HINT3_DANRE
ID HINT3_DANRE Reviewed; 160 AA.
AC Q5PNN8; Q0V966; Q1RMA9; Q5RGD5;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Adenosine 5'-monophosphoramidase HINT3 {ECO:0000250|UniProtKB:Q9NQE9};
DE EC=3.9.1.- {ECO:0000250|UniProtKB:Q9NQE9};
DE AltName: Full=Histidine triad nucleotide-binding protein 3;
DE Short=HINT-3;
GN Name=hint3; ORFNames=si:dkey-25e12.3;
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].
RC TISSUE=Intestine, and Olfactory epithelium;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Exhibits adenosine 5'-monophosphoramidase activity,
CC hydrolyzing purine nucleotide phosphoramidates with a single phosphate
CC group such as adenosine 5'monophosphoramidate (AMP-NH2) to yield AMP
CC and NH2 (By similarity). Hydrolyzes lysyl-AMP (AMP-N-epsilon-(N-alpha-
CC acetyl lysine methyl ester)) generated by lysine tRNA ligase (By
CC similarity). {ECO:0000250|UniProtKB:Q9NQE9}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine 5'-phosphoramidate + H2O = AMP + NH4(+);
CC Xref=Rhea:RHEA:67916, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:57890, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000250|UniProtKB:Q9NQE9};
CC -!- SUBUNIT: Forms dimers to octamers and even larger oligomer.
CC {ECO:0000250|UniProtKB:Q9NQE9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NQE9}. Nucleus
CC {ECO:0000250|UniProtKB:Q9NQE9}.
CC -!- SIMILARITY: Belongs to the HINT family. {ECO:0000305}.
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DR EMBL; BX537272; CAI29411.1; -; Genomic_DNA.
DR EMBL; BX927255; CAI11952.1; -; Genomic_DNA.
DR EMBL; BC115055; AAI15056.1; -; mRNA.
DR EMBL; BC121729; AAI21730.1; -; mRNA.
DR EMBL; BC133849; AAI33850.1; -; mRNA.
DR RefSeq; NP_001020726.2; NM_001025555.2.
DR AlphaFoldDB; Q5PNN8; -.
DR SMR; Q5PNN8; -.
DR STRING; 7955.ENSDARP00000072181; -.
DR PaxDb; Q5PNN8; -.
DR PRIDE; Q5PNN8; -.
DR Ensembl; ENSDART00000077715; ENSDARP00000072181; ENSDARG00000055365.
DR GeneID; 678527; -.
DR KEGG; dre:678527; -.
DR ZFIN; ZDB-GENE-041001-132; si:dkey-25e12.3.
DR eggNOG; KOG4359; Eukaryota.
DR GeneTree; ENSGT00510000047616; -.
DR HOGENOM; CLU_056776_4_2_1; -.
DR InParanoid; Q5PNN8; -.
DR OMA; SINFLPC; -.
DR OrthoDB; 1496385at2759; -.
DR PhylomeDB; Q5PNN8; -.
DR TreeFam; TF353069; -.
DR PRO; PR:Q5PNN8; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 20.
DR Bgee; ENSDARG00000055365; Expressed in granulocyte and 17 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0043530; F:adenosine 5'-monophosphoramidase activity; ISS:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.428.10; -; 1.
DR InterPro; IPR011146; HIT-like.
DR InterPro; IPR036265; HIT-like_sf.
DR SUPFAM; SSF54197; SSF54197; 1.
DR PROSITE; PS51084; HIT_2; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Hydrolase; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..160
FT /note="Adenosine 5'-monophosphoramidase HINT3"
FT /id="PRO_0000324331"
FT DOMAIN 24..132
FT /note="HIT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00464"
FT MOTIF 117..121
FT /note="Histidine triad motif"
FT ACT_SITE 119
FT /note="Tele-AMP-histidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q9NQE9"
FT BINDING 50..51
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P49773"
FT BINDING 119..121
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P49773"
FT CONFLICT 17
FT /note="E -> K (in Ref. 1; CAI11952 and 2; AAI15056)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="G -> A (in Ref. 2; AAI21730)"
FT /evidence="ECO:0000305"
FT CONFLICT 121
FT /note="H -> Y (in Ref. 2; AAI21730)"
FT /evidence="ECO:0000305"
FT CONFLICT 145
FT /note="E -> G (in Ref. 2; AAI15056)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="T -> A (in Ref. 2; AAI15056)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 160 AA; 18462 MW; 9054E54DF3D016EC CRC64;
MCDNSCFCEN KQDTIDESLD KTCIFCTIAK GDDRYTEILA EDEDFVCFRD INPGAPHHYL
VIPKKHIYSC LSLYADDISL VRGMAEMGRN VLKANNVTDL KDISLGFHVP PYITVPHLHL
HVLAPYSQLY KWAINKFRTN WYINEEKTVE ILMKGKTQMV
