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Protein

Acylamino-acid-releasing enzyme

Gene

APEH

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

This enzyme catalyzes the hydrolysis of the N-terminal peptide bond of an N-acetylated peptide to generate an N-acetylated amino acid and a peptide with a free N-terminus. It preferentially cleaves off Ac-Ala, Ac-Met and Ac-Ser.

Catalytic activityi

Cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei585 – 5851Charge relay systemPROSITE-ProRule annotation
Active sitei673 – 6731Charge relay systemPROSITE-ProRule annotation
Active sitei705 – 7051Charge relay systemPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Protein family/group databases

ESTHERibovin-acph. ACPH_Peptidase_S9.
MEROPSiS09.004.

Names & Taxonomyi

Protein namesi
Recommended name:
Acylamino-acid-releasing enzyme (EC:3.4.19.1)
Short name:
AARE
Alternative name(s):
Acyl-peptide hydrolase
Short name:
APH
Acylaminoacyl-peptidase
Gene namesi
Name:APEH
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136 Componenti: Chromosome 22

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 730730Acylamino-acid-releasing enzymePRO_0000122429Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei183 – 1831PhosphoserineBy similarity
Modified residuei185 – 1851PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiP80227.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000015388.

Structurei

3D structure databases

ProteinModelPortaliP80227.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S9C family.Curated

Phylogenomic databases

eggNOGiCOG1506.
GeneTreeiENSGT00390000013172.
HOGENOMiHOG000007443.
HOVERGENiHBG000869.
InParanoidiP80227.
KOiK01303.
OMAiIGGKCEL.
OrthoDBiEOG776SPB.
TreeFamiTF312937.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002471. Pept_S9_AS.
IPR001375. Peptidase_S9.
IPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view]
PfamiPF00326. Peptidase_S9. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00708. PRO_ENDOPEP_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P80227-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MERQVLLSEP EEAAALYRGL SRQPALSAAC LGPEVTTQYG GRYRTVHTEW
60 70 80 90 100
TQRDLERMEN IRFCRQYLVF HDGDSVVFAG PAGNSVETRG ELLSRESPSG
110 120 130 140 150
TMKAVLRKAG STGEEKQFLE VWEKNRKLKS FNLSALEKHG PVYEDDCFGC
160 170 180 190 200
LSWSHSETHL LYVAEKKRPK AESFFQTKAL DISGSDDEMA RPKKPDQAIK
210 220 230 240 250
GDQFLFYEDW GENMVSKGSP VLCVLDIESG NISVLEGVPE SVSPGQAFWA
260 270 280 290 300
PGDTGVVFAG WWHEPFRLGI RFCTNRRSAL YYVDLTGGNC ELLSDDSLAV
310 320 330 340 350
TSPRLSPDQC RIVYLQFPSL VPHQQCGQLC LYDWYTRVTV VVVDVVPRQL
360 370 380 390 400
GENFSGIYCS LLPLGCWSAD SQRVVFDTAQ RSRQDLFAVD TQMGTVTPLT
410 420 430 440 450
AGGSGGSWKL LTIDRDLMVA QFSTPNLPPC LKVGFLPPAG MEQEVVWVSL
460 470 480 490 500
EEAEPIPDIS WSIRVLQPPP EQEHAQYVGL DFEAILIQPS NPPDKTQVPM
510 520 530 540 550
VVMPHGGPHS SFVTSWMLLP AMLCKMGFAA LLVNYRGSTG FGQDSILSLP
560 570 580 590 600
GNVGSQDVKD VQFAVEQVLQ EEHFDAGRVA LLGGSHGGFL SCHLIGQYPE
610 620 630 640 650
TYGACVVRNP VINIASMMGS TDIPDWCVVE AGYLYSSDCL PDPNVWSEML
660 670 680 690 700
NKSPIKYTPQ VKTPVLLMLG QEDRRVPFKQ GMEYYRALKA RNVPVRLLLY
710 720 730
PKSTHSLSEV EVESDSFMNA VIWMCTHLGH
Length:730
Mass (Da):81,093
Last modified:February 10, 2009 - v2
Checksum:i838882B5B703DF15
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC123400 mRNA. Translation: AAI23401.1.
PIRiS36842.
RefSeqiNP_001076900.1. NM_001083431.1.
UniGeneiBt.2056.

Genome annotation databases

EnsembliENSBTAT00000015388; ENSBTAP00000015388; ENSBTAG00000011583.
GeneIDi514666.
KEGGibta:514666.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC123400 mRNA. Translation: AAI23401.1.
PIRiS36842.
RefSeqiNP_001076900.1. NM_001083431.1.
UniGeneiBt.2056.

3D structure databases

ProteinModelPortaliP80227.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000015388.

Protein family/group databases

ESTHERibovin-acph. ACPH_Peptidase_S9.
MEROPSiS09.004.

Proteomic databases

PRIDEiP80227.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000015388; ENSBTAP00000015388; ENSBTAG00000011583.
GeneIDi514666.
KEGGibta:514666.

Organism-specific databases

CTDi327.

Phylogenomic databases

eggNOGiCOG1506.
GeneTreeiENSGT00390000013172.
HOGENOMiHOG000007443.
HOVERGENiHBG000869.
InParanoidiP80227.
KOiK01303.
OMAiIGGKCEL.
OrthoDBiEOG776SPB.
TreeFamiTF312937.

Miscellaneous databases

NextBioi20871454.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002471. Pept_S9_AS.
IPR001375. Peptidase_S9.
IPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view]
PfamiPF00326. Peptidase_S9. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00708. PRO_ENDOPEP_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. NIH - Mammalian Gene Collection (MGC) project
    Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Thalamus.
  2. "Bovine lens acylpeptide hydrolase. Purification and characterization of a tetrameric enzyme resistant to urea denaturation and proteolytic inactivation."
    Sharma K.K., Ortwerth B.J.
    Eur. J. Biochem. 216:631-637(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 194-213.
    Tissue: Lens.

Entry informationi

Entry nameiACPH_BOVIN
AccessioniPrimary (citable) accession number: P80227
Secondary accession number(s): A4FUX4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: February 10, 2009
Last modified: June 24, 2015
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

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

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 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.