ACY3A_DANRE
ID ACY3A_DANRE Reviewed; 328 AA.
AC Q6DHI0; A2BG58;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming) A;
DE EC=3.5.1.114;
DE AltName: Full=Aminoacylase-3.1;
DE Short=ACY-3.1;
DE AltName: Full=Aspartoacylase-2A;
GN Name=acy3.1; ORFNames=si:ch211-217k17.2, zgc:92306;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays an important role in deacetylating mercapturic acids in
CC kidney proximal tubules. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acyl-aromatic L-alpha-amino acid + H2O = a carboxylate +
CC an aromatic L-alpha-amino acid; Xref=Rhea:RHEA:54184,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:29067, ChEBI:CHEBI:84824,
CC ChEBI:CHEBI:138093; EC=3.5.1.114;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acetyl-L-cysteine-S-conjugate + H2O = acetate + an S-
CC substituted L-cysteine; Xref=Rhea:RHEA:36855, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:58717, ChEBI:CHEBI:58718;
CC EC=3.5.1.114;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000305};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane; Peripheral membrane
CC protein. Cytoplasm.
CC -!- SIMILARITY: Belongs to the AspA/AstE family. Aspartoacylase subfamily.
CC {ECO:0000305}.
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DR EMBL; BX323839; CAM14060.1; -; Genomic_DNA.
DR EMBL; BC075994; AAH75994.1; -; mRNA.
DR RefSeq; NP_001138833.1; NM_001145361.1.
DR AlphaFoldDB; Q6DHI0; -.
DR SMR; Q6DHI0; -.
DR PaxDb; Q6DHI0; -.
DR Ensembl; ENSDART00000052907; ENSDARP00000052906; ENSDARG00000093003.
DR GeneID; 791456; -.
DR KEGG; dre:791456; -.
DR CTD; 791456; -.
DR ZFIN; ZDB-GENE-040718-345; acy3.1.
DR eggNOG; ENOG502REAZ; Eukaryota.
DR GeneTree; ENSGT00390000001189; -.
DR HOGENOM; CLU_083292_0_0_1; -.
DR InParanoid; Q6DHI0; -.
DR OMA; VIMHIYR; -.
DR OrthoDB; 1074294at2759; -.
DR PhylomeDB; Q6DHI0; -.
DR TreeFam; TF328708; -.
DR Reactome; R-DRE-5423646; Aflatoxin activation and detoxification.
DR PRO; PR:Q6DHI0; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 1.
DR Bgee; ENSDARG00000093003; Expressed in mature ovarian follicle and 20 other tissues.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004046; F:aminoacylase activity; IBA:GO_Central.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IBA:GO_Central.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR HAMAP; MF_00704; Aspartoacylase; 1.
DR InterPro; IPR016708; Aspartoacylase.
DR InterPro; IPR007036; Aste_AspA.
DR Pfam; PF04952; AstE_AspA; 1.
DR PIRSF; PIRSF018001; Aspartoacylase; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cytoplasm; Hydrolase; Membrane; Metal-binding;
KW Reference proteome; Zinc.
FT CHAIN 1..328
FT /note="N-acyl-aromatic-L-amino acid amidohydrolase
FT (carboxylate-forming) A"
FT /id="PRO_0000363363"
FT BINDING 30
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT BINDING 33
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT BINDING 74
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 81..82
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT BINDING 189
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 300
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT CONFLICT 50
FT /note="R -> K (in Ref. 2; AAH75994)"
FT /evidence="ECO:0000305"
FT CONFLICT 53
FT /note="G -> S (in Ref. 2; AAH75994)"
FT /evidence="ECO:0000305"
FT CONFLICT 233
FT /note="V -> A (in Ref. 2; AAH75994)"
FT /evidence="ECO:0000305"
FT CONFLICT 314
FT /note="T -> I (in Ref. 2; AAH75994)"
FT /evidence="ECO:0000305"
FT CONFLICT 323..325
FT /note="QTT -> HTK (in Ref. 2; AAH75994)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 328 AA; 36794 MW; 2CD6E0EDCADFD1A6 CRC64;
MTEEKAEEKN KMASVFLPAL GGVAVCGGTH GNELSGVYLV QEMERQRKER GDGVWPIPVT
TVLSNPRAVK ECRRYIDTDM NRCFSKAVLS TPITDSSPYE VRRAQELNNL LGVKGSDDVM
DMICDLHNTT SNMGLTLIHY SASDWVTLHI CKYLQTKITK VPVRVLVLDF PINDAYNLES
VSKHGFTLEV GPQPQGVVRA DIYVIMKEAV DLTIDWIHKF NSGTVFEGGD VEVFKFIKSV
DYPRDPETRN LTAAVHPQLQ DRDFCLLKRG DPLFLSFSGE TVTCEEEEPL HPFFINEGAY
YEKGIAFHLA KKWTLTVPSV QVQTTNSA
