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Protein

Angiotensin-converting enzyme 2

Gene

ACE2

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Carboxypeptidase which converts angiotensin I to angiotensin 1-9, a peptide of unknown function, and angiotensin II to angiotensin 1-7, a vasodilator. Also able to hydrolyze apelin-13 and dynorphin-13 with high efficiency. May be an important regulator of heart function (By similarity).By similarity

Catalytic activityi

Angiotensin II + H2O = angiotensin-1-7 + L-phenylalanine.

Cofactori

Protein has several cofactor binding sites:
  • Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity
  • chlorideBy similarityNote: Binds 1 Cl- ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei168 – 1681ChlorideBy similarity
Binding sitei272 – 2721SubstrateBy similarity
Binding sitei344 – 3441SubstrateBy similarity
Binding sitei345 – 3451Substrate; via carbonyl oxygenBy similarity
Binding sitei370 – 3701SubstrateBy similarity
Metal bindingi373 – 3731Zinc; catalyticPROSITE-ProRule annotation
Active sitei374 – 3741PROSITE-ProRule annotation
Metal bindingi377 – 3771Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi401 – 4011Zinc; catalyticPROSITE-ProRule annotation
Binding sitei476 – 4761ChlorideBy similarity
Binding sitei480 – 4801ChlorideBy similarity
Active sitei504 – 5041PROSITE-ProRule annotation
Binding sitei514 – 5141SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Chloride, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-BTA-2022377. Metabolism of Angiotensinogen to Angiotensins.

Protein family/group databases

MEROPSiM02.006.

Names & Taxonomyi

Protein namesi
Recommended name:
Angiotensin-converting enzyme 2 (EC:3.4.17.23)
Alternative name(s):
ACE-related carboxypeptidase
Cleaved into the following chain:
Gene namesi
Name:ACE2
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome X

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini18 – 739722ExtracellularSequence analysisAdd
BLAST
Transmembranei740 – 76021HelicalSequence analysisAdd
BLAST
Topological domaini761 – 80444CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence analysisAdd
BLAST
Chaini18 – 804787Angiotensin-converting enzyme 2PRO_0000028568Add
BLAST
Chaini18 – 707690Processed angiotensin-converting enzyme 2PRO_0000292266Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi53 – 531N-linked (GlcNAc...)Sequence analysis
Glycosylationi90 – 901N-linked (GlcNAc...)Sequence analysis
Glycosylationi298 – 2981N-linked (GlcNAc...)Sequence analysis
Disulfide bondi343 ↔ 360By similarity
Glycosylationi431 – 4311N-linked (GlcNAc...)Sequence analysis
Disulfide bondi529 ↔ 541By similarity
Glycosylationi545 – 5451N-linked (GlcNAc...)Sequence analysis
Glycosylationi659 – 6591N-linked (GlcNAc...)Sequence analysis
Glycosylationi689 – 6891N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

Proteolytic cleavage by ADAM17 generates a secreted form. Also cleaved by serine proteases: TMPRSS2, TMPRSS11D and HPN/TMPRSS1 (By similarity).By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ58DD0.
PRIDEiQ58DD0.

Interactioni

Subunit structurei

Interacts with ITGB1 and the catalytically active form of TMPRSS2.By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000045721.

Structurei

3D structure databases

ProteinModelPortaliQ58DD0.
SMRiQ58DD0. Positions 19-614.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni651 – 6588Essential for cleavage by ADAM17By similarity
Regioni696 – 71520Essential for cleavage by TMPRSS11D and TMPRSS2By similarityAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase M2 family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3690. Eukaryota.
ENOG410XPJ3. LUCA.
GeneTreeiENSGT00520000055576.
HOGENOMiHOG000292210.
HOVERGENiHBG000265.
InParanoidiQ58DD0.
OMAiCNPNNPQ.
OrthoDBiEOG76HQ13.
TreeFamiTF312861.

