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P19205

- ACPH_PIG

UniProt

P19205 - ACPH_PIG

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Protein

Acylamino-acid-releasing enzyme

Gene

APEH

Organism
Sus scrofa (Pig)
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.

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 system1 PublicationPROSITE-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
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227: Unplaced

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_0000122432Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine2 Publications
Modified residuei187 – 1871PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP19205.
PRIDEiP19205.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000012138.

Structurei

3D structure databases

ProteinModelPortaliP19205.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S9C family.Curated

Phylogenomic databases

eggNOGiCOG1506.
HOGENOMiHOG000007443.
HOVERGENiHBG000869.
InParanoidiP19205.
KOiK01303.

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.

P19205-1 [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 GTGTAEEKQF LEVWEKNRKL KSFNLSALEK HGPVYEDDCF
160 170 180 190 200
GCLSWSHSET HLLYVADKKR PKAESFFQTK ALDVTGSDDE MARTKKPDQA
210 220 230 240 250
IKGDQFLFYE DWGENMVSKS TPVLCVLDIE SGNISVLEGV PESVSPGQAF
260 270 280 290 300
WAPGDTGVVF VGWWHEPFRL GIRFCTNRRS ALYYVDLTGG KCELLSDESV
310 320 330 340 350
AVTSPRLSPD QCRIVYLRFP SLVPHQQCGQ LCLYDWYTRV TSVVVDIVPR
360 370 380 390 400
QLGEDFSGIY CSLLPLGCWS ADSQRVVFDS PQRSRQDLFA VDTQMGSVTS
410 420 430 440 450
LTAGGSGGSW KLLTIDRDLM VVQFSTPSVP PSLKVGFLPP AGKEQAVSWV
460 470 480 490 500
SLEEAEPFPD ISWSIRVLQP PPQQEHVQYA GLDFEAILLQ PSNSPEKTQV
510 520 530 540 550
PMVVMPHGGP HSSFVTAWML FPAMLCKMGF AVLLVNYRGS TGFGQDSILS
560 570 580 590 600
LPGNVGHQDV KDVQFAVEQV LQEEHFDAGR VALMGGSHGG FLSCHLIGQY
610 620 630 640 650
PETYSACVVR NPVINIASMM GSTDIPDWCM VEAGFSYSSD CLPDLSVWAA
660 670 680 690 700
MLDKSPIKYA PQVKTPLLLM LGQEDRRVPF KQGMEYYRVL KARNVPVRLL
710 720 730
LYPKSTHALS EVEVESDSFM NAVLWLCTHL GS
Length:732
Mass (Da):81,244
Last modified:February 1, 1996 - v2
Checksum:i017BD40E049A604C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti167 – 1671D → E AA sequence (PubMed:8576092)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D00524 mRNA. Translation: BAA00411.1.
PIRiJU0132.
RefSeqiNP_999088.1. NM_213923.1.
UniGeneiSsc.3208.

Genome annotation databases

GeneIDi396961.
KEGGissc:396961.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D00524 mRNA. Translation: BAA00411.1 .
PIRi JU0132.
RefSeqi NP_999088.1. NM_213923.1.
UniGenei Ssc.3208.

3D structure databases

ProteinModelPortali P19205.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9823.ENSSSCP00000012138.

Chemistry

ChEMBLi CHEMBL2021757.

Protein family/group databases

MEROPSi S09.004.

Proteomic databases

PaxDbi P19205.
PRIDEi P19205.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 396961.
KEGGi ssc:396961.

Organism-specific databases

CTDi 327.

Phylogenomic databases

eggNOGi COG1506.
HOGENOMi HOG000007443.
HOVERGENi HBG000869.
InParanoidi P19205.
KOi K01303.

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. "The primary structure of porcine liver acylamino acid-releasing enzyme deduced from cDNA sequences."
    Mitta M., Asada K., Uchimura Y., Kimizuka F., Kato I., Sakiyama F., Tsunasawa S.
    J. Biochem. 106:548-551(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, ACETYLATION AT MET-1.
    Tissue: Liver.
  2. "Complete covalent structure of porcine liver acylamino acid-releasing enzyme and identification of its active site serine residue."
    Miyagi M., Sakiyama F., Kato I., Tsunasawa S.
    J. Biochem. 118:771-779(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY, ACTIVE SITE SER-587.
    Tissue: Liver.

Entry informationi

Entry nameiACPH_PIG
AccessioniPrimary (citable) accession number: P19205
Secondary accession number(s): Q9TS46
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: February 1, 1996
Last modified: October 29, 2014
This is version 98 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