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Q10715

- ACE_HAEIX

UniProt

Q10715 - ACE_HAEIX

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Protein
Angiotensin-converting enzyme
Gene
ACE
Organism
Haematobia irritans exigua (Buffalo fly)
Status
Reviewed - Annotation score: 3 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

Binds 1 zinc ion per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi367 – 3671Zinc; catalytic By similarity
Active sitei368 – 3681 By similarity
Metal bindingi371 – 3711Zinc; catalytic By similarity

GO - Molecular functioni

  1. carboxypeptidase activity Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. metallopeptidase activity Source: UniProtKB-KW
  4. peptidyl-dipeptidase activity Source: InterPro
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

  1. extracellular space Source: UniProtKB-SubCell
  2. membrane Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717 Reviewed prediction
Add
BLAST
Chaini18 – 611594Angiotensin-converting enzyme
PRO_0000028565Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi53 – 531N-linked (GlcNAc...) Reviewed prediction
Glycosylationi196 – 1961N-linked (GlcNAc...) Reviewed prediction
Glycosylationi531 – 5311N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Glycoprotein

Expressioni

Tissue specificityi

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

Structurei

3D structure databases

ProteinModelPortaliQ10715.
SMRiQ10715. Positions 23-603.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M2 family.

Keywords - Domaini

Signal

Family and domain databases

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

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MKLLVVTILA GLAVCHGATK EEIVATEYLQ NINKELAKHT NVETEVSWAY    50
ASNITDENER LRNEISAENA KFLKEVAKDI QKFNWRTYGS ADVRRQFKSL 100
SKTGYSALPA EDYAELLEVL SAMESNFAKV RVCDYKNSAK CDLSLDPEIE 150
EIITKSRDPE ELKYYWTQFY DKAGTPTRSN FEKYVELNTK SAKLNNFTDG 200
AEVWLDEYED ATFEDQLEAI FEDIKPLYDQ VHGYVRYRLN KFYGDEVVSK 250
TGPLPMHLLG NMWAQQWSSI ADIVSPFPEK PLVDVSDEMV AQGYTPLKMF 300
QMGDDFFQSM GLKKLPQEFW DKSILEKPDD GRDLVCHASA WDFYLTDDVR 350
IKQCTRVTQD QFFTVHHEMG HIQYFLQYQH QPFVYRTGAN PGFHEAVGDV 400
LSLSVSTPKH LERVGLLKNY VSDNEARINQ LFLTALDKIV FLPFAFTMDK 450
YRWALFRGQA DKSEWNCAFW KLREEYSGIE PPVVRTEKDF DAPAKYHVSA 500
DVEYLRYLVS FIIQFQFYKS ACITAGEYVP NQTEYPLDNC DIYGSKEAGK 550
LFENMLSLGA SKPWPDALEA FNGERTMTGK AIAEYFEPLR VWLEAVAVES 600
LCHQRYKNVD L 611
Length:611
Mass (Da):70,506
Last modified:November 1, 1997 - v1
Checksum:iA43D6DF5A83ECB53
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L43965 Genomic DNA. Translation: AAA70427.1.
PIRiS65472.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L43965 Genomic DNA. Translation: AAA70427.1 .
PIRi S65472.

3D structure databases

ProteinModelPortali Q10715.
SMRi Q10715. Positions 23-603.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi M02.003.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

InterProi IPR001548. Peptidase_M2.
[Graphical view ]
PANTHERi PTHR10514. PTHR10514. 1 hit.
Pfami PF01401. Peptidase_M2. 1 hit.
[Graphical view ]
PRINTSi PR00791. PEPDIPTASEA.
PROSITEi PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Cloning and characterisation of angiotensin-converting enzyme from the dipteran species, Haematobia irritans exigua, and its expression in the maturing male reproductive system."
    Wijffels G.L., Fitzgerald C., Gough J., Riding G.A., Elvin C., Kemp D.J., Willadsen P.
    Eur. J. Biochem. 237:414-423(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

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: May 14, 2014
This is version 66 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

External Data

Dasty 3

Similar proteinsi