ACPH_RAT
ID ACPH_RAT Reviewed; 732 AA.
AC P13676; P14320; P70479;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 25-MAY-2022, entry version 144.
DE RecName: Full=Acylamino-acid-releasing enzyme;
DE Short=AARE;
DE EC=3.4.19.1;
DE AltName: Full=Acyl-peptide hydrolase;
DE Short=APH;
DE AltName: Full=Acylaminoacyl-peptidase;
GN Name=Apeh;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=2722805; DOI=10.1016/s0021-9258(18)81877-4;
RA Kobayashi K., Lin L.-W., Yeadon J.E., Klickstein L.B., Smith J.A.;
RT "Cloning and sequence analysis of a rat liver cDNA encoding acyl-peptide
RT hydrolase.";
RL J. Biol. Chem. 264:8892-8899(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=2578023; DOI=10.1093/nar/17.11.4397;
RA Lin L.-W., Lee F.J.S., Smith J.A.;
RT "Structural organization of the rat acyl-peptide hydrolase gene.";
RL Nucleic Acids Res. 17:4397-4400(1989).
RN [3]
RP BLOCKAGE OF N-TERMINUS, AND FUNCTION.
RX PubMed=3305492; DOI=10.1016/s0021-9258(18)60825-7;
RA Kobayashi K., Smith J.A.;
RT "Acyl-peptide hydrolase from rat liver. Characterization of enzyme
RT reaction.";
RL J. Biol. Chem. 262:11435-11445(1987).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: This enzyme catalyzes the hydrolysis of the N-terminal
CC peptide bond of an N-acetylated peptide to generate an N-acetylated
CC amino acid and a peptide with a free N-terminus. It preferentially
CC cleaves off Ac-Ala, Ac-Met and Ac-Ser. {ECO:0000269|PubMed:3305492}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of an N-acetyl or N-formyl amino acid from the N-
CC terminus of a polypeptide.; EC=3.4.19.1;
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the peptidase S9C family. {ECO:0000305}.
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DR EMBL; J04733; AAA88506.1; -; mRNA.
DR EMBL; X14915; CAA33040.1; ALT_SEQ; Genomic_DNA.
DR PIR; A33706; S07624.
DR RefSeq; NP_036632.1; NM_012500.1.
DR AlphaFoldDB; P13676; -.
DR SMR; P13676; -.
DR STRING; 10116.ENSRNOP00000043843; -.
DR ESTHER; ratno-acph; ACPH_Peptidase_S9.
DR iPTMnet; P13676; -.
DR PhosphoSitePlus; P13676; -.
DR jPOST; P13676; -.
DR PaxDb; P13676; -.
DR PRIDE; P13676; -.
DR GeneID; 24206; -.
DR KEGG; rno:24206; -.
DR UCSC; RGD:2125; rat.
DR CTD; 327; -.
DR RGD; 2125; Apeh.
DR eggNOG; KOG2100; Eukaryota.
DR InParanoid; P13676; -.
DR OrthoDB; 265965at2759; -.
DR PhylomeDB; P13676; -.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-72764; Eukaryotic Translation Termination.
DR PRO; PR:P13676; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0008242; F:omega peptidase activity; ISO:RGD.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISO:RGD.
DR GO; GO:0050435; P:amyloid-beta metabolic process; ISO:RGD.
DR GO; GO:0006508; P:proteolysis; ISO:RGD.
DR Gene3D; 2.120.10.30; -; 1.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR045550; AARE_N.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002471; Pept_S9_AS.
DR InterPro; IPR001375; Peptidase_S9.
DR Pfam; PF19283; APEH_N; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Hydrolase; Phosphoprotein; Reference proteome.
FT CHAIN 1..732
FT /note="Acylamino-acid-releasing enzyme"
FT /id="PRO_0000122434"
FT ACT_SITE 587
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT ACT_SITE 675
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT ACT_SITE 707
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT MOD_RES 1
FT /note="Blocked amino end (Met); alternate"
FT /evidence="ECO:0000269|PubMed:2722805"
FT MOD_RES 1
FT /note="N-acetylmethionine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P13798"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13798"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CONFLICT 625..628
FT /note="IPDW -> M (in Ref. 2; CAA33040)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 732 AA; 81384 MW; 43F234879E10235B CRC64;
MERQVLLSEP QEAAALYRGL SRQPSLSAAC LGPEVTTQYG GLYRTVHTEW TQRDLERMEN
IRFCRQYLVF HDGDSVVFAG PAGNSVETRG ELLSRESPSG TMKAVLRKAG GTVSGEEKQF
LEVWEKNRKL KSFNLSALEK HGPVYEDDCF GCLSWSHSET HLLYVAEKKR PKAESFFQTK
ALDISASDDE MARPKKPDQA IKGDQFVFYE DWGETMVSKS IPVLCVLDID SGNISVLEGV
PENVSPGQAF WAPGDTGVVF VGWWHEPFRL GIRYCTNRRS ALYYVDLSGG KCELLSDGSL
AICSPRLSPD QCRIVYLQYP CLAPHHQCSQ LCLYDWYTKV TSVVVDIVPR QLGESFSGIY
CSLLPLGCWS ADSQRVVFDS AQRSRQDLFA VDTQTGSITS LTAAGSAGSW KLLTIDKDLM
VAQFSTPSLP PSLKVGFLPP PGKEQSVSWV SLEEAEPIPG IHWGVRVLHP PPDQENVQYA
DLDFEAILLQ PSNPPDKTQV PMVVMPHGGP HSSFVTAWML FPAMLCKMGF AVLLVNYRGS
TGFGQDSILS LPGNVGHQDV KDVQFAVEQV LQEEHFDARR VALMGGSHGG FLSCHLIGQY
PETYSACIAR NPVINIASMM GSTDIPDWCM VETGFPYSNS CLPDLNVWEE MLDKSPIKYI
PQVKTPVLLM LGQEDRRVPF KQGMEYYRAL KARNVPVRLL LYPKSNHALS EVEAESDSFM
NAVLWLHTHL GS
