Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Angiotensin-converting enzyme

Gene

ACE

Organism
Haematobia irritans exigua (Buffalo fly)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Involved in the specific maturation or degradation of a number of bioactive peptides.

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

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi367Zinc; catalyticPROSITE-ProRule annotation1
Active sitei368PROSITE-ProRule annotation1
Metal bindingi371Zinc; catalyticPROSITE-ProRule annotation1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM02.003.

Names & Taxonomyi

Protein namesi
Recommended name:
Angiotensin-converting enzyme (EC:3.4.15.1)
Alternative name(s):
Dipeptidyl carboxypeptidase I
Kininase II
Gene namesi
Name:ACE
OrganismiHaematobia irritans exigua (Buffalo fly)
Taxonomic identifieri34678 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaMuscoideaMuscidaeHaematobia

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 17Sequence analysisAdd BLAST17
ChainiPRO_000002856518 – 611Angiotensin-converting enzymeAdd BLAST594

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi53N-linked (GlcNAc...)Sequence analysis1
Glycosylationi196N-linked (GlcNAc...)Sequence analysis1
Glycosylationi531N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Glycoprotein

Expressioni

Tissue specificityi

Expressed in the compound ganglion and in the posterior region of the midgut.

Structurei

3D structure databases

ProteinModelPortaliQ10715.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M2 family.Curated

Keywords - Domaini

Signal

Family and domain databases

CDDicd06461. M2_ACE. 1 hit.
InterProiIPR001548. Peptidase_M2.
[Graphical view]
PANTHERiPTHR10514. PTHR10514. 1 hit.
PfamiPF01401. 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.

Q10715-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLLVVTILA GLAVCHGATK EEIVATEYLQ NINKELAKHT NVETEVSWAY
60 70 80 90 100
ASNITDENER LRNEISAENA KFLKEVAKDI QKFNWRTYGS ADVRRQFKSL
110 120 130 140 150
SKTGYSALPA EDYAELLEVL SAMESNFAKV RVCDYKNSAK CDLSLDPEIE
160 170 180 190 200
EIITKSRDPE ELKYYWTQFY DKAGTPTRSN FEKYVELNTK SAKLNNFTDG
210 220 230 240 250
AEVWLDEYED ATFEDQLEAI FEDIKPLYDQ VHGYVRYRLN KFYGDEVVSK
260 270 280 290 300
TGPLPMHLLG NMWAQQWSSI ADIVSPFPEK PLVDVSDEMV AQGYTPLKMF
310 320 330 340 350
QMGDDFFQSM GLKKLPQEFW DKSILEKPDD GRDLVCHASA WDFYLTDDVR
360 370 380 390 400
IKQCTRVTQD QFFTVHHEMG HIQYFLQYQH QPFVYRTGAN PGFHEAVGDV
410 420 430 440 450
LSLSVSTPKH LERVGLLKNY VSDNEARINQ LFLTALDKIV FLPFAFTMDK
460 470 480 490 500
YRWALFRGQA DKSEWNCAFW KLREEYSGIE PPVVRTEKDF DAPAKYHVSA
510 520 530 540 550
DVEYLRYLVS FIIQFQFYKS ACITAGEYVP NQTEYPLDNC DIYGSKEAGK
560 570 580 590 600
LFENMLSLGA SKPWPDALEA FNGERTMTGK AIAEYFEPLR VWLEAVAVES
610
LCHQRYKNVD L
Length:611
Mass (Da):70,506
Last modified:November 1, 1997 - v1
Checksum:iA43D6DF5A83ECB53
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L43965 Genomic DNA. Translation: AAA70427.1.
PIRiS65472.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L43965 Genomic DNA. Translation: AAA70427.1.
PIRiS65472.

3D structure databases

ProteinModelPortaliQ10715.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiM02.003.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

CDDicd06461. M2_ACE. 1 hit.
InterProiIPR001548. Peptidase_M2.
[Graphical view]
PANTHERiPTHR10514. PTHR10514. 1 hit.
PfamiPF01401. Peptidase_M2. 1 hit.
[Graphical view]
PRINTSiPR00791. PEPDIPTASEA.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiACE_HAEIX
AccessioniPrimary (citable) accession number: Q10715
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: November 30, 2016
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

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.