ID HINT3_BOVIN Reviewed; 182 AA.
AC Q2YDJ4; Q8MJJ8;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 27-MAR-2024, entry version 100.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Huang C.-H., Chen H., Peng J., Chen Y.;
RT "A novel member of the histidine triad protein family with differential
RT polyadenylation (Bovine HINT-4).";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) 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 -!- SIMILARITY: Belongs to the HINT family. {ECO:0000305}.
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DR EMBL; AF398236; AAM90584.1; -; mRNA.
DR EMBL; BC110193; AAI10194.1; -; mRNA.
DR RefSeq; NP_776766.1; NM_174341.2.
DR AlphaFoldDB; Q2YDJ4; -.
DR SMR; Q2YDJ4; -.
DR STRING; 9913.ENSBTAP00000002542; -.
DR PaxDb; 9913-ENSBTAP00000002542; -.
DR Ensembl; ENSBTAT00000002542.5; ENSBTAP00000002542.4; ENSBTAG00000001956.5.
DR GeneID; 281817; -.
DR KEGG; bta:281817; -.
DR CTD; 135114; -.
DR VEuPathDB; HostDB:ENSBTAG00000001956; -.
DR VGNC; VGNC:29856; HINT3.
DR eggNOG; KOG4359; Eukaryota.
DR GeneTree; ENSGT00510000047616; -.
DR HOGENOM; CLU_056776_4_2_1; -.
DR InParanoid; Q2YDJ4; -.
DR OMA; FCKIVNN; -.
DR TreeFam; TF353069; -.
DR Proteomes; UP000009136; Chromosome 9.
DR Bgee; ENSBTAG00000001956; Expressed in semen and 109 other cell types or 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 CDD; cd01278; aprataxin_related; 1.
DR Gene3D; 3.30.428.10; HIT-like; 1.
DR InterPro; IPR011146; HIT-like.
DR InterPro; IPR036265; HIT-like_sf.
DR PANTHER; PTHR12486:SF5; ADENOSINE 5'-MONOPHOSPHORAMIDASE HINT3; 1.
DR PANTHER; PTHR12486; APRATAXIN-RELATED; 1.
DR Pfam; PF11969; DcpS_C; 1.
DR SUPFAM; SSF54197; HIT-like; 1.
DR PROSITE; PS51084; HIT_2; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Hydrolase; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..182
FT /note="Adenosine 5'-monophosphoramidase HINT3"
FT /id="PRO_0000324326"
FT DOMAIN 49..158
FT /note="HIT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00464"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 143..147
FT /note="Histidine triad motif"
FT ACT_SITE 145
FT /note="Tele-AMP-histidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q9NQE9"
FT BINDING 76..77
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P49773"
FT BINDING 145..147
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P49773"
FT CONFLICT 164
FT /note="R -> K (in Ref. 1; AAM90584)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="F -> V (in Ref. 1; AAM90584)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 182 AA; 20470 MW; 39CA8A1A2C5C7CEF CRC64;
MMEEEECGLG KSCARSEPVA AAQPAGSPGE TPAVAAESPE LANYSSKCVF CRIAAHQDPG
TELLHCENED LVCFKDIKPA APHHYLVVPK KHFENCKYLK KDQIELIENM VTVGKAILER
NNFTDFENTR MGFHVSPFCS IAHLHLHVLA PADQLSFMSR LVYRVNSYWF ITADYLIEKL
RT
//
