 

       670        680        690        700        710        720 
FHPLDPDLTD ILATSRDYNE LLFAWKGWWD ASGAKIKDKY KRYVELSNKA AVLNGYTDNG 

       730        740        750        760        770        780 
AYWRSLYETP TFEEDLERLY LQLQPLYLNL HAYVRRALYN KYGAEHISLK GPIPAHLLGN 

       790        800        810        820        830        840 
MWAQSWSNIF DLVMPFPDAT KVDATPAMKQ QGWTPKMMFE ESDRFFTSLG LIPMPQEFWD 

       850        860        870        880        890        900 
KSMIEKPADG REVVCHASAW DFYNRKDFRI KQCTVVNMDD LITVHHEMGH VQYFLQYMDQ 

       910        920        930        940        950        960 
PISFRDGANP GFHEAIGDVM ALSVSTPKHL HSINLLDQVT ENEESDINYL MSIALDKIAF 

       970        980        990       1000       1010       1020 
LPFGYLMDQW RWKVFDGRIK EDEYNQQWWN LRLKYQGLCP PVPRSEDDFD PGAKFHIPAN 

      1030       1040       1050       1060       1070       1080 
VPYIRYFVSF VIQFQFHQAL CKAAGHTGPL HTCDIYQSKE AGKLLGDAMK LGFSKPWPEA 

      1090       1100       1110       1120       1130       1140 
MQLITGQPNM SAEALMSYFE PLMTWLVKKN TENGEVLGWP EYSWTPYAVT EFHAATDTAD 

      1150       1160       1170       1180       1190 
FLGMSVGTKQ ATAGAWVLLA LALVFLITSI FLGVKLFSSR RKAFKSSSEM ELK 

« Hide

References

[1]"Chicken lacks the testis specific isozyme of angiotensin converting enzyme found in mammals."
Esther C.R., Thomas K.E., Bernstein K.E.
Biochem. Biophys. Res. Commun. 205:1916-1921(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Lung.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L40175 mRNA. Translation: AAA75554.1.
PIRJC2489.
UniGeneGga.3781.

3D structure databases

ProteinModelPortalQ10751.
SMRQ10751. Positions 1-539, 543-1120.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9031.ENSGALP00000039731.

Protein family/group databases

MEROPSM02.001.

Proteomic databases

PaxDbQ10751.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGNOG71044.
HOGENOMHOG000007838.
HOVERGENHBG000264.
PhylomeDBQ10751.

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_CHICK
AccessionPrimary (citable) accession number: Q10751
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 14, 2014
This is version 91 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