Family and domain databases

InterProiIPR033591. ACE2.
IPR031588. Collectrin_dom.
IPR001548. Peptidase_M2.
[Graphical view]
PANTHERiPTHR10514. PTHR10514. 2 hits.
PTHR10514:SF24. PTHR10514:SF24. 2 hits.
PfamiPF16959. Collectrin. 1 hit.
PF01401. Peptidase_M2. 1 hit.
[Graphical view]
PRINTSiPR00791. PEPDIPTASEA.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q58DD0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTGSFWLLLS LVAVTAAQST TEEQAKTFLE KFNHEAEDLS YQSSLASWNY
60 70 80 90 100
NTNITDENVQ KMNEARAKWS AFYEEQSRMA KTYSLEEIQN LTLKRQLKAL
110 120 130 140 150
QHSGTSALSA EKSKRLNTIL NKMSTIYSTG KVLDPNTQEC LALEPGLDDI
160 170 180 190 200
MENSRDYNRR LWAWEGWRAE VGKQLRPLYE EYVVLENEMA RANNYEDYGD
210 220 230 240 250
YWRGDYEVTG AGDYDYSRDQ LMKDVERTFA EIKPLYEQLH AYVRAKLMHT
260 270 280 290 300
YPSYISPTGC LPAHLLGDMW GRFWTNLYSL TVPFEHKPSI DVTEKMENQS
310 320 330 340 350
WDAERIFKEA EKFFVSISLP YMTQGFWDNS MLTEPGDGRK VVCHPTAWDL
360 370 380 390 400
GKGDFRIKMC TKVTMDDFLT AHHEMGHIQY DMAYAAQPYL LRNGANEGFH
410 420 430 440 450
EAVGEIMSLS AATPHYLKAL GLLAPDFHED NETEINFLLK QALTIVGTLP
460 470 480 490 500
FTYMLEKWRW MVFKGEIPKQ QWMEKWWEMK REIVGVVEPL PHDETYCDPA
510 520 530 540 550
CLFHVAEDYS FIRYYTRTIY QFQFHEALCK TAKHEGALFK CDISNSTEAG
560 570 580 590 600
QRLLQMLRLG KSEPWTLALE NIVGIKTMDV KPLLNYFEPL FTWLKEQNRN
610 620 630 640 650
SFVGWSTEWT PYSDQSIKVR ISLKSALGEN AYEWNDNEMY LFQSSVAYAM
660 670 680 690 700
RKYFSEARNE TVLFGEDNVW VSDKKPRISF KFFVTSPNNV SDIIPRTEVE
710 720 730 740 750
NAIRLSRDRI NDVFQLDDNS LEFLGIQPTL GPPYEPPVTI WLIIFGVVMG
760 770 780 790 800
VVVIGIVVLI FTGIRNRRKK NQASSEENPY GSVDLNKGEN NSGFQNIDDV

QTSL
Length:804
Mass (Da):93,067
Last modified:April 26, 2005 - v1
Checksum:iE81570A96872A963
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT021667 mRNA. Translation: AAX46514.1.
RefSeqiXP_005228486.1. XM_005228429.3.
UniGeneiBt.28278.

Genome annotation databases

EnsembliENSBTAT00000048730; ENSBTAP00000045721; ENSBTAG00000034402.
GeneIDi509235.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT021667 mRNA. Translation: AAX46514.1.
RefSeqiXP_005228486.1. XM_005228429.3.
UniGeneiBt.28278.

3D structure databases

ProteinModelPortaliQ58DD0.
SMRiQ58DD0. Positions 19-614.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000045721.

Protein family/group databases

MEROPSiM02.006.

Proteomic databases

PaxDbiQ58DD0.
PRIDEiQ58DD0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000048730; ENSBTAP00000045721; ENSBTAG00000034402.
GeneIDi509235.

Organism-specific databases

CTDi59272.

Phylogenomic databases

eggNOGiKOG3690. Eukaryota.
ENOG410XPJ3. LUCA.
GeneTreeiENSGT00520000055576.
HOGENOMiHOG000292210.
HOVERGENiHBG000265.
InParanoidiQ58DD0.
OMAiCNPNNPQ.
OrthoDBiEOG76HQ13.
TreeFamiTF312861.

Enzyme and pathway databases

ReactomeiR-BTA-2022377. Metabolism of Angiotensinogen to Angiotensins.

Family and domain databases

InterProiIPR033591. ACE2.
IPR031588. Collectrin_dom.
IPR001548. Peptidase_M2.
[Graphical view]
PANTHERiPTHR10514. PTHR10514. 2 hits.
PTHR10514:SF24. PTHR10514:SF24. 2 hits.
PfamiPF16959. Collectrin. 1 hit.
PF01401. Peptidase_M2. 1 hit.
[Graphical view]
PRINTSiPR00791. PEPDIPTASEA.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].

Entry informationi

Entry nameiACE2_BOVIN
AccessioniPrimary (citable) accession number: Q58DD0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: April 26, 2005
Last modified: July 6, 2016
This is version 101 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. Peptidase families
    Classification of peptidase families and list of entries
  2. 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.