HINT2_BOVIN
ID HINT2_BOVIN Reviewed; 163 AA.
AC Q8SQ21; Q24JY2;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Adenosine 5'-monophosphoramidase HINT2 {ECO:0000250|UniProtKB:Q9BX68};
DE EC=3.9.1.- {ECO:0000250|UniProtKB:Q9BX68};
DE AltName: Full=HINT-3 {ECO:0000250|UniProtKB:Q9BX68};
DE AltName: Full=Histidine triad nucleotide-binding protein 2, mitochondrial {ECO:0000250|UniProtKB:Q9BX68};
DE Short=HINT-2 {ECO:0000250|UniProtKB:Q9BX68};
DE Flags: Precursor;
GN Name=HINT2 {ECO:0000250|UniProtKB:Q9BX68};
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 Peng J., Chen H., Huang C.-H.;
RT "HINT-3 is a novel member of the histidine triad protein family.";
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) 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 adenosine 5'-O-p-
CC nitrophenylphosphoramidate (AMP-pNA) (By similarity). May be involved
CC in steroid biosynthesis (By similarity). May play a role in apoptosis
CC (By similarity). {ECO:0000250|UniProtKB:Q9BX68}.
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:Q9BX68};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9BX68}.
CC -!- SIMILARITY: Belongs to the HINT family. {ECO:0000305}.
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DR EMBL; AF366940; AAM00370.1; -; mRNA.
DR EMBL; BC114199; AAI14200.1; -; mRNA.
DR RefSeq; NP_776765.1; NM_174340.2.
DR AlphaFoldDB; Q8SQ21; -.
DR SMR; Q8SQ21; -.
DR STRING; 9913.ENSBTAP00000015208; -.
DR PaxDb; Q8SQ21; -.
DR PeptideAtlas; Q8SQ21; -.
DR PRIDE; Q8SQ21; -.
DR Ensembl; ENSBTAT00000015208; ENSBTAP00000015208; ENSBTAG00000011444.
DR GeneID; 281816; -.
DR KEGG; bta:281816; -.
DR CTD; 84681; -.
DR VEuPathDB; HostDB:ENSBTAG00000011444; -.
DR VGNC; VGNC:29855; HINT2.
DR eggNOG; KOG3275; Eukaryota.
DR GeneTree; ENSGT00940000157905; -.
DR HOGENOM; CLU_056776_8_0_1; -.
DR InParanoid; Q8SQ21; -.
DR OMA; SDCLFCK; -.
DR OrthoDB; 1190598at2759; -.
DR TreeFam; TF314862; -.
DR Proteomes; UP000009136; Chromosome 8.
DR Bgee; ENSBTAG00000011444; Expressed in thyroid gland and 105 other tissues.
DR ExpressionAtlas; Q8SQ21; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0043530; F:adenosine 5'-monophosphoramidase activity; ISS:UniProtKB.
DR GO; GO:0016787; F:hydrolase activity; IBA:GO_Central.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic process; IEA:Ensembl.
DR GO; GO:2000757; P:negative regulation of peptidyl-lysine acetylation; IEA:Ensembl.
DR GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.428.10; -; 1.
DR InterPro; IPR019808; Histidine_triad_CS.
DR InterPro; IPR001310; Histidine_triad_HIT.
DR InterPro; IPR011146; HIT-like.
DR InterPro; IPR036265; HIT-like_sf.
DR PANTHER; PTHR23089; PTHR23089; 1.
DR Pfam; PF01230; HIT; 1.
DR PRINTS; PR00332; HISTRIAD.
DR SUPFAM; SSF54197; SSF54197; 1.
DR PROSITE; PS00892; HIT_1; 1.
DR PROSITE; PS51084; HIT_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Apoptosis; Hydrolase; Lipid biosynthesis; Lipid metabolism;
KW Mitochondrion; Nucleotide-binding; Reference proteome;
KW Steroid biosynthesis; Transit peptide.
FT TRANSIT 1..17
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 18..163
FT /note="Adenosine 5'-monophosphoramidase HINT2"
FT /id="PRO_0000109785"
FT DOMAIN 55..163
FT /note="HIT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00464"
FT MOTIF 147..151
FT /note="Histidine triad motif"
FT ACT_SITE 149
FT /note="Tele-AMP-histidine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q9BX68"
FT BINDING 80
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q9BX68"
FT BINDING 136
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q9BX68"
FT BINDING 142..145
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q9BX68"
FT BINDING 149..151
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q9BX68"
FT MOD_RES 119
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9D0S9"
FT MOD_RES 139
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9D0S9"
SQ SEQUENCE 163 AA; 17147 MW; 2A7BFC6B1CB4D400 CRC64;
MAAAVVLAAG LCVARRAVAV AGPRGVQVRG AAGVTDGDEV AKAQQAAPGG AAPTIFSRIL
DRSLPADILY EDQQCLAFRD VAPQAPVHFL VIPKKPIPRI SQAEEEDQQL LGHLLLVAKE
TAKAEGLGDG YRLVINDGKL GAQSVYHLHI HVLGGRQLQW PPG
