ACY3B_DANRE
ID ACY3B_DANRE Reviewed; 314 AA.
AC Q6DHQ3; A2BG59;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming) B;
DE EC=3.5.1.114;
DE AltName: Full=Aminoacylase-3.2;
DE Short=ACY-3.2;
DE AltName: Full=Aspartoacylase-2B;
GN Name=acy3.2; ORFNames=si:ch211-217k17.4, zgc:92178;
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 {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the AspA/AstE family. Aspartoacylase subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAM14061.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; BX323839; CAM14061.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BX323839; CAM14062.1; -; Genomic_DNA.
DR EMBL; BC075914; AAH75914.1; -; mRNA.
DR RefSeq; NP_001002347.1; NM_001002347.1.
DR RefSeq; XP_009292806.1; XM_009294531.2.
DR RefSeq; XP_017209311.1; XM_017353822.1.
DR AlphaFoldDB; Q6DHQ3; -.
DR SMR; Q6DHQ3; -.
DR PaxDb; Q6DHQ3; -.
DR Ensembl; ENSDART00000004233; ENSDARP00000023827; ENSDARG00000005525.
DR Ensembl; ENSDART00000122217; ENSDARP00000108439; ENSDARG00000005525.
DR GeneID; 436619; -.
DR KEGG; dre:436619; -.
DR CTD; 436619; -.
DR ZFIN; ZDB-GENE-040718-37; acy3.2.
DR eggNOG; ENOG502REAZ; Eukaryota.
DR GeneTree; ENSGT00390000001189; -.
DR HOGENOM; CLU_083292_0_0_1; -.
DR InParanoid; Q6DHQ3; -.
DR OMA; YPRDPTT; -.
DR OrthoDB; 1074294at2759; -.
DR PhylomeDB; Q6DHQ3; -.
DR TreeFam; TF328708; -.
DR PRO; PR:Q6DHQ3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 1.
DR Bgee; ENSDARG00000005525; Expressed in kidney and 32 other tissues.
DR ExpressionAtlas; Q6DHQ3; differential.
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..314
FT /note="N-acyl-aromatic-L-amino acid amidohydrolase
FT (carboxylate-forming) B"
FT /id="PRO_0000363364"
FT BINDING 19
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT BINDING 22
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT BINDING 63
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 70..71
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT BINDING 178
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 289
FT /ligand="substrate"
FT /evidence="ECO:0000255"
SQ SEQUENCE 314 AA; 35253 MW; 82CB40A0FC2F0CC1 CRC64;
MASVFLPALG GVAVCGGTHG NELSGVYLVQ EMERQRKEKG DGVWPIPVTT VLSNPRAVKE
CRRYIDTDMN RCFSRDTLST PITDSSPYEV RRAQELNNQL GPKESTGAID MICDLHNTTS
NMGLTLIHYT TSDWATLHIC KYLQTKITKV PVRVMVLDVP YSDAYSLESV SKHGFSIEVG
PQPHGVVRAD IYVIMKEAVD LTIDWIHKFN SGTVFEGGDV EAFKIIKSVD YPRDPVTRSL
NAAVHPQLQD RDFCLLKRGD PLFLSFSGET VKYEEEEPLH PLFINECAYY EKGIAFHLAK
RMRLTIPAVQ VQKD
