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P13676

- ACPH_RAT

UniProt

P13676 - ACPH_RAT

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Protein

Acylamino-acid-releasing enzyme

Gene

Apeh

Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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.1 Publication

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 sitei587 – 5871Charge relay systemPROSITE-ProRule annotation
Active sitei675 – 6751Charge relay systemPROSITE-ProRule annotation
Active sitei707 – 7071Charge relay systemPROSITE-ProRule annotation

GO - Molecular functioni

  1. serine-type endopeptidase activity Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Protein family/group databases

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi2125. Apeh.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 732732Acylamino-acid-releasing enzymePRO_0000122434Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11Blocked amino end (Met)1 Publication
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei185 – 1851PhosphoserineBy similarity
Modified residuei187 – 1871PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP13676.
PRIDEiP13676.

PTM databases

PhosphoSiteiP13676.

Expressioni

Gene expression databases

GenevestigatoriP13676.

Interactioni

Subunit structurei

Homotetramer.

Structurei

3D structure databases

ProteinModelPortaliP13676.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S9C family.Curated

Phylogenomic databases

eggNOGiCOG1506.
HOGENOMiHOG000007443.
HOVERGENiHBG000869.
InParanoidiP13676.
KOiK01303.
PhylomeDBiP13676.

Family and domain databases

Gene3Di2.120.10.30. 2 hits.
3.40.50.1820. 1 hit.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR029058. AB_hydrolase.
IPR002471. Pept_S9_AS.
IPR001375. Peptidase_S9.
[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.

P13676 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MERQVLLSEP QEAAALYRGL SRQPSLSAAC LGPEVTTQYG GLYRTVHTEW
60 70 80 90 100
TQRDLERMEN IRFCRQYLVF HDGDSVVFAG PAGNSVETRG ELLSRESPSG
110 120 130 140 150
TMKAVLRKAG GTVSGEEKQF LEVWEKNRKL KSFNLSALEK HGPVYEDDCF
160 170 180 190 200
GCLSWSHSET HLLYVAEKKR PKAESFFQTK ALDISASDDE MARPKKPDQA
210 220 230 240 250
IKGDQFVFYE DWGETMVSKS IPVLCVLDID SGNISVLEGV PENVSPGQAF
260 270 280 290 300
WAPGDTGVVF VGWWHEPFRL GIRYCTNRRS ALYYVDLSGG KCELLSDGSL
310 320 330 340 350
AICSPRLSPD QCRIVYLQYP CLAPHHQCSQ LCLYDWYTKV TSVVVDIVPR
360 370 380 390 400
QLGESFSGIY CSLLPLGCWS ADSQRVVFDS AQRSRQDLFA VDTQTGSITS
410 420 430 440 450
LTAAGSAGSW KLLTIDKDLM VAQFSTPSLP PSLKVGFLPP PGKEQSVSWV
460 470 480 490 500
SLEEAEPIPG IHWGVRVLHP PPDQENVQYA DLDFEAILLQ PSNPPDKTQV
510 520 530 540 550
PMVVMPHGGP HSSFVTAWML FPAMLCKMGF AVLLVNYRGS TGFGQDSILS
560 570 580 590 600
LPGNVGHQDV KDVQFAVEQV LQEEHFDARR VALMGGSHGG FLSCHLIGQY
610 620 630 640 650
PETYSACIAR NPVINIASMM GSTDIPDWCM VETGFPYSNS CLPDLNVWEE
660 670 680 690 700
MLDKSPIKYI PQVKTPVLLM LGQEDRRVPF KQGMEYYRAL KARNVPVRLL
710 720 730
LYPKSNHALS EVEAESDSFM NAVLWLHTHL GS
Length:732
Mass (Da):81,384
Last modified:January 1, 1990 - v1
Checksum:i43F234879E10235B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti625 – 6284IPDW → M in CAA33040. (PubMed:2578023)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J04733 mRNA. Translation: AAA88506.1.
X14915 Genomic DNA. Translation: CAA33040.1. Sequence problems.
PIRiA33706. S07624.
RefSeqiNP_036632.1. NM_012500.1.
UniGeneiRn.11057.

Genome annotation databases

GeneIDi24206.
KEGGirno:24206.
UCSCiRGD:2125. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J04733 mRNA. Translation: AAA88506.1 .
X14915 Genomic DNA. Translation: CAA33040.1 . Sequence problems.
PIRi A33706. S07624.
RefSeqi NP_036632.1. NM_012500.1.
UniGenei Rn.11057.

3D structure databases

ProteinModelPortali P13676.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi S09.004.

PTM databases

PhosphoSitei P13676.

Proteomic databases

PaxDbi P13676.
PRIDEi P13676.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 24206.
KEGGi rno:24206.
UCSCi RGD:2125. rat.

Organism-specific databases

CTDi 327.
RGDi 2125. Apeh.

Phylogenomic databases

eggNOGi COG1506.
HOGENOMi HOG000007443.
HOVERGENi HBG000869.
InParanoidi P13676.
KOi K01303.
PhylomeDBi P13676.

Miscellaneous databases

NextBioi 602597.

Gene expression databases

Genevestigatori P13676.

Family and domain databases

Gene3Di 2.120.10.30. 2 hits.
3.40.50.1820. 1 hit.
InterProi IPR011042. 6-blade_b-propeller_TolB-like.
IPR029058. AB_hydrolase.
IPR002471. Pept_S9_AS.
IPR001375. Peptidase_S9.
[Graphical view ]
Pfami PF00326. Peptidase_S9. 1 hit.
[Graphical view ]
SUPFAMi SSF53474. SSF53474. 1 hit.
PROSITEi PS00708. PRO_ENDOPEP_SER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Cloning and sequence analysis of a rat liver cDNA encoding acyl-peptide hydrolase."
    Kobayashi K., Lin L.-W., Yeadon J.E., Klickstein L.B., Smith J.A.
    J. Biol. Chem. 264:8892-8899(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. "Structural organization of the rat acyl-peptide hydrolase gene."
    Lin L.-W., Lee F.J.S., Smith J.A.
    Nucleic Acids Res. 17:4397-4400(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Sprague-Dawley.
  3. "Acyl-peptide hydrolase from rat liver. Characterization of enzyme reaction."
    Kobayashi K., Smith J.A.
    J. Biol. Chem. 262:11435-11445(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: BLOCKAGE OF N-TERMINUS, FUNCTION.

Entry informationi

Entry nameiACPH_RAT
AccessioniPrimary (citable) accession number: P13676
Secondary accession number(s): P14320, P70479
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: October 29, 2014
This is version 118 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

External Data

Dasty 3