HINT3_RAT
ID HINT3_RAT Reviewed; 175 AA.
AC Q8K3P7;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Adenosine 5'-monophosphoramidase HINT3 {ECO:0000250|UniProtKB:Q9NQE9};
DE EC=3.9.1.- {ECO:0000250|UniProtKB:Q9NQE9};
DE AltName: Full=HINT-4;
DE AltName: Full=Histidine triad nucleotide-binding protein 3;
DE Short=HINT-3;
GN Name=Hint3; Synonyms=Hint4;
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], AND TISSUE SPECIFICITY.
RX PubMed=15277470; DOI=10.1167/iovs.03-1391;
RA Farkas R.H., Qian J., Goldberg J.L., Quigley H.A., Zack D.J.;
RT "Gene expression profiling of purified rat retinal ganglion cells.";
RL Invest. Ophthalmol. Vis. Sci. 45:2503-2513(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 10-175.
RC STRAIN=Sprague-Dawley;
RA Huang C.-H., Chen H., Peng J., Chen Y.;
RT "Conservation of the fourth member of the histidine triad protein family
RT (Hint-4) in rat and mouse.";
RL Submitted (JUN-2001) 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 (By
CC similarity). Interacts with CALM1 (By similarity).
CC {ECO:0000250|UniProtKB:Q9CPS6, ECO:0000250|UniProtKB:Q9NQE9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NQE9}. Nucleus
CC {ECO:0000250|UniProtKB:Q9NQE9}.
CC -!- TISSUE SPECIFICITY: Expressed in retinal ganglion cells.
CC {ECO:0000269|PubMed:15277470}.
CC -!- SIMILARITY: Belongs to the HINT family. {ECO:0000305}.
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DR EMBL; CF977728; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AY040767; AAK94777.1; -; mRNA.
DR AlphaFoldDB; Q8K3P7; -.
DR SMR; Q8K3P7; -.
DR STRING; 10116.ENSRNOP00000019047; -.
DR SwissPalm; Q8K3P7; -.
DR PaxDb; Q8K3P7; -.
DR UCSC; RGD:621603; rat.
DR RGD; 621603; Hint3.
DR eggNOG; KOG4359; Eukaryota.
DR InParanoid; Q8K3P7; -.
DR PhylomeDB; Q8K3P7; -.
DR PRO; PR:Q8K3P7; -.
DR Proteomes; UP000002494; Unplaced.
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:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
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 Acetylation; Cytoplasm; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9NQE9"
FT CHAIN 2..175
FT /note="Adenosine 5'-monophosphoramidase HINT3"
FT /id="PRO_0000324329"
FT DOMAIN 33..144
FT /note="HIT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00464"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 136..140
FT /note="Histidine triad motif"
FT ACT_SITE 138
FT /note="Tele-AMP-histidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q9NQE9"
FT BINDING 69..70
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P49773"
FT BINDING 138..140
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P49773"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQE9"
FT CONFLICT 10
FT /note="G -> H (in Ref. 2; AAK94777)"
FT /evidence="ECO:0000305"
FT CONFLICT 12
FT /note="P -> A (in Ref. 2; AAK94777)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="G -> V (in Ref. 2; AAK94777)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 175 AA; 19694 MW; 7DADCC7E50D17E58 CRC64;
MAEKQAGLAG EPNPDCTVTA KAGPEVSSPG TSESRDYDSN CVFCRVAAGQ EPETELLYCE
NKDLVCFKDI KPAALHHYLV VPKKHIGSCK DLNKDHIEMV ESMVTVGKTI LERNNFTDFT
DVRMGFHVPP FCSVSHLHLH VIAPAKEFGF LSRVVYRRDS YWFITGDYLL EKLRK
